https://www.cazypedia.org/api.php?action=feedcontributions&feedformat=atom&user=Harry+BrumerCAZypedia - User contributions [en-ca]2026-05-10T03:49:36ZUser contributionsMediaWiki 1.35.10https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_35&diff=19840Glycoside Hydrolase Family 352026-03-20T16:25:30Z<p>Harry Brumer: Added PMID for Boehr reference</p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]s: [[User:Anna Kulminskaya|Anna Kulminskaya]], [[User:Mirko Maksimainen|Mirko Maksimainen]], [[User:Juha Rouvinen|Juha Rouvinen]], [[User:Masahiro Nakajima|Masahiro Nakajima]]<br />
* [[Responsible Curator]]: [[User:Anna Kulminskaya|Anna Kulminskaya]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH35'''<br />
|-<br />
|'''Clan''' <br />
|GH-A<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH35.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
The majority of [[glycoside hydrolases]] of GH35 are β-galactosidases (EC [{{EClink}}3.2.1.23 3.2.1.23]). GH35 enzymes have been isolated from microorganisms such as fungi, bacteria and yeasts, as well as higher organisms such as plants, animals, and human cells. These β-galactosidases catalyse the hydrolysis of terminal non-reducing β-D-galactose residues in, for example, lactose (1,4-O-β-D-galactopyranosyl-D-glucose), oligosaccharides, glycolipids, and glycoproteins. Various GH35 β-galactosidases demonstrate specificity towards β-1,3-, β-1,6- or β-1,4-galactosidic linkages <cite>Zinin2002, Gamauf2007, Tanthanuch2008</cite>, and are often most active under acidic conditions <cite>Zhang1994, vanCasteren2000, Wang2009</cite>. As with many other CAZy families <cite>GeislerLee2006, Henrissat2001, Tuskan2006</cite>, GH35 members tend to be represented by multi-gene families in plants <cite>Ahn2007, Smith2000, Lazan2004, Ross1994, Tanthanuch2008</cite>. Moreover, plant GH35 β-galactosidases have be divided into two classes: members of the first are capable of hydrolyzing pectic β-1,4-galactans, while those of the second can specifically cleave β-1,3- and β-1,6-galactosyl linkages of arabinogalactan proteins <cite>Kotake2005</cite>. In 2025, a β-galactosidase acting specifically on β-1,2-galactooligosaccharides (EC [{{EClink}}3.2.1.230 3.2.1.230]) was reported <cite>Nakazawa2025</cite>.<br />
<br />
In addition to β-galactosidases, GH35 also contains a limited number of archeal [[exo]]-β-glucosaminidases (EC [{{EClink}}3.2.1.165 3.2.1.165]) <cite>Tanaka2003 Liu2006</cite> and β-1,2-glucosyltransferase (EC [{{EClink}}2.4.1.391 2.4.1.391]) <cite>Kobayashi2022</cite>. The former enzymes hydrolyze chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from non-reducing termini. The latter enzyme disproportionates β-1,2-glucooligosaccharides by transferring glucose units but prefers sophorose (Glc-β-1,2-Glc) as a donor and alkyl- or acyl-glucosides as acceptors, regardless of their anomeric configuration.<br />
<br />
== Kinetics and Mechanism ==<br />
Beta-galactosidases of GH35 catalyze the hydrolysis of terminal β-galactosyl residues via a [[classical Koshland retaining mechanism]], which leads to net retention of the β-anomeric configuration of the released galactose molecule. The stereochemistry of the reaction was first shown by NMR for the human β-galactosidase precursor <cite>Zhang1994</cite> and has been subsequently confirmed by other investigators for microbial and plant enzymes <cite>vanCasteren2000, Zinin2002</cite> .<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues for family 35 were first predicted on the basis of hydrophobic cluster analysis of proteins of similar protein fold <cite>Henrissat1995</cite>. Experimentally, the glutamic acid residue 268 was first identified as the [[catalytic nucleophile]] in human lysosomal β-galactosidase precursor using a slow substrate, 2,4-dinitrophenyl 2-deoxy-2-fluoro-β-D-galactopyranoside, which allowed trapping of a covalent glycosyl-enzyme intermediate and subsequent peptide mapping <cite>McCarter1997</cite>. This approach was repeated for two bacterial β-galactosidases from ''Xanthomonas manihotis'' and ''Bacillus circulans'' <cite>Blanchard2001</cite>. The [[general acid/base]] residue was inferred to be Glu200 from structural studies of a ''Penicillium'' sp. β-galactosidase <cite>Rojas2004</cite>. Recent structural studies (''vide infra'') revealed two different conformations of the [[general acid/base]] residue in the β-galactosidase of ''Trichoderma reesei'' <cite> Maksimainen2010</cite>.<br />
<br />
== Three-dimensional structures ==<br />
The first 3D-structures of a GH35 enzyme, those of a β-galactosidase from ''Pencillium'' sp. (Psp-β-gal) in native (PDB [{{PDBlink}}1tg7 1tg7]) and product-complexed (PDB [{{PDBlink}}1xc6 1xc6]) forms, were reported in 2004 at 1.90 Å and 2.10 Å resolution, respectively <cite>Rojas2004</cite>. The structure of a β-galactosidase from ''Bacteriodes thetaiotamicron'' (Btm-β-gal) was subsequently reported by the New York Structural GenomiX Research Consortium in 2008 at 2.15 Å resolution (PDB [{{PDBlink}}3d3a 3d3a]). In 2010, an atomic (1.2 Å) resolution crystal structure of a ''Trichoderma reesei'' (''Hypocrea jecorina'') β-galactosidase (Tr-β-gal, PDB [{{PDBlink}}3og2 3og2]) was reported, together with complex structures with galactose, IPTG and PETG at 1.5, 1.75 and 1.4 Å resolutions, respectively (PDB codes [{{PDBlink}}3ogr 3ogr], [{{PDBlink}}3ogs 3ogs], and [{{PDBlink}}3ogv 3ogv], respectively) <cite>Maksimainen2010</cite>.<br />
<br />
GH35 enzymes belong to Clan GH-A, and thus have an (α/β)<sub>8</sub> (TIM) barrel as the catalytic domain, in which two glutamic acid residues act as the general acid-base and nucleophilic catalysts. These residues are located in strands 4 and 7 of the barrel.<br />
<br />
The comparison of the native structures of Psp-β-gal, Tr-β-gal and Btmβ-gal reveals two things ('''Figure 1'''): Firstly, Btm-β-gal consists of three distinct domains, whereas Psp-β-gal and Tr-β-gal consist of five and six domains, respectively. The second and third domains of Btm-β-gal are quite similar with the fourth and fifth domains of Psp-β-gal, and with the fifth and sixth domains of Tr-β-gal. Secondly, major structural differences between Psp-β-gal and Tr-β-gal are in the conformations of the loop regions. Although the crystal structures of Psp-β-gal and Tr-β-gal are similar, the interpretation of the structure of Tr-β-gal is somewhat different from that presented earlier for Psp-β-gal: Rojas et al. considered Psp-β-gal to be composed of five distinct structural domains. The overall structure is built around the first, TIM barrel, domain. Domain 2 is an all β-sheet domain containing an immunoglobulin-like subdomain, Domain 3 is based on a Greek-key β-sandwich, and Domains 4 and 5 are jelly rolls <cite>Rojas2004</cite>. In contrast, Maksimainen et al. concluded the domain 2 includes two different domains and thus the Tr-β-gal and Psp-β-gal structures both form six similar domains <cite>Maksimainen2010</cite>.<br />
<br />
The superimposition of the active sites of the GH35 β-galactosidases shows a remarkable similarity. In addition to the catalytic residues, the active sites of the GH35 β-galactosidases contain many identical residues ('''Figure 1B'''). Based on the galactose-bound crystallographic models of Psp-β-gal and Tr-β-gal, a single galactose molecule is bound to the active site of the GH35 enzyme in the chair conformation in the β-anomeric configuration.<br />
<br />
Additionally, Maksimainen et al. have described conformational changes in two loop regions of the active site of Tr-β-gal, that implicates a conformational selection mechanism for the enzyme (Figure 2). Unlike the induced fit theory, which assumes that the initial interaction between a protein and its binding partner induces a conformational change in the protein through a stepwise process, the conformational selection theory is based on the assumption that the unbound protein exists as an ensemble of conformations in dynamic equilibrium. Interaction between a weakly populated, higher-energy conformation and a binding partner causes the equilibrium to move in favor of the selected conformation <cite>Tsai1999, Boehr2008</cite>. This can be seen in the structures of Tr-β-gal: the open and closed conformation are both favorable in the native structure and the closed conformation becomes more favorable in the complex structures. Furthermore, The acid/base catalyst Glu200 has two different conformations in the IPTG and PETG complex structures that clearly affects the p''K''<sub>a</sub> value of this residue and thus the catalytic mechanism of the enzyme <cite>Maksimainen2010</cite>.<br />
<br />
=== Structure images ===<br />
<br />
[[Image: GH35 comparison.png|thumb|left|750px|'''Figure 1. Comparison of the native structures of GH35 β-galactosidases.''' A. Global structures, B. Active sites. Psp-β-gal (PDB code [{{PDBlink}}1tg7 1tg7]), Tr-β-gal (PDB code [{{PDBlink}}3og2 3og2]) and Btm-β-gal (PDB code [{{PDBlink}}3d3a 3d3a]) are colored in green, brown and blue, respectively.]]<br />
<br />
[[Image: Conformational selection.png|thumb|left|750px| '''Figure 2. Illustration of the conformational selection mechanism observed in Tr-β-gal <cite>Maksimainen2010</cite>.''']]<br />
<br />
<br style="clear: both" /><br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: <br />
[[Retaining]] stereochemical outcome for human β-galactosidase precursor by NMR <cite>Zhang1994</cite><br />
<br />
;First [[catalytic nucleophile]] identification: <br />
Human β-galactosidase precursor by 2-fluorogalactose labeling <cite>McCarter1997</cite>.<br />
<br />
;First [[general acid/base]] residue identification: <br />
''Penicillium sp.'' β-galactosidase by structural identification <cite>Rojas2004</cite>.<br />
<br />
;First 3-D structure: <br />
''Penicillium sp.'' β-galactosidase <cite>Rojas2004</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Ahn2007 pmid=17466346<br />
#Smith2000 pmid=10889266<br />
#Lazan2004 pmid=15694277<br />
#Ross1994 pmid=7991682<br />
#Tanthanuch2008 pmid=18664295<br />
#Tanka2003 pmid=12923090<br />
#Liu2006 pmid=16912928<br />
#Zhang1994 pmid=7998946<br />
#Henrissat1995 pmid=7624375<br />
#McCarter1997 pmid=8995274<br />
#Rojas2004 pmid=15491613<br />
#Blanchard2001 pmid=11423106<br />
#Maksimainen2010 pmid=21130883<br />
#GeislerLee2006 pmid=16415215<br />
#Henrissat2001 pmid=11554480<br />
#Tuskan2006 pmid=16973872<br />
#Gamauf2007 pmid=17381511<br />
#Zinin2002 pmid=11909597<br />
#vanCasteren2000 pmid=11086688<br />
#Wang2009 pmid=19453169<br />
#Kotake2005 pmid=15980190<br />
#Boehr2008 pmid=18556537<br />
#Tsai1999 pmid=10468538<br />
#Nakazawa2025 pmid=39820076<br />
#Kobayashi2022 pmid=35065074<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH035]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_35&diff=19839Glycoside Hydrolase Family 352026-03-20T16:22:14Z<p>Harry Brumer: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]s: [[User:Anna Kulminskaya|Anna Kulminskaya]], [[User:Mirko Maksimainen|Mirko Maksimainen]], [[User:Juha Rouvinen|Juha Rouvinen]], [[User:Masahiro Nakajima|Masahiro Nakajima]]<br />
* [[Responsible Curator]]: [[User:Anna Kulminskaya|Anna Kulminskaya]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH35'''<br />
|-<br />
|'''Clan''' <br />
|GH-A<br />
|-<br />
|'''Mechanism'''<br />
|retaining<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH35.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
The majority of [[glycoside hydrolases]] of GH35 are β-galactosidases (EC [{{EClink}}3.2.1.23 3.2.1.23]). GH35 enzymes have been isolated from microorganisms such as fungi, bacteria and yeasts, as well as higher organisms such as plants, animals, and human cells. These β-galactosidases catalyse the hydrolysis of terminal non-reducing β-D-galactose residues in, for example, lactose (1,4-O-β-D-galactopyranosyl-D-glucose), oligosaccharides, glycolipids, and glycoproteins. Various GH35 β-galactosidases demonstrate specificity towards β-1,3-, β-1,6- or β-1,4-galactosidic linkages <cite>Zinin2002, Gamauf2007, Tanthanuch2008</cite>, and are often most active under acidic conditions <cite>Zhang1994, vanCasteren2000, Wang2009</cite>. As with many other CAZy families <cite>GeislerLee2006, Henrissat2001, Tuskan2006</cite>, GH35 members tend to be represented by multi-gene families in plants <cite>Ahn2007, Smith2000, Lazan2004, Ross1994, Tanthanuch2008</cite>. Moreover, plant GH35 β-galactosidases have be divided into two classes: members of the first are capable of hydrolyzing pectic β-1,4-galactans, while those of the second can specifically cleave β-1,3- and β-1,6-galactosyl linkages of arabinogalactan proteins <cite>Kotake2005</cite>. In 2025, a β-galactosidase acting specifically on β-1,2-galactooligosaccharides (EC [{{EClink}}3.2.1.230 3.2.1.230]) was reported <cite>Nakazawa2025</cite>.<br />
<br />
In addition to β-galactosidases, GH35 also contains a limited number of archeal [[exo]]-β-glucosaminidases (EC [{{EClink}}3.2.1.165 3.2.1.165]) <cite>Tanaka2003 Liu2006</cite> and β-1,2-glucosyltransferase (EC [{{EClink}}2.4.1.391 2.4.1.391]) <cite>Kobayashi2022</cite>. The former enzymes hydrolyze chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from non-reducing termini. The latter enzyme disproportionates β-1,2-glucooligosaccharides by transferring glucose units but prefers sophorose (Glc-β-1,2-Glc) as a donor and alkyl- or acyl-glucosides as acceptors, regardless of their anomeric configuration.<br />
<br />
== Kinetics and Mechanism ==<br />
Beta-galactosidases of GH35 catalyze the hydrolysis of terminal β-galactosyl residues via a [[classical Koshland retaining mechanism]], which leads to net retention of the β-anomeric configuration of the released galactose molecule. The stereochemistry of the reaction was first shown by NMR for the human β-galactosidase precursor <cite>Zhang1994</cite> and has been subsequently confirmed by other investigators for microbial and plant enzymes <cite>vanCasteren2000, Zinin2002</cite> .<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues for family 35 were first predicted on the basis of hydrophobic cluster analysis of proteins of similar protein fold <cite>Henrissat1995</cite>. Experimentally, the glutamic acid residue 268 was first identified as the [[catalytic nucleophile]] in human lysosomal β-galactosidase precursor using a slow substrate, 2,4-dinitrophenyl 2-deoxy-2-fluoro-β-D-galactopyranoside, which allowed trapping of a covalent glycosyl-enzyme intermediate and subsequent peptide mapping <cite>McCarter1997</cite>. This approach was repeated for two bacterial β-galactosidases from ''Xanthomonas manihotis'' and ''Bacillus circulans'' <cite>Blanchard2001</cite>. The [[general acid/base]] residue was inferred to be Glu200 from structural studies of a ''Penicillium'' sp. β-galactosidase <cite>Rojas2004</cite>. Recent structural studies (''vide infra'') revealed two different conformations of the [[general acid/base]] residue in the β-galactosidase of ''Trichoderma reesei'' <cite> Maksimainen2010</cite>.<br />
<br />
== Three-dimensional structures ==<br />
The first 3D-structures of a GH35 enzyme, those of a β-galactosidase from ''Pencillium'' sp. (Psp-β-gal) in native (PDB [{{PDBlink}}1tg7 1tg7]) and product-complexed (PDB [{{PDBlink}}1xc6 1xc6]) forms, were reported in 2004 at 1.90 Å and 2.10 Å resolution, respectively <cite>Rojas2004</cite>. The structure of a β-galactosidase from ''Bacteriodes thetaiotamicron'' (Btm-β-gal) was subsequently reported by the New York Structural GenomiX Research Consortium in 2008 at 2.15 Å resolution (PDB [{{PDBlink}}3d3a 3d3a]). In 2010, an atomic (1.2 Å) resolution crystal structure of a ''Trichoderma reesei'' (''Hypocrea jecorina'') β-galactosidase (Tr-β-gal, PDB [{{PDBlink}}3og2 3og2]) was reported, together with complex structures with galactose, IPTG and PETG at 1.5, 1.75 and 1.4 Å resolutions, respectively (PDB codes [{{PDBlink}}3ogr 3ogr], [{{PDBlink}}3ogs 3ogs], and [{{PDBlink}}3ogv 3ogv], respectively) <cite>Maksimainen2010</cite>.<br />
<br />
GH35 enzymes belong to Clan GH-A, and thus have an (α/β)<sub>8</sub> (TIM) barrel as the catalytic domain, in which two glutamic acid residues act as the general acid-base and nucleophilic catalysts. These residues are located in strands 4 and 7 of the barrel.<br />
<br />
The comparison of the native structures of Psp-β-gal, Tr-β-gal and Btmβ-gal reveals two things ('''Figure 1'''): Firstly, Btm-β-gal consists of three distinct domains, whereas Psp-β-gal and Tr-β-gal consist of five and six domains, respectively. The second and third domains of Btm-β-gal are quite similar with the fourth and fifth domains of Psp-β-gal, and with the fifth and sixth domains of Tr-β-gal. Secondly, major structural differences between Psp-β-gal and Tr-β-gal are in the conformations of the loop regions. Although the crystal structures of Psp-β-gal and Tr-β-gal are similar, the interpretation of the structure of Tr-β-gal is somewhat different from that presented earlier for Psp-β-gal: Rojas et al. considered Psp-β-gal to be composed of five distinct structural domains. The overall structure is built around the first, TIM barrel, domain. Domain 2 is an all β-sheet domain containing an immunoglobulin-like subdomain, Domain 3 is based on a Greek-key β-sandwich, and Domains 4 and 5 are jelly rolls <cite>Rojas2004</cite>. In contrast, Maksimainen et al. concluded the domain 2 includes two different domains and thus the Tr-β-gal and Psp-β-gal structures both form six similar domains <cite>Maksimainen2010</cite>.<br />
<br />
The superimposition of the active sites of the GH35 β-galactosidases shows a remarkable similarity. In addition to the catalytic residues, the active sites of the GH35 β-galactosidases contain many identical residues ('''Figure 1B'''). Based on the galactose-bound crystallographic models of Psp-β-gal and Tr-β-gal, a single galactose molecule is bound to the active site of the GH35 enzyme in the chair conformation in the β-anomeric configuration.<br />
<br />
Additionally, Maksimainen et al. have described conformational changes in two loop regions of the active site of Tr-β-gal, that implicates a conformational selection mechanism for the enzyme (Figure 2). Unlike the induced fit theory, which assumes that the initial interaction between a protein and its binding partner induces a conformational change in the protein through a stepwise process, the conformational selection theory is based on the assumption that the unbound protein exists as an ensemble of conformations in dynamic equilibrium. Interaction between a weakly populated, higher-energy conformation and a binding partner causes the equilibrium to move in favor of the selected conformation <cite>Tsai1999, Boehr2008</cite>. This can be seen in the structures of Tr-β-gal: the open and closed conformation are both favorable in the native structure and the closed conformation becomes more favorable in the complex structures. Furthermore, The acid/base catalyst Glu200 has two different conformations in the IPTG and PETG complex structures that clearly affects the p''K''<sub>a</sub> value of this residue and thus the catalytic mechanism of the enzyme <cite>Maksimainen2010</cite>.<br />
<br />
=== Structure images ===<br />
<br />
[[Image: GH35 comparison.png|thumb|left|750px|'''Figure 1. Comparison of the native structures of GH35 β-galactosidases.''' A. Global structures, B. Active sites. Psp-β-gal (PDB code [{{PDBlink}}1tg7 1tg7]), Tr-β-gal (PDB code [{{PDBlink}}3og2 3og2]) and Btm-β-gal (PDB code [{{PDBlink}}3d3a 3d3a]) are colored in green, brown and blue, respectively.]]<br />
<br />
[[Image: Conformational selection.png|thumb|left|750px| '''Figure 2. Illustration of the conformational selection mechanism observed in Tr-β-gal <cite>Maksimainen2010</cite>.''']]<br />
<br />
<br style="clear: both" /><br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: <br />
[[Retaining]] stereochemical outcome for human β-galactosidase precursor by NMR <cite>Zhang1994</cite><br />
<br />
;First [[catalytic nucleophile]] identification: <br />
Human β-galactosidase precursor by 2-fluorogalactose labeling <cite>McCarter1997</cite>.<br />
<br />
;First [[general acid/base]] residue identification: <br />
''Penicillium sp.'' β-galactosidase by structural identification <cite>Rojas2004</cite>.<br />
<br />
;First 3-D structure: <br />
''Penicillium sp.'' β-galactosidase <cite>Rojas2004</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Ahn2007 pmid=17466346<br />
#Smith2000 pmid=10889266<br />
#Lazan2004 pmid=15694277<br />
#Ross1994 pmid=7991682<br />
#Tanthanuch2008 pmid=18664295<br />
#Tanka2003 pmid=12923090<br />
#Liu2006 pmid=16912928<br />
#Zhang1994 pmid=7998946<br />
#Henrissat1995 pmid=7624375<br />
#McCarter1997 pmid=8995274<br />
#Rojas2004 pmid=15491613<br />
#Blanchard2001 pmid=11423106<br />
#Maksimainen2010 pmid=21130883<br />
#GeislerLee2006 pmid=16415215<br />
#Henrissat2001 pmid=11554480<br />
#Tuskan2006 pmid=16973872<br />
#Gamauf2007 pmid=17381511<br />
#Zinin2002 pmid=11909597<br />
#vanCasteren2000 pmid=11086688<br />
#Wang2009 pmid=19453169<br />
#Kotake2005 pmid=15980190<br />
#Boehr2008 Boehr DD, Wright PE ''How do proteins interact?'' Science 2008, 320 1429-1430. <br />
#Tsai1999 pmid=10468538<br />
#Nakazawa2025 pmid=39820076<br />
#Kobayashi2022 pmid=35065074<br />
</biblio><br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH035]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=User:Masahiro_Nakajima&diff=19837User:Masahiro Nakajima2026-03-18T15:49:00Z<p>Harry Brumer: fixed errors introduced in EC links in previous edit</p>
<hr />
<div>[[Image:Candidate2png.png|200px|right]]<br />
<br />
[https://www.rs.tus.ac.jp/m-nakajima/index.html Masahiro Nakajima] received his Ph.D. from the Graduate School of Agricultural and Life Science, The University of Tokyo in 2006. He joined the group of Dr. [[User:Motomitsu Kitaoka|Motomitsu Kitaoka]] as a postdoctoral fellow (2006–2010). He moved to Iwate Biotechnology Research Center as a researcher (2010–2012). He was an assistant professor in Taguchi Laboratory (2012–2020) and is currently an associate professor in his own laboratory (2020-) at Department of Applied Biological Science, Tokyo University of Science. His research currently focuses on structures and functions of carbohydrate-active enzymes acting on unique sugar chains such as β-1,2-glucan. He acts as a Responsible Curator of Glycoside Hydrolase Families '''[[GH144]]''', '''[[GH162]]''', '''[[GH186]]''', '''[[GH189]]''', '''[[GH192]]''', '''[[GH193]]''' and '''[[GH194]]''', and also created '''clan GH-S'''. He determined the functions and/or crystal structures of <br />
<br />
* [[GH1]] β-Glucosidase <cite>Nakajima2025b</cite><br />
* [[GH3]] β-Glucosidases <cite>Nakajima2012a Nakajima2016 Ishiguro2017</cite><br />
* [[GH16]] β-1,3-Glucanase <cite>Nakajima2012b</cite><br />
* [[GH35]] β-1,2-Glucosyltransglycosylase <cite>Kobayashi2022</cite> ('''[{{EClink}}2.4.1.391 2.4.1.391 new EC number]''') and β-1,2-galactosidase <cite>Nakazawa2025</cite> ('''[{{EClink}}3.2.1.230 3.2.1.230 new EC number]''')<br />
* [[GH38]] α-Mannosidase <cite>Nakajima2003</cite><br />
* [[GH57]] 4-α-Glucanotransferase <cite>Nakajima2004</cite><br />
* [[GH94]] 1,2-β-Oligoglucan phosphorylases <cite>Nakajima2017 Nakajima2014</cite> ('''[{{EClink}}2.4.1.333 2.4.1.333 new EC number]''')<br />
* [[GH112]] D-Galactosyl-β-1,4-L-rhamnose phosphorylase <cite>Nakajima2009a</cite> ('''[{{EClink}}2.4.1.247 2.4.1.247 new EC number]''') and β-1,3-galactosyl-''N''-acetylhexosamine phosphorylases <cite>Nakajima2009a Nakajima2009b Nakajima2008a Nakajima2008b</cite><br />
* [[GH144]] Bacterial β-1,2-glucanases <cite>Abe2017</cite> ('''family created''') and sophorosylhydrolase <cite>Shimizu2018</cite> ('''[{{EClink}}3.2.1.214 3.2.1.214 new EC number]''')<br />
* [[GH162]] Fungal β-1,2-glucanase <cite>Tanaka2019</cite> ('''family created''') ('''clan GH-S created''')<br />
* [[GH186]] ''E. coli'' β-1,2-glucanase <cite>Motouchi2023</cite> ('''family created''') and α-1,6-cyclized β-1,2-glucohexadecaose synthase from ''Xanthomonas campestris'' pv. ''campestris'' (new EC number enzyme)<cite>Motouchi2024</cite><br />
* [[GH189]] Cyclic β-1,2-glucan synthase ([[Transglycosylases|transglycosylase]] domain) <cite>Tanaka2024</cite> ('''family created''') ('''[{{EClink}}2.4.1.397 2.4.1.397 new EC number]''')<br />
* [[GH192]] Bacterial β-1,2-glucanase <cite>Nakajima2025a</cite> ('''family created''')<br />
* [[GH193]] Bacterial β-1,2-glucanase <cite>Nakajima2025a</cite> ('''family created''')<br />
* [[GH194]] Bacterial β-1,2-glucanase <cite>Nakajima2025a</cite> ('''family created''')<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Nakajima2012a pmid=21850431<br />
#Nakajima2016 pmid=26886583<br />
#Ishiguro2017 pmid=29131329<br />
<br />
#Nakajima2012b pmid=22685137<br />
#Nakajima2003 pmid=12801516<br />
#Nakajima2004 pmid=15564678<br />
<br />
#Nakajima2017 pmid=28198470<br />
#Nakajima2014 pmid=24647662<br />
<br />
#Nakajima2009a pmid=19491100<br />
#Nakajima2009b pmid=19132369<br />
#Nakajima2008a pmid=18723650<br />
#Nakajima2008b pmid=18183385<br />
<br />
#Abe2017 pmid=28270506<br />
#Shimizu2018 pmid=29763309<br />
#Tanaka2019 pmid=30926603<br />
#Kobayashi2022 pmid=35065074<br />
#Motouchi2023 pmid=37735577<br />
#Motouchi2024 pmid=38957137<br />
#Tanaka2024 pmid=38300345<br />
#Nakazawa2025 pmid=39820076<br />
#Nakajima2025a pmid=40411428<br />
#Nakajima2025b pmid=40838837<br />
<br />
<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Nakajima,Masahiro]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=User:Masahiro_Nakajima&diff=19836User:Masahiro Nakajima2026-03-18T15:46:42Z<p>Harry Brumer: Revised to use EClink template</p>
<hr />
<div>[[Image:Candidate2png.png|200px|right]]<br />
<br />
[https://www.rs.tus.ac.jp/m-nakajima/index.html Masahiro Nakajima] received his Ph.D. from the Graduate School of Agricultural and Life Science, The University of Tokyo in 2006. He joined the group of Dr. [[User:Motomitsu Kitaoka|Motomitsu Kitaoka]] as a postdoctoral fellow (2006–2010). He moved to Iwate Biotechnology Research Center as a researcher (2010–2012). He was an assistant professor in Taguchi Laboratory (2012–2020) and is currently an associate professor in his own laboratory (2020-) at Department of Applied Biological Science, Tokyo University of Science. His research currently focuses on structures and functions of carbohydrate-active enzymes acting on unique sugar chains such as β-1,2-glucan. He acts as a Responsible Curator of Glycoside Hydrolase Families '''[[GH144]]''', '''[[GH162]]''', '''[[GH186]]''', '''[[GH189]]''', '''[[GH192]]''', '''[[GH193]]''' and '''[[GH194]]''', and also created '''clan GH-S'''. He determined the functions and/or crystal structures of <br />
<br />
* [[GH1]] β-Glucosidase <cite>Nakajima2025b</cite><br />
* [[GH3]] β-Glucosidases <cite>Nakajima2012a Nakajima2016 Ishiguro2017</cite><br />
* [[GH16]] β-1,3-Glucanase <cite>Nakajima2012b</cite><br />
* [[GH35]] β-1,2-Glucosyltransglycosylase <cite>Kobayashi2022</cite> ('''[{{EClink}}2.4.1.391 new EC number]''') and β-1,2-galactosidase <cite>Nakazawa2025</cite> ('''[{{EClink}}3.2.1.230 new EC number]''')<br />
* [[GH38]] α-Mannosidase <cite>Nakajima2003</cite><br />
* [[GH57]] 4-α-Glucanotransferase <cite>Nakajima2004</cite><br />
* [[GH94]] 1,2-β-Oligoglucan phosphorylases <cite>Nakajima2017 Nakajima2014</cite> ('''[{{EClink}}2.4.1.333 new EC number]''')<br />
* [[GH112]] D-Galactosyl-β-1,4-L-rhamnose phosphorylase <cite>Nakajima2009a</cite> ('''[{{EClink}}2.4.1.247 new EC number]''') and β-1,3-galactosyl-''N''-acetylhexosamine phosphorylases <cite>Nakajima2009a Nakajima2009b Nakajima2008a Nakajima2008b</cite><br />
* [[GH144]] Bacterial β-1,2-glucanases <cite>Abe2017</cite> ('''family created''') and sophorosylhydrolase <cite>Shimizu2018</cite> ('''{{EClink}}3.2.1.214 new EC number]''')<br />
* [[GH162]] Fungal β-1,2-glucanase <cite>Tanaka2019</cite> ('''family created''') ('''clan GH-S created''')<br />
* [[GH186]] ''E. coli'' β-1,2-glucanase <cite>Motouchi2023</cite> ('''family created''') and α-1,6-cyclized β-1,2-glucohexadecaose synthase from ''Xanthomonas campestris'' pv. ''campestris'' (new EC number enzyme)<cite>Motouchi2024</cite><br />
* [[GH189]] Cyclic β-1,2-glucan synthase ([[Transglycosylases|transglycosylase]] domain) <cite>Tanaka2024</cite> ('''family created''') ('''[{{EClink}}2.4.1.397 new EC number]''')<br />
* [[GH192]] Bacterial β-1,2-glucanase <cite>Nakajima2025a</cite> ('''family created''')<br />
* [[GH193]] Bacterial β-1,2-glucanase <cite>Nakajima2025a</cite> ('''family created''')<br />
* [[GH194]] Bacterial β-1,2-glucanase <cite>Nakajima2025a</cite> ('''family created''')<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Nakajima2012a pmid=21850431<br />
#Nakajima2016 pmid=26886583<br />
#Ishiguro2017 pmid=29131329<br />
<br />
#Nakajima2012b pmid=22685137<br />
#Nakajima2003 pmid=12801516<br />
#Nakajima2004 pmid=15564678<br />
<br />
#Nakajima2017 pmid=28198470<br />
#Nakajima2014 pmid=24647662<br />
<br />
#Nakajima2009a pmid=19491100<br />
#Nakajima2009b pmid=19132369<br />
#Nakajima2008a pmid=18723650<br />
#Nakajima2008b pmid=18183385<br />
<br />
#Abe2017 pmid=28270506<br />
#Shimizu2018 pmid=29763309<br />
#Tanaka2019 pmid=30926603<br />
#Kobayashi2022 pmid=35065074<br />
#Motouchi2023 pmid=37735577<br />
#Motouchi2024 pmid=38957137<br />
#Tanaka2024 pmid=38300345<br />
#Nakazawa2025 pmid=39820076<br />
#Nakajima2025a pmid=40411428<br />
#Nakajima2025b pmid=40838837<br />
<br />
<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Nakajima,Masahiro]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Template:News&diff=19835Template:News2026-03-18T15:44:36Z<p>Harry Brumer: </p>
<hr />
<div>'''13 March 2026:''' ''Three more on beta-one-two!'' '''[[User:Masahiro Nakajima|Masahiro Nakajima]]''' completed and [[Curator Approved]] no less than three new pages on beta(1-2)-glucanases today. First reported by [[User:Masahiro Nakajima|Masahiro Nakajima]] and co-workers in a single publication in 2025, '''[[Glycoside Hydrolase Family 192]]''', '''[[Glycoside Hydrolase Family 193]]''', and '''[[Glycoside Hydrolase Family 194]]''' further expand our understanding of beta(1-2)-glucan metabolism in bacteria. [[User:Masahiro Nakajima|Masahiro Nakajima]] has truly been instrumental in revealing new beta(1-2)-glucan-active [[GH|hydrolases]] and [[transglycosylases]], leading to the establishment of several new families in CAZy, so ''make sure to check-out his work on '''[[GH192]]''', '''[[GH193]]''', and '''[[GH194]]''', as well as '''[[GH144]]''', '''[[GH162]]''', '''[[GH186]]''', and '''[[GH189]]'''!''<br />
----<br />
<br />
'''23 January 2026:''' ''An oldie, but a goodie:'' As our first page of the new year, the '''[[Glycoside Hydrolase Family 71]]''' page, written by '''[[User:Antonielle Vieira Monclaro|Antonielle Vieira Monclaro]]''', was [[Curator Approved]] by '''[[User:Johan Larsbrink|Johan Larsbrink]]''' today. '''[[GH71]]''' is a family of mostly fungal alpha-1,3-glucanases that was established and subjected to mechanistic characterization in the early 2000s. More recently in 2025, the Yano and [[User:Johan Larsbrink|Larsbrink]] groups independently presented the first crystal structures of '''[[GH71]]''' members (from ''Schizosaccharomyces'' and ''Aspergillus'', respectively). ''[[User:Antonielle Vieira Monclaro|Antonielle]] wrote an excellent overview of '''[[GH71]]''', which you should definitely check out '''[[GH71|here]]'''.''<br />
<br />
----<br />
'''8 December 2025:''' ''Just in time for the holidays:'' The '''[[Glycosyltransferase Family 138]]''' page by [[Author]] '''[[User:Wei Peng|Wei Peng]]''' and [[Responsible Curator]] '''[[User:Kim Orth|Kim Orth]]''' was [[Curator Approved]] today. '''[[GT138]]''' is small family of plant-associated bacterial members. The archetype from ''Pseudomonas syringae'', AvrB, is a rhamnosyl transferase that glycosylates the plant host protein RIN4 to effect programmed cell death (hypersensitive response). Also notable, AvrB has an unusual protein fold among [[glycosyltransferases]], based upon a "Fido" domain. '''''[[GT138]]''' represents one of a small, but hopefully growing, number of [[Glycosyltransferases|GT]] pages in ''CAZypedia'', whose unique features you should read more about '''[[GT138|here]]'''.''<br />
----<br />
'''31 October 2025:''' ''A spooktacular addition to the CAZypedia family!'' Come and say 'Boo!' to the frighteningly well written '''[[CBM13]]''' ''CAZypedia'' page. The '''[[CBM13]]''' family is a '''[[Carbohydrate-binding_modules#Blurred Lines: CBMs, Lectins and Outliers|lectin-like CBM family]]'''. Its first characterized members were lectins, including the B chain from the highly toxic [https://en.wikipedia.org/wiki/Ricin ricin] toxin from ''Ricinus communis''. This spine tingling read was authored by '''[[User:Scott Mazurkewich|Scott Mazurkewich]]''' and '''[[User:Lauren McKee|Lauren McKee]]''' who also acted as responsible curator. ''Come and visit the scariest of ''CAZypedia'' CBM pages, '''[[CBM13|here!]]'''... if you dare...'' <br />
----<br />
'''29 July 2025:''' ''[[CBM91]] is in the news!'' The xylan binding '''[[CBM91]]''' family ''CAZypedia'' page is up and running. Appended to mainly [[GH43]] xylanases this [[CBM91]] family drives interaction with substrate. The [[CBM91]] page was authored by '''[[User:Daichi Ito|Daichi Ito]]''' who also discovered the initial xylan-binding function which resulted in the creation of the [[CBM91]] CAZy family. ''Read up on this industrially interesting '''[[CBM91]]''' family '''[[CBM91|here]]'''.''<br />
----</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Template:News&diff=19834Template:News2026-03-18T15:42:44Z<p>Harry Brumer: </p>
<hr />
<div>'''13 March 2026:''' ''Three more on beta-one-two!'' '''[[User:Masahiro Nakajima|Masahiro Nakajima]]''' completed and [[Curator Approved]] no less than three new pages on beta(1-2)-glucanases today. First reported by [[User:Masahiro Nakajima|Masahiro Nakajima]] and co-workers in a single publication in 2025, '''[[Glycoside Hydrolase Family 192]]''', '''[[Glycoside Hydrolase Family 193]]''', '''[[Glycoside Hydrolase Family 194]]''' further expand our understanding of beta(1-2)-glucan metabolism in bacteria. [[User:Masahiro Nakajima|Masahiro Nakajima]] has truly been instrumental in revealing new beta(1-2)-glucan-active [[GH|hydrolases]] and [[transglycosylases]], leading to the establishment of several new families in CAZy, so ''make sure to check-out his work on '''[[GH192]]''', '''[[GH193]]''', and '''[[GH194]]''', as well as '''[[GH144]]''', '''[[GH162]]''', '''[[GH186]]''', and '''[[GH189]]'''!''<br />
----<br />
<br />
'''23 January 2026:''' ''An oldie, but a goodie:'' As our first page of the new year, the '''[[Glycoside Hydrolase Family 71]]''' page, written by '''[[User:Antonielle Vieira Monclaro|Antonielle Vieira Monclaro]]''', was [[Curator Approved]] by '''[[User:Johan Larsbrink|Johan Larsbrink]]''' today. '''[[GH71]]''' is a family of mostly fungal alpha-1,3-glucanases that was established and subjected to mechanistic characterization in the early 2000s. More recently in 2025, the Yano and [[User:Johan Larsbrink|Larsbrink]] groups independently presented the first crystal structures of '''[[GH71]]''' members (from ''Schizosaccharomyces'' and ''Aspergillus'', respectively). ''[[User:Antonielle Vieira Monclaro|Antonielle]] wrote an excellent overview of '''[[GH71]]''', which you should definitely check out '''[[GH71|here]]'''.''<br />
<br />
----<br />
'''8 December 2025:''' ''Just in time for the holidays:'' The '''[[Glycosyltransferase Family 138]]''' page by [[Author]] '''[[User:Wei Peng|Wei Peng]]''' and [[Responsible Curator]] '''[[User:Kim Orth|Kim Orth]]''' was [[Curator Approved]] today. '''[[GT138]]''' is small family of plant-associated bacterial members. The archetype from ''Pseudomonas syringae'', AvrB, is a rhamnosyl transferase that glycosylates the plant host protein RIN4 to effect programmed cell death (hypersensitive response). Also notable, AvrB has an unusual protein fold among [[glycosyltransferases]], based upon a "Fido" domain. '''''[[GT138]]''' represents one of a small, but hopefully growing, number of [[Glycosyltransferases|GT]] pages in ''CAZypedia'', whose unique features you should read more about '''[[GT138|here]]'''.''<br />
----<br />
'''31 October 2025:''' ''A spooktacular addition to the CAZypedia family!'' Come and say 'Boo!' to the frighteningly well written '''[[CBM13]]''' ''CAZypedia'' page. The '''[[CBM13]]''' family is a '''[[Carbohydrate-binding_modules#Blurred Lines: CBMs, Lectins and Outliers|lectin-like CBM family]]'''. Its first characterized members were lectins, including the B chain from the highly toxic [https://en.wikipedia.org/wiki/Ricin ricin] toxin from ''Ricinus communis''. This spine tingling read was authored by '''[[User:Scott Mazurkewich|Scott Mazurkewich]]''' and '''[[User:Lauren McKee|Lauren McKee]]''' who also acted as responsible curator. ''Come and visit the scariest of ''CAZypedia'' CBM pages, '''[[CBM13|here!]]'''... if you dare...'' <br />
----<br />
'''29 July 2025:''' ''[[CBM91]] is in the news!'' The xylan binding '''[[CBM91]]''' family ''CAZypedia'' page is up and running. Appended to mainly [[GH43]] xylanases this [[CBM91]] family drives interaction with substrate. The [[CBM91]] page was authored by '''[[User:Daichi Ito|Daichi Ito]]''' who also discovered the initial xylan-binding function which resulted in the creation of the [[CBM91]] CAZy family. ''Read up on this industrially interesting '''[[CBM91]]''' family '''[[CBM91|here]]'''.''<br />
----</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Template:News&diff=19833Template:News2026-03-18T15:42:06Z<p>Harry Brumer: </p>
<hr />
<div>'''13 March 2026:''' ''Three more on beta-one-two!'' '''[[User:Masahiro Nakajima|Masahiro Nakajima]]''' completed and [[Curator Approved]] no less than three new pages on beta(1-2)-glucanases today. First reported by [[User:Masahiro Nakajima|Masahiro Nakajima]] and co-workers in a single publication in 2025, '''[[Glycoside Hydrolase Family 192]]''', '''[[Glycoside Hydrolase Family 193]]''', '''[[Glycoside Hydrolase Family 194]]''' further expand our understanding of beta(1-2)-glucan metabolism in bacteria. [[User:Masahiro Nakajima|Masahiro Nakajima]] has truly been instrumental in revealing new beta(1-2)-glucan-active [[GH|hydrolases]] and [[transglycosylases]], leading to the establishment of several new families, so ''make sure to check-out his work on '''[[GH192]]''', '''[[GH193]]''', and '''[[GH194]]''', as well as '''[[GH144]]''', '''[[GH162]]''', '''[[GH186]]''', and '''[[GH189]]'''!''<br />
----<br />
<br />
'''23 January 2026:''' ''An oldie, but a goodie:'' As our first page of the new year, the '''[[Glycoside Hydrolase Family 71]]''' page, written by '''[[User:Antonielle Vieira Monclaro|Antonielle Vieira Monclaro]]''', was [[Curator Approved]] by '''[[User:Johan Larsbrink|Johan Larsbrink]]''' today. '''[[GH71]]''' is a family of mostly fungal alpha-1,3-glucanases that was established and subjected to mechanistic characterization in the early 2000s. More recently in 2025, the Yano and [[User:Johan Larsbrink|Larsbrink]] groups independently presented the first crystal structures of '''[[GH71]]''' members (from ''Schizosaccharomyces'' and ''Aspergillus'', respectively). ''[[User:Antonielle Vieira Monclaro|Antonielle]] wrote an excellent overview of '''[[GH71]]''', which you should definitely check out '''[[GH71|here]]'''.''<br />
<br />
----<br />
'''8 December 2025:''' ''Just in time for the holidays:'' The '''[[Glycosyltransferase Family 138]]''' page by [[Author]] '''[[User:Wei Peng|Wei Peng]]''' and [[Responsible Curator]] '''[[User:Kim Orth|Kim Orth]]''' was [[Curator Approved]] today. '''[[GT138]]''' is small family of plant-associated bacterial members. The archetype from ''Pseudomonas syringae'', AvrB, is a rhamnosyl transferase that glycosylates the plant host protein RIN4 to effect programmed cell death (hypersensitive response). Also notable, AvrB has an unusual protein fold among [[glycosyltransferases]], based upon a "Fido" domain. '''''[[GT138]]''' represents one of a small, but hopefully growing, number of [[Glycosyltransferases|GT]] pages in ''CAZypedia'', whose unique features you should read more about '''[[GT138|here]]'''.''<br />
----<br />
'''31 October 2025:''' ''A spooktacular addition to the CAZypedia family!'' Come and say 'Boo!' to the frighteningly well written '''[[CBM13]]''' ''CAZypedia'' page. The '''[[CBM13]]''' family is a '''[[Carbohydrate-binding_modules#Blurred Lines: CBMs, Lectins and Outliers|lectin-like CBM family]]'''. Its first characterized members were lectins, including the B chain from the highly toxic [https://en.wikipedia.org/wiki/Ricin ricin] toxin from ''Ricinus communis''. This spine tingling read was authored by '''[[User:Scott Mazurkewich|Scott Mazurkewich]]''' and '''[[User:Lauren McKee|Lauren McKee]]''' who also acted as responsible curator. ''Come and visit the scariest of ''CAZypedia'' CBM pages, '''[[CBM13|here!]]'''... if you dare...'' <br />
----<br />
'''29 July 2025:''' ''[[CBM91]] is in the news!'' The xylan binding '''[[CBM91]]''' family ''CAZypedia'' page is up and running. Appended to mainly [[GH43]] xylanases this [[CBM91]] family drives interaction with substrate. The [[CBM91]] page was authored by '''[[User:Daichi Ito|Daichi Ito]]''' who also discovered the initial xylan-binding function which resulted in the creation of the [[CBM91]] CAZy family. ''Read up on this industrially interesting '''[[CBM91]]''' family '''[[CBM91|here]]'''.''<br />
----</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Template:News&diff=19832Template:News2026-03-18T15:39:33Z<p>Harry Brumer: </p>
<hr />
<div>'''13 March 2026:''' ''Three more on beta-one-two!'' '''[[User:Masahiro Nakajima|Masahiro Nakajima]]''' completed and [[Curator Approved]] no less than three new pages on beta(1-2)-glucanases today. First reported by [[User:Masahiro Nakajima|Masahiro Nakajima]] and co-workers in a single publication in 2025, '''[[Glycoside Hydrolase Family 192]]''', '''[[Glycoside Hydrolase Family 193]]''', '''[[Glycoside Hydrolase Family 194]]''' further expand our understanding of beta(1-2)-glucan metabolism in bacteria. [[User:Masahiro Nakajima|Masahiro Nakajima]] has truly been instrumental in revealing new beta(1-2)-glucan-active enzymes, leading to the establishment of several new families, so ''make sure to check-out his work on '''[[GH192]]''', '''[[GH193]]''', and '''[[GH194]]''', as well as '''[[GH144]]''', '''[[GH162]]''', '''[[GH186]]''', and '''[[GH189]]'''!''<br />
----<br />
<br />
'''23 January 2026:''' ''An oldie, but a goodie:'' As our first page of the new year, the '''[[Glycoside Hydrolase Family 71]]''' page, written by '''[[User:Antonielle Vieira Monclaro|Antonielle Vieira Monclaro]]''', was [[Curator Approved]] by '''[[User:Johan Larsbrink|Johan Larsbrink]]''' today. '''[[GH71]]''' is a family of mostly fungal alpha-1,3-glucanases that was established and subjected to mechanistic characterization in the early 2000s. More recently in 2025, the Yano and [[User:Johan Larsbrink|Larsbrink]] groups independently presented the first crystal structures of '''[[GH71]]''' members (from ''Schizosaccharomyces'' and ''Aspergillus'', respectively). ''[[User:Antonielle Vieira Monclaro|Antonielle]] wrote an excellent overview of '''[[GH71]]''', which you should definitely check out '''[[GH71|here]]'''.''<br />
<br />
----<br />
'''8 December 2025:''' ''Just in time for the holidays:'' The '''[[Glycosyltransferase Family 138]]''' page by [[Author]] '''[[User:Wei Peng|Wei Peng]]''' and [[Responsible Curator]] '''[[User:Kim Orth|Kim Orth]]''' was [[Curator Approved]] today. '''[[GT138]]''' is small family of plant-associated bacterial members. The archetype from ''Pseudomonas syringae'', AvrB, is a rhamnosyl transferase that glycosylates the plant host protein RIN4 to effect programmed cell death (hypersensitive response). Also notable, AvrB has an unusual protein fold among [[glycosyltransferases]], based upon a "Fido" domain. '''''[[GT138]]''' represents one of a small, but hopefully growing, number of [[Glycosyltransferases|GT]] pages in ''CAZypedia'', whose unique features you should read more about '''[[GT138|here]]'''.''<br />
----<br />
'''31 October 2025:''' ''A spooktacular addition to the CAZypedia family!'' Come and say 'Boo!' to the frighteningly well written '''[[CBM13]]''' ''CAZypedia'' page. The '''[[CBM13]]''' family is a '''[[Carbohydrate-binding_modules#Blurred Lines: CBMs, Lectins and Outliers|lectin-like CBM family]]'''. Its first characterized members were lectins, including the B chain from the highly toxic [https://en.wikipedia.org/wiki/Ricin ricin] toxin from ''Ricinus communis''. This spine tingling read was authored by '''[[User:Scott Mazurkewich|Scott Mazurkewich]]''' and '''[[User:Lauren McKee|Lauren McKee]]''' who also acted as responsible curator. ''Come and visit the scariest of ''CAZypedia'' CBM pages, '''[[CBM13|here!]]'''... if you dare...'' <br />
----<br />
'''29 July 2025:''' ''[[CBM91]] is in the news!'' The xylan binding '''[[CBM91]]''' family ''CAZypedia'' page is up and running. Appended to mainly [[GH43]] xylanases this [[CBM91]] family drives interaction with substrate. The [[CBM91]] page was authored by '''[[User:Daichi Ito|Daichi Ito]]''' who also discovered the initial xylan-binding function which resulted in the creation of the [[CBM91]] CAZy family. ''Read up on this industrially interesting '''[[CBM91]]''' family '''[[CBM91|here]]'''.''<br />
----</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=User:Masahiro_Nakajima&diff=19831User:Masahiro Nakajima2026-03-16T15:41:18Z<p>Harry Brumer: edited to use EClink template</p>
<hr />
<div>[[Image:Candidate2png.png|200px|right]]<br />
<br />
[https://www.rs.tus.ac.jp/m-nakajima/index.html Masahiro Nakajima] received his Ph.D. from the Graduate School of Agricultural and Life Science, The University of Tokyo in 2006. He joined the group of Dr. [[User:Motomitsu Kitaoka|Motomitsu Kitaoka]] as a postdoctoral fellow (2006–2010). He moved to Iwate Biotechnology Research Center as a researcher (2010–2012). He was an assistant professor in Taguchi Laboratory (2012–2020) and is currently an associate professor in his own laboratory (2020-) at Department of Applied Biological Science, Tokyo University of Science. His research currently focuses on structures and functions of carbohydrate-active enzymes acting on unique sugar chains such as β-1,2-glucan. He acts as a Responsible Curator of Glycoside Hydrolase Families '''[[GH144]]''', '''[[GH162]]''', '''[[GH186]]''', '''[[GH189]]''', '''[[GH192]]''', '''[[GH193]]''' and '''[[GH194]]''', and also created '''clan GH-S'''. He determined the functions and/or crystal structures of <br />
<br />
* [[GH1]] β-Glucosidase <cite>Nakajima2025b</cite><br />
<br />
* [[GH3]] β-Glucosidases <cite>Nakajima2012a Nakajima2016 Ishiguro2017</cite><br />
* [[GH16]] β-1,3-Glucanase <cite>Nakajima2012b</cite><br />
* [[GH35]] β-1,2-Glucosyltransglycosylase <cite>Kobayashi2022</cite> ('''[https://www.enzyme-database.org/query.php?ec=2.4.1.391 new EC number]''') and β-1,2-galactosidase <cite>Nakazawa2025</cite> ('''[https://www.enzyme-database.org/query.php?ec=3.2.1.230 new EC number]''')<br />
* [[GH38]] α-Mannosidase <cite>Nakajima2003</cite><br />
* [[GH57]] 4-α-Glucanotransferase <cite>Nakajima2004</cite><br />
* [[GH94]] 1,2-β-Oligoglucan phosphorylases <cite>Nakajima2017 Nakajima2014</cite> ('''[https://www.enzyme-database.org/query.php?ec=2.4.1.333 new EC number]''')<br />
* [[GH112]] D-Galactosyl-β-1,4-L-rhamnose phosphorylase <cite>Nakajima2009a</cite> ('''[https://www.enzyme-database.org/query.php?ec=2.4.1.247 new EC number]''') and β-1,3-galactosyl-''N''-acetylhexosamine phosphorylases <cite>Nakajima2009a Nakajima2009b Nakajima2008a Nakajima2008b</cite><br />
* [[GH144]] Bacterial β-1,2-glucanases <cite>Abe2017</cite> ('''family created''') and sophorosylhydrolase <cite>Shimizu2018</cite> ('''[https://www.enzyme-database.org/query.php?ec=3.2.1.214 new EC number]''')<br />
* [[GH162]] Fungal β-1,2-glucanase <cite>Tanaka2019</cite> ('''family created''') ('''clan GH-S created''')<br />
* [[GH186]] ''E. coli'' β-1,2-glucanase <cite>Motouchi2023</cite> ('''family created''') and α-1,6-cyclized β-1,2-glucohexadecaose synthase from ''Xanthomonas campestris'' pv. ''campestris'' (new EC number enzyme)<cite>Motouchi2024</cite><br />
* [[GH189]] Cyclic β-1,2-glucan synthase ([[Transglycosylases|transglycosylase]] domain) <cite>Tanaka2024</cite> ('''family created''') ('''[{{EClink}}2.4.1.397 new EC number]''')<br />
* [[GH192]] Bacterial β-1,2-glucanase <cite>Nakajima2025a</cite> ('''family created''')<br />
* [[GH193]] Bacterial β-1,2-glucanase <cite>Nakajima2025a</cite> ('''family created''')<br />
* [[GH194]] Bacterial β-1,2-glucanase <cite>Nakajima2025a</cite> ('''family created''')<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Nakajima2012a pmid=21850431<br />
#Nakajima2016 pmid=26886583<br />
#Ishiguro2017 pmid=29131329<br />
<br />
#Nakajima2012b pmid=22685137<br />
#Nakajima2003 pmid=12801516<br />
#Nakajima2004 pmid=15564678<br />
<br />
#Nakajima2017 pmid=28198470<br />
#Nakajima2014 pmid=24647662<br />
<br />
#Nakajima2009a pmid=19491100<br />
#Nakajima2009b pmid=19132369<br />
#Nakajima2008a pmid=18723650<br />
#Nakajima2008b pmid=18183385<br />
<br />
#Abe2017 pmid=28270506<br />
#Shimizu2018 pmid=29763309<br />
#Tanaka2019 pmid=30926603<br />
#Kobayashi2022 pmid=35065074<br />
#Motouchi2023 pmid=37735577<br />
#Motouchi2024 pmid=38957137<br />
#Tanaka2024 pmid=38300345<br />
#Nakazawa2025 pmid=39820076<br />
#Nakajima2025a pmid=40411428<br />
#Nakajima2025b pmid=40838837<br />
<br />
<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Nakajima,Masahiro]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=B.A._Stone_Award_for_Excellence_in_Plant_Polysaccharide_Biochemistry&diff=19817B.A. Stone Award for Excellence in Plant Polysaccharide Biochemistry2026-03-13T21:33:03Z<p>Harry Brumer: </p>
<hr />
<div>[[File:BAStone.png|thumb|150px|right|'''Emeritus Professor [[Bruce Stone]], 1928-2008<sup>&dagger;</sup>''']]<br />
[[File:BAStoneAwardMedal.png|thumb|150px|right|'''The B.A. Stone Medal''']]<br />
== Introduction ==<br />
The B.A. Stone Award was conceived "to recognise outstanding contributions to our understanding of cell wall and more general carbohydrate biochemistry," in honor of Emeritus Professor Bruce Arthur Stone (1928-2008<sup>&dagger;</sup>, a biosketch is available [[Bruce Stone|here]]). The Award, which includes a medal (pictured on right) and an honorarium, will generally be made biannually, although under some circumstances it may be awarded more (or less) frequently. The B.A. Stone Award was initiated by [https://www.megazyme.com/ Megazyme Ltd.] and continues to be sponsored by [https://www.neogen.com/ NEOGEN Corporation], which [https://www.megazyme.com/news/megazyme-has-been-acquired-by-neogen acquired Megazyme in 2021].<br />
<br />
Aspects of the award include the following:<br />
* Reflecting Bruce's international outlook, the Award is open to scientists from all countries around the world.<br />
* Where appropriate, the Award will be directed toward mid-career scientists.<br />
* The awardee will have made at least one major contribution in the field that has achieved international recognition.<br />
* When possible, the Award will be presented publicly at an appropriate international scientific conference.<br />
<br />
== Awardees ==<br />
* 2024 - '''Dr. Jenny Mortimer''', [https://researchers.adelaide.edu.au/profile/jenny.mortimer University of Adelaide, Australia], and '''Dr. Antony Bacic''', [https://scholars.latrobe.edu.au/tbacic La Trobe University, Australia]<br />
* 2021 - '''Dr. Bernard Henrissat''', [https://orbit.dtu.dk/en/persons/bernard-paul-henrissat/ Technical University of Denmark]; [http://www.afmb.univ-mrs.fr/Bernard-Henrissat?lang=en Emeritus CNRS Director of Research, CNRS and Aix-Marseille University]; <br />
* 2019 - '''Dr. Paul Dupree''', [https://www.bioc.cam.ac.uk/research/dupree University of Cambridge, United Kingdom] ''(see also [https://www.bioc.cam.ac.uk/news/paul-dupree-receives-ba-stone-award here])''<br />
* 2016 - '''Dr. Harry Brumer''', [https://www.msl.ubc.ca/people/dr-harry-brumer/ University of British Columbia, Canada] ''(see also [https://www.chem.ubc.ca/congratulations-dr-harry-brumer here])''<br />
* 2014 - '''Dr. Jochen Zimmer''', [https://med.virginia.edu/faculty/faculty-listing/jz3x/ University of Virginia, USA], and '''Dr. Geoffrey Fincher''', [http://www.adelaide.edu.au/directory/geoffrey.fincher University of Adelaide, Australia]<br />
* 2013 - '''Dr. Birte Svensson''', [https://orbit.dtu.dk/en/persons/birte-svensson/ Technical University of Denmark, Denmark]<br />
* 2011 - '''Dr. Harry Gilbert''', [https://en.wikipedia.org/wiki/Harry_Gilbert_(biochemist) University of Newcastle, UK]<br />
* 2010 - '''Dr. Vincent Bulone''', [https://www.kth.se/profile/bulone/?l=en Royal Institute to Technology (KTH), Sweden] (now [https://www.flinders.edu.au/people/vincent.bulone Flinders University, Australia])<br />
* 2008 - '''Dr. Debra Mohnen''', [https://www.ccrc.uga.edu/research/index.php?uid=25 University of Georgia, USA]<br />
<br />
----<br />
==== Acknowledgement ====<br />
''This page was initially produced based on key information kindly provided by [https://www.flinders.edu.au/people/vincent.bulone Prof. Vincent Bulone] and [https://www.linkedin.com/in/barry-mccleary-09a0a9b/ Dr. Barry McCleary].''</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=B.A._Stone_Award_for_Excellence_in_Plant_Polysaccharide_Biochemistry&diff=19816B.A. Stone Award for Excellence in Plant Polysaccharide Biochemistry2026-03-13T17:19:42Z<p>Harry Brumer: </p>
<hr />
<div>[[File:BAStone.png|thumb|150px|right|'''Emeritus Professor [[Bruce Stone]], 1928-2008<sup>&dagger;</sup>''']]<br />
[[File:BAStoneAwardMedal.png|thumb|150px|right|'''The B.A. Stone Medal''']]<br />
== Introduction ==<br />
The B.A. Stone Award was conceived "to recognise outstanding contributions to our understanding of cell wall and more general carbohydrate biochemistry," in honor of Emeritus Professor Bruce Arthur Stone (1928-2008<sup>&dagger;</sup>, a biosketch is available [[Bruce Stone|here]]). The Award, which includes a medal (pictured on right) and an honorarium, will generally be made biannually, although under some circumstances it may be awarded more (or less) frequently. The B.A. Stone Award was initiated by [https://www.megazyme.com/ Megazyme Ltd.] and continues to be sponsored by [https://www.neogen.com/ NEOGEN Corporation], which [https://www.megazyme.com/news/megazyme-has-been-acquired-by-neogen acquired Megazyme in 2021].<br />
<br />
Aspects of the award include the following:<br />
* Reflecting Bruce's international outlook, the Award is open to scientists from all countries around the world.<br />
* Where appropriate, the Award will be directed toward mid-career scientists.<br />
* The awardee will have made at least one major contribution in the field that has achieved international recognition.<br />
* When possible, the Award will be presented publicly at an appropriate international scientific conference.<br />
<br />
== Awardees ==<br />
* 2024 - '''Dr. Jenny Mortimer''', [https://researchers.adelaide.edu.au/profile/jenny.mortimer University of Adelaide, Australia]<br />
* 2021 - '''Dr. Bernard Henrissat''', [https://orbit.dtu.dk/en/persons/bernard-paul-henrissat/ Technical University of Denmark]; [http://www.afmb.univ-mrs.fr/Bernard-Henrissat?lang=en Emeritus CNRS Director of Research, CNRS and Aix-Marseille University]; <br />
* 2019 - '''Dr. Paul Dupree''', [https://www.bioc.cam.ac.uk/research/dupree University of Cambridge, United Kingdom] ''(see also [https://www.bioc.cam.ac.uk/news/paul-dupree-receives-ba-stone-award here])''<br />
* 2016 - '''Dr. Harry Brumer''', [https://www.msl.ubc.ca/people/dr-harry-brumer/ University of British Columbia, Canada] ''(see also [https://www.chem.ubc.ca/congratulations-dr-harry-brumer here])''<br />
* 2014 - '''Dr. Geoffrey Fincher''', [http://www.adelaide.edu.au/directory/geoffrey.fincher University of Adelaide, Australia]<br />
* 2014 - '''Dr. Jochen Zimmer''', [https://med.virginia.edu/faculty/faculty-listing/jz3x/ University of Virginia, USA]<br />
* 2013 - '''Dr. Birte Svensson''', [https://orbit.dtu.dk/en/persons/birte-svensson/ Technical University of Denmark, Denmark]<br />
* 2011 - '''Dr. Harry Gilbert''', [https://en.wikipedia.org/wiki/Harry_Gilbert_(biochemist) University of Newcastle, UK]<br />
* 2010 - '''Dr. Vincent Bulone''', [https://www.kth.se/profile/bulone/?l=en Royal Institute to Technology (KTH), Sweden] (now [https://www.flinders.edu.au/people/vincent.bulone Flinders University, Australia])<br />
* 2008 - '''Dr. Debra Mohnen''', [https://www.ccrc.uga.edu/research/index.php?uid=25 University of Georgia, USA]<br />
<br />
----<br />
==== Acknowledgement ====<br />
''This page was initially produced based on key information kindly provided by [https://www.flinders.edu.au/people/vincent.bulone Prof. Vincent Bulone] and [https://www.linkedin.com/in/barry-mccleary-09a0a9b/ Dr. Barry McCleary].''</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=B.A._Stone_Award_for_Excellence_in_Plant_Polysaccharide_Biochemistry&diff=19815B.A. Stone Award for Excellence in Plant Polysaccharide Biochemistry2026-03-13T17:16:39Z<p>Harry Brumer: </p>
<hr />
<div>[[File:BAStone.png|thumb|150px|right|'''Emeritus Professor [[Bruce Stone]], 1928-2008<sup>&dagger;</sup>''']]<br />
[[File:BAStoneAwardMedal.png|thumb|150px|right|'''The B.A. Stone Medal''']]<br />
== Introduction ==<br />
The B.A. Stone Award was conceived "to recognise outstanding contributions to our understanding of cell wall and more general carbohydrate biochemistry," in honor of Emeritus Professor Bruce Arthur Stone (1928-2008<sup>&dagger;</sup>, a biosketch is available [[Bruce Stone|here]]). The Award, which includes a medal (pictured on right) and an honorarium, will generally be made biannually, although under some circumstances it may be awarded more (or less) frequently. The B.A. Stone Award was initiated by [https://www.megazyme.com/ Megazyme Ltd.] and continues to be sponsored by [https://www.neogen.com/ NEOGEN Corporation], which [https://www.megazyme.com/news/megazyme-has-been-acquired-by-neogen acquired Megazyme in 2021].<br />
<br />
Aspects of the award include the following:<br />
* Reflecting Bruce's international outlook, the Award is open to scientists from all countries around the world.<br />
* Where appropriate, the Award will be directed toward mid-career scientists.<br />
* The awardee will have made at least one major contribution in the field that has achieved international recognition.<br />
* When possible, the Award will be presented publicly at an appropriate international scientific conference.<br />
<br />
== Awardees ==<br />
* 2024 - '''Dr. Jenny Mortimer''', [https://researchers.adelaide.edu.au/profile/jenny.mortimer University of Adelaide, Australia]<br />
* 2021 - '''Dr. Bernard Henrissat''', [https://orbit.dtu.dk/en/persons/bernard-paul-henrissat/ Technical University of Denmark]; [http://www.afmb.univ-mrs.fr/Bernard-Henrissat?lang=en Emeritus CNRS Director of Research, CNRS and Aix-Marseille University]; <br />
* 2019 - '''Dr. Paul Dupree''', [https://www.bioc.cam.ac.uk/research/dupree University of Cambridge, United Kingdom] ''(see also [https://www.bioc.cam.ac.uk/news/paul-dupree-receives-ba-stone-award here])''<br />
* 2016 - '''Dr. Harry Brumer''', [https://www.msl.ubc.ca/people/dr-harry-brumer/ University of British Columbia, Canada] ''(see also [https://www.chem.ubc.ca/congratulations-dr-harry-brumer here])''<br />
* 2014 - '''Dr. Geoffrey Fincher''', [http://www.adelaide.edu.au/directory/geoffrey.fincher University of Adelaide, Australia]<br />
* 2014 - '''Dr. Jochen Zimmer''', [https://med.virginia.edu/faculty/faculty-listing/jz3x/ University of Virginia, USA]<br />
* 2013 - '''Dr. Birte Svensson''', [https://orbit.dtu.dk/en/persons/birte-svensson/ Technical University of Denmark, Denmark]<br />
* 2011 - '''Dr. Harry Gilbert''', [https://en.wikipedia.org/wiki/Harry_Gilbert_(biochemist) University of Newcastle, UK]<br />
* 2010 - '''Dr. Vincent Bulone''', [https://www.kth.se/profile/bulone/?l=en Royal Institute to Technology (KTH), Sweden] (now [https://www.flinders.edu.au/people/vincent.bulone Flinders University, Australia])<br />
* 2008 - '''Dr. Debra Mohnen''', [https://www.ccrc.uga.edu/research/index.php?uid=25 University of Georgia, USA]<br />
<br />
<br />
<br />
<br />
<br />
----<br />
==== Acknowledgement ====<br />
''This page was initially produced based on key information kindly provided by [https://www.kth.se/profile/bulone/?l=en Prof. Vincent Bulone] and [https://www.megazyme.com/about-us Dr. Barry McCleary].''</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=B.A._Stone_Award_for_Excellence_in_Plant_Polysaccharide_Biochemistry&diff=19814B.A. Stone Award for Excellence in Plant Polysaccharide Biochemistry2026-03-13T17:09:43Z<p>Harry Brumer: </p>
<hr />
<div>[[File:BAStone.png|thumb|150px|right|'''Emeritus Professor [[Bruce Stone]], 1928-2008<sup>&dagger;</sup>''']]<br />
[[File:BAStoneAwardMedal.png|thumb|150px|right|'''The B.A. Stone Medal''']]<br />
== Introduction ==<br />
The B.A. Stone Award was conceived "to recognise outstanding contributions to our understanding of cell wall and more general carbohydrate biochemistry," in honor of Emeritus Professor Bruce Arthur Stone (1928-2008<sup>&dagger;</sup>, a biosketch is available [[Bruce Stone|here]]). The Award, which includes a medal (pictured on right) and an honorarium, will generally be made biannually, although under some circumstances it may be awarded more (or less) frequently. The B.A. Stone Award was initiated by [https://www.megazyme.com/ Megazyme Ltd.] and continues to be sponsored by [https://www.neogen.com/ NEOGEN Corporation], which [https://www.megazyme.com/news/megazyme-has-been-acquired-by-neogen acquired Megazyme in 2021].<br />
<br />
Aspects of the award include the following:<br />
* Reflecting Bruce's international outlook, the Award is open to scientists from all countries around the world.<br />
* Where appropriate, the Award will be directed toward mid-career scientists.<br />
* The awardee will have made at least one major contribution in the field that has achieved international recognition.<br />
* When possible, the Award will be presented publicly at an appropriate international scientific conference.<br />
<br />
== Awardees ==<br />
* 2024 - '''Dr. Jenny Mortimer''', [https://researchers.adelaide.edu.au/profile/jenny.mortimer University of Adelaide, Australia]<br />
<br />
* 2021 - '''Dr. Bernard Henrissat''', [https://www.bioengineering.dtu.dk/english/news/nyhed?id=0040d9f7-cfda-4be4-a31c-05fd831eb45d Technical University of Denmark]; [http://www.afmb.univ-mrs.fr/Bernard-Henrissat?lang=en Emeritus CNRS Director of Research, CNRS and Aix-Marseille University]; <br />
<br />
* 2019 - '''Dr. Paul Dupree''', [https://www.bioc.cam.ac.uk/research/dupree University of Cambridge, United Kingdom] ''(see also [https://www.bioc.cam.ac.uk/news/paul-dupree-receives-ba-stone-award here])''<br />
* 2016 - '''Dr. Harry Brumer''', [https://www.msl.ubc.ca/people/dr-harry-brumer/ University of British Columbia, Canada] ''(see also [https://www.chem.ubc.ca/congratulations-dr-harry-brumer here])''<br />
* 2014 - '''Dr. Geoffrey Fincher''', [http://www.adelaide.edu.au/directory/geoffrey.fincher University of Adelaide, Australia]<br />
* 2014 - '''Dr. Jochen Zimmer''', [https://med.virginia.edu/faculty/faculty-listing/jz3x/ University of Virginia, USA]<br />
* 2013 - '''Dr. Birte Svensson''', [http://www.dtu.dk/english/Service/Phonebook/Person?id=25177&tab=2&qt=dtupublicationquery Technical University of Denmark, Denmark]<br />
* 2011 - '''Dr. Harry Gilbert''', [https://www.ncl.ac.uk/csbb/people/profile/harrygilbert.html University of Newcastle, UK]<br />
* 2010 - '''Dr. Vincent Bulone''', [https://www.kth.se/profile/bulone/?l=en Royal Institute to Technology (KTH), Sweden]<br />
* 2008 - '''Dr. Debra Mohnen''', [https://www.ccrc.uga.edu/research/index.php?uid=25 University of Georgia, USA]<br />
<br />
<br />
<br />
<br />
<br />
----<br />
==== Acknowledgement ====<br />
''This page was initially produced based on key information kindly provided by [https://www.kth.se/profile/bulone/?l=en Prof. Vincent Bulone] and [https://www.megazyme.com/about-us Dr. Barry McCleary].''</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=B.A._Stone_Award_for_Excellence_in_Plant_Polysaccharide_Biochemistry&diff=19813B.A. Stone Award for Excellence in Plant Polysaccharide Biochemistry2026-03-13T16:25:27Z<p>Harry Brumer: </p>
<hr />
<div>[[File:BAStone.png|thumb|150px|right|'''Emeritus Professor [[Bruce Stone]], 1928-2008<sup>&dagger;</sup>''']]<br />
[[File:BAStoneAwardMedal.png|thumb|150px|right|'''The B.A. Stone Medal''']]<br />
== Introduction ==<br />
The B.A. Stone Award was conceived "to recognise outstanding contributions to our understanding of cell wall and more general carbohydrate biochemistry," in honor of Emeritus Professor Bruce Arthur Stone (1928-2008<sup>&dagger;</sup>, a biosketch is available [[Bruce Stone|here]]). The Award, which includes a medal (pictured on right) and an honorarium, will generally be made biannually, although under some circumstances it may be awarded more (or less) frequently. The B.A. Stone Award was initiated by [https://www.megazyme.com/ Megazyme Ltd.] and continues to be sponsored by [https://www.neogen.com/ NEOGEN Corporation], which [https://www.megazyme.com/news/megazyme-has-been-acquired-by-neogen acquired Megazyme in 2021].<br />
<br />
Aspects of the award include the following:<br />
* Reflecting Bruce's international outlook, the Award is open to scientists from all countries around the world.<br />
* Where appropriate, the Award will be directed toward mid-career scientists.<br />
* The awardee will have made at least one major contribution in the field that has achieved international recognition.<br />
* When possible, the Award will be presented publicly at an appropriate international scientific conference.<br />
<br />
== Awardees ==<br />
* 2021 - '''Prof. Bernard Henrissat''', [https://www.bioengineering.dtu.dk/english/news/nyhed?id=0040d9f7-cfda-4be4-a31c-05fd831eb45d Technical University of Denmark]; [http://www.afmb.univ-mrs.fr/Bernard-Henrissat?lang=en Emeritus CNRS Director of Research, CNRS and Aix-Marseille University]; <br />
* 2019 - '''Prof. Paul Dupree''', [https://www.bioc.cam.ac.uk/research/dupree University of Cambridge, United Kingdom] ''(see also [https://www.bioc.cam.ac.uk/news/paul-dupree-receives-ba-stone-award here])''<br />
* 2016 - '''Prof. Harry Brumer''', [https://www.msl.ubc.ca/people/dr-harry-brumer/ University of British Columbia, Canada] ''(see also [https://www.chem.ubc.ca/congratulations-dr-harry-brumer here])''<br />
* 2014 - '''Prof. Geoffrey Fincher''', [http://www.adelaide.edu.au/directory/geoffrey.fincher University of Adelaide, Australia]<br />
* 2014 - '''Assoc. Prof. Jochen Zimmer''', [https://med.virginia.edu/faculty/faculty-listing/jz3x/ University of Virginia, USA]<br />
* 2013 - '''Prof. Birte Svensson''', [http://www.dtu.dk/english/Service/Phonebook/Person?id=25177&tab=2&qt=dtupublicationquery Technical University of Denmark, Denmark]<br />
* 2011 - '''Prof. Harry Gilbert''', [https://www.ncl.ac.uk/csbb/people/profile/harrygilbert.html University of Newcastle, UK]<br />
* 2010 - '''Prof. Vincent Bulone''', [https://www.kth.se/profile/bulone/?l=en Royal Institute to Technology (KTH), Sweden]<br />
* 2008 - '''Prof. Debra Mohnen''', [https://www.ccrc.uga.edu/research/index.php?uid=25 University of Georgia, USA]<br />
<br />
<br />
<br />
<br />
<br />
----<br />
==== Acknowledgement ====<br />
''This page was initially produced based on key information kindly provided by [https://www.kth.se/profile/bulone/?l=en Prof. Vincent Bulone] and [https://www.megazyme.com/about-us Dr. Barry McCleary].''</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=User:Navindu_Dinara_Gajanayaka&diff=19763User:Navindu Dinara Gajanayaka2026-02-24T17:20:26Z<p>Harry Brumer: made hyperlinks consistent, removed extra lines</p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
Navindu Dinara Gajanayaka completed his Bachelor of Science Honours in Marine and Freshwater Sciences at the [https://www.ruh.ac.lk/index.php/en/ University of Ruhuna], Sri Lanka, in 2021. Since 2022, he is pursuing a combined Master's/PhD program in Marine Convergence Engineering (Marine Biotechnology) at the [https://www.ust.ac.kr/eng/ University of Science & Technology (UST)], Daejeon, South Korea. His research focuses on the discovery and characterization of microbial CAZymes involved in the degradation of marine algal polysaccharides, with particular emphasis on ulvan lyases and the biochemical properties of their enzymatic products. His work contributes to a broader understanding of enzymatic mechanisms underlying marine biomass degradation, with potential applications in biotechnology and sustainable bio-based industries. He conducts his research as a student researcher at the Jeju Bio Research Center, [https://www.kiost.ac.kr/eng.do Korea Institute of Ocean Science and Technology (KIOST)], Jeju, South Korea, where he has access to diverse marine biological resources supporting his investigations into novel enzyme discovery.<br />
<br />
----<br />
<biblio><br />
#Gajanayaka2025 pmid=39919756<br />
#Gajanayaka2024 pmid=39728150<br />
#Lee2024 pmid=39728133<br />
#Jo2024 pmid=39590775<br />
#Marasinghe2024 pmid=39009167<br />
</biblio><br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Gajanayaka,Navindu]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Polysaccharide_Lyase_Family_40&diff=19757Polysaccharide Lyase Family 402026-02-24T01:53:47Z<p>Harry Brumer: added standardized PDBlink template</p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Navindu Dinara Gajanayaka|Navindu Dinara Gajanayaka]]<br />
<br />
* [[Responsible Curator]]: [[User:Jan-Hendrik Hehemann|Jan-Hendrik Hehemann]]<br />
<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Polysaccharide Lyase Family PL40'''<br />
|-<br />
|'''3D Structure''' <br />
|<br />
|-<br />
|'''Mechanism''' <br />
|<br />
|-<br />
|'''Charge neutraliser'''<br />
|<br />
|-<br />
|'''Active site residues'''<br />
|<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}PL40.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Substrate specificities ==<br />
PL40 enzymes are categorized as ulvan lyases that primarily degrade ulvan, a sulfated polysaccharide found in green macroalgae (''Ulva'' spp.). These enzymes specifically target the uronic acid-rich backbone regions of ulvan, particularly the GlcA/IdoA-Rha3S motif <cite>Reisky2019</cite>. PL40 family members function as endolytic enzymes, cleaving internal glycosidic linkages to release oligosaccharides terminated with Δ4,5-unsaturated uronic acids <cite>Reisky2019 Gajanayaka2024 Fu2026 Wang2026</cite>. <br />
== Kinetics and Mechanism ==<br />
<br />
PL40 ulvan lyases employ a β-elimination mechanism in which abstraction of the C5 proton from the uronic acid residue triggers cleavage of the C-O4 glycosidic bond, generating a Δ4,5-unsaturated uronic acid at the non-reducing end of the product <cite>Wang2026</cite>. The catalytic machinery of PL40 Uly1040 involves key residues including histidine and tyrosine, along with Mn²⁺ and additional residues within the substrate binding pocket, which collectively organize and activate the catalytic center <cite>Wang2026</cite>. Enzymes within the PL40 family typically exhibit optimal activity at pH 7-8 and temperatures of 35-40°C <cite>Gajanayaka2024 Wang2026</cite>. Their catalytic efficiency is often enhanced by divalent metal ions, including Mn²⁺, Fe²⁺, Mg²⁺, and Ca²⁺ <cite>Gajanayaka2024 Wang2026</cite>.<br />
<br />
== Catalytic Residues ==<br />
<br />
To date, Uly1040 remains the only comprehensively characterized PL40 enzyme with detailed structural and mechanistic information, serving as the prototypical model for the entire family <cite>Wang2026</cite>. The catalytic mechanism centers on a conserved His/Tyr dyad, a histidine residue (His485) functions as the general base, abstracting the C5 proton from the uronic acid during β-elimination, while a tyrosine (Tyr305) acts as the general acid, donating a proton to the leaving group. The active site architecture includes several supporting residues that facilitate catalysis. Trp246 and Asn245 stabilize the transition state by neutralizing the negative charge on the uronic acid carboxyl group at the +1 subsite. Additionally, His487 and Asp358 coordinate with a bound Mn²⁺ ion to properly orient and activate the catalytic histidine (His485). Bioinformatic and phylogenetic analyses reveal that this His/Tyr catalytic dyad and its network of supporting residues are highly conserved across PL40 family members, suggesting a shared catalytic mechanism throughout the family <cite>Wang2026</cite>.<br />
<br />
== Three-dimensional structures ==<br />
<br />
The crystal structure of Uly1040 from ''Alteromonas macleodii'', solved at 1.74 Å resolution (PDB ID [{{PDBlink}}9VTK 9VTK]) , represents the only structurally characterized member of the PL40 family to date. Uly1040 exhibits a two-domain architecture characteristic of PL40 ulvan lyases. The N-terminal domain (residues 27–430) consists a distinctive (α/α)₆ toroid fold comprising 16 α-helices and 2 β-strands. This domain region critical catalytic machinery, including the catalytic base His485 and the Mn²⁺ coordination site. The C-terminal domain (residues 444–856) contains a more complex architecture with 7 α-helices and 29 β-strands organized into six antiparallel β-sheets. Together, these two domains create a deep substrate binding groove specifically creatred to accommodate ulvan's sulfated uronic acid–rhamnose backbone. The domains are connected by a short linker region (residues 431–443). This structural architecture strategically positions the conserved catalytic residues, including the general acid Tyr305 and supporting residues Trp246 and Asn245, to facilitate the β-elimination mechanism <cite>Wang2026</cite>. <br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: P10_PLnc BN863_21990 from ''Formosa agariphila'' provided the first evidence of β-elimination activity in PL40 by generating Δ4,5-unsaturated uronic acid products <cite>Reisky2019</cite>.<br />
<br />
;First general acid/base residue identification: Uly1040 structure and mutagenesis first identified His485 (general base) and Tyr305 (general acid) as the conserved catalytic dyad for PL40 β-elimination <cite>Wang2026</cite>.<br />
<br />
;First charge neutralizer: Trp246 and Asn245 were identified as the key charge neutralizer residues that stabilize the negative charge on the uronic acid carboxylate group at the +1 subsite during β-elimination <cite>Wang2026</cite>.<br />
<br />
;First 3-D structure: Uly1040 at 1.74 Å showing the (α/α)₆ toroid and anti-parallel β-sheet domains <cite>Wang2026</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Reisky2019 Reisky, L., Prechoux, A., Zuhlke, M.K., Baumgen, M., Robb, C.S., Gerlach, N., Roret, T., Stanetty, C., Larocque, R., Michel, G., Song, T., Markert, S., Unfried, F., Mihovilovic, M.D., Trautwein-Schult, A., Becher, D., Schweder, T., Bornscheuer, U.T., and Hehemann, J.H. (2019) A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan. Nat Chem Biol 15(8):803–812. DOI:10.1038/s41589-019-0311-9<br />
<br />
#Gajanayaka2024 Gajanayaka, N.D., Jo, E., Bandara, M.S., Marasinghe, S.D., Hettiarachchi, S.A., Wijewickrama, S., Park, G.H., Oh, C., and Lee, Y. (2024) Pseudoalteromonas agarivorans-derived novel ulvan lyase of polysaccharide lyase family 40: Potential application of ulvan and partially hydrolyzed products in cosmetic industry. J Ind Microbiol Biotechnol 52. DOI:10.1093/jimb/kuaf004<br />
<br />
#Fu2026 Fu, Z., Wang, W., Lv, S., Yin, C., Wang, X., Sun, X., Zeng, R., Xu, F., Yu, W., and Han, F. (2026) Mechanistic insights into catalysis of a novel polysaccharide lyase family 40 ulvan lyase from Thalassomonas sp. LD5. Int J Biol Macromol 336:149298. DOI:10.1016/j.ijbiomac.2025.149298<br />
<br />
#Wang2026 Wang, H.-Q., Suo, C.-L., Liu, D., Wang, M.-Q., Li, J.-X., Cao, H.-Y., Qin, Q.-L., Zhang, Y.-Z., Wang, P., and Xu, F. (2026) Structural and functional insights into Uly1040, an ulvan lyase from polysaccharide lyase family 40. Appl Environ Microbiol e02101-25. DOI:10.1128/aem.02101-25<br />
</biblio><br />
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<!-- Do not delete this Category tag --><br />
[[Category:Polysaccharide Lyase Families|PL040]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_118&diff=19736Glycoside Hydrolase Family 1182026-02-06T16:45:43Z<p>Harry Brumer: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Bruno de Oliveira|Bruno Francesco Rodrigues de Oliveira]]<br />
* [[Responsible Curator]]: [[User:Bruno de Oliveira|Bruno Francesco Rodrigues de Oliveira]]<br />
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{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH118'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH118.html<br />
|}<br />
</div><br />
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<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<br />
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br />
<br />
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 DOI:10.1042/BIO03004026].<br />
</biblio><br />
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<!-- Do not delete this Category tag --><br />
[[Category:Glycoside Hydrolase Families|GH118]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_96&diff=19735Glycoside Hydrolase Family 962026-02-06T16:44:40Z<p>Harry Brumer: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Bruno de Oliveira|Bruno Francesco Rodrigues de Oliveira]]<br />
* [[Responsible Curator]]: [[User:Bruno de Oliveira|Bruno Francesco Rodrigues de Oliveira]]<br />
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<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH96'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH96.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<br />
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br />
<br />
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
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== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 DOI:10.1042/BIO03004026].<br />
</biblio><br />
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<!-- Do not delete this Category tag --><br />
[[Category:Glycoside Hydrolase Families|GH096]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=User:Bruno_de_Oliveira&diff=19734User:Bruno de Oliveira2026-02-06T16:39:12Z<p>Harry Brumer: Created page with "right '''This is an empty template to help you get started with composing your User page.''' You should begin by opening this page for ed..."</p>
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<div>[[Image:Blank_user-200px.png|200px|right]]<br />
'''This is an empty template to help you get started with composing your User page.'''<br />
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You should begin by opening this page for editing by clicking on the Edit tab above. Your biography goes in this area of the page.<br />
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<biblio><br />
#Gilbert2008 pmid=18430603<br />
<br />
</biblio><br />
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[[Category:Contributors|deOliveira,Bruno]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Polysaccharide_Lyase_Family_40&diff=19731Polysaccharide Lyase Family 402026-02-04T21:45:33Z<p>Harry Brumer: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Navindu Dinara Gajanayaka|Navindu Dinara Gajanayaka]]<br />
<br />
* [[Responsible Curator]]: [[User:Jan-Hendrik Hehemann|Jan-Hendrik Hehemann]]<br />
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<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Polysaccharide Lyase Family PL40'''<br />
|-<br />
|'''3D Structure''' <br />
|<br />
|-<br />
|'''Mechanism''' <br />
|<br />
|-<br />
|'''Charge neutraliser'''<br />
|<br />
|-<br />
|'''Active site residues'''<br />
|<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}PL40.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
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Authors may get an idea of what to put in each field from ''Curator Approved'' [[Polysaccharide Lyase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br />
<br />
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
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== Catalytic Residues ==<br />
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;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 Download PDF version].<br />
</biblio><br />
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<!-- Do not delete this Category tag --><br />
[[Category:Polysaccharide Lyase Families|PL040]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=User:Navindu_Dinara_Gajanayaka&diff=19730User:Navindu Dinara Gajanayaka2026-02-04T21:44:49Z<p>Harry Brumer: Created page with "right '''This is an empty template to help you get started with composing your User page.''' You should begin by opening this page for ed..."</p>
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----<br />
<br />
<biblio><br />
#Gilbert2008 pmid=18430603<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Gajanayaka,Navindu]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Polysaccharide_Lyase_Family_40&diff=19729Polysaccharide Lyase Family 402026-02-04T21:41:04Z<p>Harry Brumer: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: [[User:Jan-Hendrik Hehemann|Jan-Hendrik Hehemann]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Polysaccharide Lyase Family PL40'''<br />
|-<br />
|'''3D Structure''' <br />
|<br />
|-<br />
|'''Mechanism''' <br />
|<br />
|-<br />
|'''Charge neutraliser'''<br />
|<br />
|-<br />
|'''Active site residues'''<br />
|<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}PL40.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<br />
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Polysaccharide Lyase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br />
<br />
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
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== Three-dimensional structures ==<br />
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== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
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<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 Download PDF version].<br />
</biblio><br />
<br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Polysaccharide Lyase Families|PL040]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=User:Antonielle_Vieira_Monclaro&diff=19728User:Antonielle Vieira Monclaro2026-02-03T01:28:38Z<p>Harry Brumer: </p>
<hr />
<div>[[File:AntonielleCMET.jpg|200px|right]]<br />
<br />
I completed my PhD in 2018 at the University of Brasília (UnB), including a research secondment at the Norwegian University of Life Sciences (NMBU). I have worked as a scientific collaborator at EMBRAPA (Brazilian Agricultural Research Corporation), Université Libre de Bruxelles (ULB), Ghent University (UGent), and the Center for Plant Biotechnology and Genomics (CBGP).<br />
<br />
I am currently a postdoctoral researcher at UGent and a collaborating researcher at UnB. My research focuses on CAZymes, mainly from filamentous fungi, including [[AA9]], [[GH5]], [[GH7]], [[GH11]], [[GH12]], [[GH45]], and others, targeting lignocellulosic biomass degradation and related biotechnological applications.<br />
<br />
More information is available on [https://cmet.ugent.be/users/dr-antonielle-vieira-monclaro/ my CMET profile.] <br />
<br />
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<!-- Do not remove this Category tag --><br />
[[Category:Contributors|VieiraMonclaro,Antonielle]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Template:News&diff=19723Template:News2026-01-26T15:14:56Z<p>Harry Brumer: </p>
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<div>'''23 January 2026:''' ''An oldie, but a goodie:'' As our first page of the new year, the '''[[Glycoside Hydrolase Family 71]]''' page, written by '''[[User:Antonielle Vieira Monclaro|Antonielle Vieira Monclaro]]''', was [[Curator Approved]] by '''[[User:Johan Larsbrink|Johan Larsbrink]]''' today. '''[[GH71]]''' is a family of mostly fungal alpha-1,3-glucanases that was established and subjected to mechanistic characterization in the early 2000s. More recently in 2025, the Yano and [[User:Johan Larsbrink|Larsbrink]] groups independently presented the first crystal structures of '''[[GH71]]''' members (from ''Schizosaccharomyces'' and ''Aspergillus'', respectively). ''[[User:Antonielle Vieira Monclaro|Antonielle]] wrote an excellent overview of '''[[GH71]]''', which you should definitely check out '''[[GH71|here]]'''.''<br />
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'''8 December 2025:''' ''Just in time for the holidays:'' The '''[[Glycosyltransferase Family 138]]''' page by [[Author]] '''[[User:Wei Peng|Wei Peng]]''' and [[Responsible Curator]] '''[[User:Kim Orth|Kim Orth]]''' was [[Curator Approved]] today. '''[[GT138]]''' is small family of plant-associated bacterial members. The archetype from ''Pseudomonas syringae'', AvrB, is a rhamnosyl transferase that glycosylates the plant host protein RIN4 to effect programmed cell death (hypersensitive response). Also notable, AvrB has an unusual protein fold among [[glycosyltransferases]], based upon a "Fido" domain. '''''[[GT138]]''' represents one of a small, but hopefully growing, number of [[Glycosyltransferases|GT]] pages in ''CAZypedia'', whose unique features you should read more about '''[[GT138|here]]'''.''<br />
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'''31 October 2025:''' ''A spooktacular addition to the CAZypedia family!'' Come and say 'Boo!' to the frighteningly well written '''[[CBM13]]''' ''CAZypedia'' page. The '''[[CBM13]]''' family is a '''[[Carbohydrate-binding_modules#Blurred Lines: CBMs, Lectins and Outliers|lectin-like CBM family]]'''. Its first characterized members were lectins, including the B chain from the highly toxic [https://en.wikipedia.org/wiki/Ricin ricin] toxin from ''Ricinus communis''. This spine tingling read was authored by '''[[User:Scott Mazurkewich|Scott Mazurkewich]]''' and '''[[User:Lauren McKee|Lauren McKee]]''' who also acted as responsible curator. ''Come and visit the scariest of ''CAZypedia'' CBM pages, '''[[CBM13|here!]]'''... if you dare...'' <br />
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'''29 July 2025:''' ''[[CBM91]] is in the news!'' The xylan binding '''[[CBM91]]''' family ''CAZypedia'' page is up and running. Appended to mainly [[GH43]] xylanases this [[CBM91]] family drives interaction with substrate. The [[CBM91]] page was authored by '''[[User:Daichi Ito|Daichi Ito]]''' who also discovered the initial xylan-binding function which resulted in the creation of the [[CBM91]] CAZy family. ''Read up on this industrially interesting '''[[CBM91]]''' family '''[[CBM91|here]]'''.''<br />
----</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Template:News&diff=19722Template:News2026-01-26T15:08:55Z<p>Harry Brumer: </p>
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<div>'''23 January 2026:''' ''An oldie, but a goodie:'' As our first page of the new year, the '''[[Glycoside Hydrolase Family 71]]''' page written by '''[[User:Antonielle Vieira Monclaro|Antonielle Vieira Monclaro]]''', was [[Curator Approved]] by '''[[User:Johan Larsbrink|Johan Larsbrink]]''' today. '''[[GH71]]''' is a family of mostly fungal alpha-1,3-glucanases that was established and subjected to mechanistic characterization in the early 2000s. More recently in 2025, the Yano and [[User:Johan Larsbrink|Larsbrink]] groups independently presented the first crystal structures of '''[[GH71]]''' members (from ''Schizosaccharomyces'' and ''Aspergillus'', respectively). ''[[User:Antonielle Vieira Monclaro|Antonielle]] wrote an excellent overview of '''[[GH71]]''', which you should definitely check out '''[[GH71|here]]'''.''<br />
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'''8 December 2025:''' ''Just in time for the holidays:'' The '''[[Glycosyltransferase Family 138]]''' page by [[Author]] '''[[User:Wei Peng|Wei Peng]]''' and [[Responsible Curator]] '''[[User:Kim Orth|Kim Orth]]''' was [[Curator Approved]] today. '''[[GT138]]''' is small family of plant-associated bacterial members. The archetype from ''Pseudomonas syringae'', AvrB, is a rhamnosyl transferase that glycosylates the plant host protein RIN4 to effect programmed cell death (hypersensitive response). Also notable, AvrB has an unusual protein fold among [[glycosyltransferases]], based upon a "Fido" domain. '''''[[GT138]]''' represents one of a small, but hopefully growing, number of [[Glycosyltransferases|GT]] pages in ''CAZypedia'', whose unique features you should read more about '''[[GT138|here]]'''.''<br />
----<br />
'''31 October 2025:''' ''A spooktacular addition to the CAZypedia family!'' Come and say 'Boo!' to the frighteningly well written '''[[CBM13]]''' ''CAZypedia'' page. The '''[[CBM13]]''' family is a '''[[Carbohydrate-binding_modules#Blurred Lines: CBMs, Lectins and Outliers|lectin-like CBM family]]'''. Its first characterized members were lectins, including the B chain from the highly toxic [https://en.wikipedia.org/wiki/Ricin ricin] toxin from ''Ricinus communis''. This spine tingling read was authored by '''[[User:Scott Mazurkewich|Scott Mazurkewich]]''' and '''[[User:Lauren McKee|Lauren McKee]]''' who also acted as responsible curator. ''Come and visit the scariest of ''CAZypedia'' CBM pages, '''[[CBM13|here!]]'''... if you dare...'' <br />
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'''29 July 2025:''' ''[[CBM91]] is in the news!'' The xylan binding '''[[CBM91]]''' family ''CAZypedia'' page is up and running. Appended to mainly [[GH43]] xylanases this [[CBM91]] family drives interaction with substrate. The [[CBM91]] page was authored by '''[[User:Daichi Ito|Daichi Ito]]''' who also discovered the initial xylan-binding function which resulted in the creation of the [[CBM91]] CAZy family. ''Read up on this industrially interesting '''[[CBM91]]''' family '''[[CBM91|here]]'''.''<br />
----</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Template:News&diff=19721Template:News2026-01-25T19:08:57Z<p>Harry Brumer: </p>
<hr />
<div>'''23 January 2026:''' ''An oldie, but a goodie:'' As our first page of the new year, the '''[[Glycoside Hydrolase Family 71]]''' page, written by '''[[User:Antonielle Vieira Monclaro|Antonielle Vieira Monclaro]]''', was [[Curator Approved]] by '''[[User:Johan Larsbrink|Johan Larsbrink]]''' today. '''[[GH71]]''' is a family of mostly fungal alpha-1,3-glucanases that was established and subjected to mechanistic characterization in the early 2000s. More recently in 2025, the Yano and [[User:Johan Larsbrink|Larsbrink]] groups independently presented the first crystal structures of '''[[GH71]]''' members (from ''Schizosaccharomyces'' and ''Aspergillus'', respectively). ''[[User:Antonielle Vieira Monclaro|Antonielle]] wrote an excellent overview of '''[[GH71]]''', which you should definitely check out '''[[GH71|here]]'''.''<br />
----<br />
'''8 December 2025:''' ''Just in time for the holidays:'' The '''[[Glycosyltransferase Family 138]]''' page by [[Author]] '''[[User:Wei Peng|Wei Peng]]''' and [[Responsible Curator]] '''[[User:Kim Orth|Kim Orth]]''' was [[Curator Approved]] today. '''[[GT138]]''' is small family of plant-associated bacterial members. The archetype from ''Pseudomonas syringae'', AvrB, is a rhamnosyl transferase that glycosylates the plant host protein RIN4 to effect programmed cell death (hypersensitive response). Also notable, AvrB has an unusual protein fold among [[glycosyltransferases]], based upon a "Fido" domain. '''''[[GT138]]''' represents one of a small, but hopefully growing, number of [[Glycosyltransferases|GT]] pages in ''CAZypedia'', whose unique features you should read more about '''[[GT138|here]]'''.''<br />
----<br />
'''31 October 2025:''' ''A spooktacular addition to the CAZypedia family!'' Come and say 'Boo!' to the frighteningly well written '''[[CBM13]]''' ''CAZypedia'' page. The '''[[CBM13]]''' family is a '''[[Carbohydrate-binding_modules#Blurred Lines: CBMs, Lectins and Outliers|lectin-like CBM family]]'''. Its first characterized members were lectins, including the B chain from the highly toxic [https://en.wikipedia.org/wiki/Ricin ricin] toxin from ''Ricinus communis''. This spine tingling read was authored by '''[[User:Scott Mazurkewich|Scott Mazurkewich]]''' and '''[[User:Lauren McKee|Lauren McKee]]''' who also acted as responsible curator. ''Come and visit the scariest of ''CAZypedia'' CBM pages, '''[[CBM13|here!]]'''... if you dare...'' <br />
----<br />
'''29 July 2025:''' ''[[CBM91]] is in the news!'' The xylan binding '''[[CBM91]]''' family ''CAZypedia'' page is up and running. Appended to mainly [[GH43]] xylanases this [[CBM91]] family drives interaction with substrate. The [[CBM91]] page was authored by '''[[User:Daichi Ito|Daichi Ito]]''' who also discovered the initial xylan-binding function which resulted in the creation of the [[CBM91]] CAZy family. ''Read up on this industrially interesting '''[[CBM91]]''' family '''[[CBM91|here]]'''.''<br />
----</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19720Glycosyltransferase Family 1382026-01-25T18:32:13Z<p>Harry Brumer: /* Catalytic Residues */</p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
The GT138 family of [[glycosyltransferases]] is exemplified by AvrB <cite>Peng2024</cite>. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', AvrB utilizes host UDP-rhamnose (or dTDP-rhamnose ''in vitro'') as a co-substrate to rhamnosylate the host protein RIN4, and causes the programmed cell death (i.e. the hypersensitive response) <cite>Peng2024, Mackey2002</cite>. AvrB contains a "Fido" domain <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases (see below). Interestingly, Fido proteins can also have AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite> activities. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 1) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 1. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures (image from''' <cite>Peng2024</cite>''').''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 1) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 1) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for [[glycosyltransferases]] comprised of a Fido fold (Fig. 2A) <cite>Peng2024</cite>. Most [[glycosyltransferases]] contain GT-A, GT-B, GT-C, lysozyme-type, [[GT101]], or [[GT108]] folds (Fig. 2B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 2A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite substantial primary sequence divergence <cite>Kinch2009</cite>.<br />
<br />
[[File:GT138-Fig1-V3.png|thumb|1250px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left, image from <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB (Fig. 2A) <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_108&diff=19719Glycosyltransferase Family 1082026-01-25T18:31:32Z<p>Harry Brumer: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Spencer Williams|Spencer Williams]]<br />
* [[Responsible Curator]]: [[User:Spencer Williams|Spencer Williams]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT108'''<br />
|-<br />
|'''Clan''' <br />
|GH-S<br />
|-<br />
|'''Mechanism'''<br />
|inverting<br />
|-<br />
|'''Reactions'''<br />
|GDP-Man β-1,2-mannosyltransferase 2.4.1-, donor is GDP-α-Man;<br>1,2-β-oligomannan phosphorylase [{{EClink}}2.4.1.340 2.4.1.340], product is α-mannose-1-phosphate <br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT108.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
The [[glycosyltransferases]] in family GT108 were originally identified by bioinformatics analysis using GH130 sequences as a query. This identified a tandem repeat of seven genes on chromosome 10 of ''Leishmania mexicana'' and varying numbers of orthologs in other trypanosomatids <cite>Sernee2019</cite>. A null mutant lacking the entire array of seven genes lost the ability to synthesize 1,2-β-oligomannan (termed mannogen). These enzymes were termed mannosyltransferase/phosphorylases (MTPs) owing to ability to both synthesize mannogen from GDPMan and/or Man-1-P, as well as an ability to catalyze phosphorolysis of mannogen to form Man-1-P. Specifically, the ''L. mexicana'' enzymes MPT3, MPT4, MPT6 and MPT7 catalyze the phosphorolysis of mannogen to give Man-1-P, as well as the reverse reaction to synthesize mannogen by mannosyltransfer from Man-1-P. The ‘’L. mexicana’’ enzymes MPT1 and MPT2 act as GDP-Man dependent β-1,2-mannosyltransferases, elongating mannogen, and lack detectable phosphorolytic activity.<br />
<br />
== Kinetics and Mechanism ==<br />
In the glycoside cleavage reaction Asp83 of ''Leishmania mexicana'' MPT4 acts as a [[general acid]], protonating the glycosidic leaving group via a proton relay through the -1 subsite mannose 3-OH, allowing phosphate to displace the anomeric glycoside leaving group. In the reverse reaction involving mannosyl transfer from Man-1-P (or GDP-Man for MPT1 and 2), this residue acts as a [[general base]], deprotonating the 2-OH of the sugar nucleophile to promote glycosidic bond formation. The proposed mechanism is similar to that for family [[GH130]] β-1,2-mannoside phosphorylases <cite> Nakae2013</cite><br />
<br />
== Catalytic Residues ==<br />
Asp83 is the catalytic general base in the ''Leishmania mexicana'' MPT4 <cite>Sernee2019</cite>. Activity as a mannosyltransferase or phosphorylase is achieved by a His/Arg switch: the GDP-Man transferases MTP1 and MTP2 contain a His residue (His168 in MTP1 and His161 in MTP2) in the active site; at the equivalent position the phosphorolytic MTPs such as MTP4 contain an Arg residue (Arg150) <cite>Sernee2019</cite>. <br />
<br />
== Three-dimensional structures ==<br />
The three-dimensional structures of several GT108 proteins have been reported. The Structural Genomics of Pathogenic Protozoa Consortium (SGPP) deposited the first structure of a member of this family as a 'hypothetical protein' from ''L. major'' <cite>Holmes2005</cite>; the function of this protein remains unknown. The structures of several MPTs from ''L. mexicana'' have been reported <cite>Sernee2019</cite>. All proteins have a five-bladed β-propeller fold. Similar folds are predicted for other family members <cite>Sernee2019</cite>. A complex of the D94N variant of ''L. mexicana'' MPT2 with mannobiose highlighted this conserved residue as the likely [[general acid]] for the reverse phosphorolytic reaction. Superposition of the structures of the MPTs with [[GH130]] β-mannoside phosphorylases highlighted conserved active site residues in the -1 subsite, and conserved interactions with the sugar residue. The Arg/His residues that correlates with GDP-Man transferase/mannoside phosphorylase activity were located in the active site cleft, in a position that was proposed to result in specific interactions with GDP or phosphate in the respective catalytic reactions <cite>Sernee2019</cite>.<br />
<br />
== Family Firsts ==<br />
;First catalytic residue identification: Asp83 in ''Leishmania mexicana'' MPT4 and other MPT enzymes <cite>Sernee2019</cite>. The His/Arg switch distinguishing GDP-Man dependent transferase activity, and phosphorolytic activity was also identified in this study.<br />
;First 3-D structure: The ''Leishmania major'' strain Friedlin protein LMJF_10_1260 was determined by X-ray crystallography <cite>Holmes2005</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Holmes2005 2B4W, Hypothetical protein from ''Leishmania major'' [http://www.rcsb.org/structure/2B4W].<br />
<br />
#Sernee2019 pmid=31513773<br />
<br />
#Nakae2013 pmid=23954514<br />
<br />
</biblio><br />
<br />
[[Category:Glycosyltransferase Families|GT108]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19718Glycosyltransferase Family 1382026-01-25T18:30:49Z<p>Harry Brumer: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
The GT138 family of [[glycosyltransferases]] is exemplified by AvrB <cite>Peng2024</cite>. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', AvrB utilizes host UDP-rhamnose (or dTDP-rhamnose ''in vitro'') as a co-substrate to rhamnosylate the host protein RIN4, and causes the programmed cell death (i.e. the hypersensitive response) <cite>Peng2024, Mackey2002</cite>. AvrB contains a "Fido" domain <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases (see below). Interestingly, Fido proteins can also have AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite> activities. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 1) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 1. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures (image from''' <cite>Peng2024</cite>''').''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for [[glycosyltransferases]] comprised of a Fido fold (Fig. 2A) <cite>Peng2024</cite>. Most [[glycosyltransferases]] contain GT-A, GT-B, GT-C, lysozyme-type, [[GT101]], or [[GT108]] folds (Fig. 2B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 2A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite substantial primary sequence divergence <cite>Kinch2009</cite>.<br />
<br />
[[File:GT138-Fig1-V3.png|thumb|1250px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left, image from <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB (Fig. 2A) <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19717Glycosyltransferase Family 1382026-01-25T18:27:41Z<p>Harry Brumer: Reformatted to maintain section consistency with other GT pages, also minor rephrasing.</p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
The GT138 family of glycosyltransferase is exemplified by AvrB <cite>Peng2024</cite>. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', AvrB utilizes host UDP-rhamnose (or dTDP-rhamnose ''in vitro'') as a co-substrate to rhamnosylate the host protein RIN4, and causes the programmed cell death (i.e. the hypersensitive response) <cite>Peng2024, Mackey2002</cite>. AvrB contains a "Fido" domain <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases (see below). Interestingly, Fido proteins can also have AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite> activities. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 1) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 1. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures (image from''' <cite>Peng2024</cite>''').''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for [[glycosyltransferases]] comprised of a Fido fold (Fig. 2A) <cite>Peng2024</cite>. Most [[glycosyltransferases]] contain GT-A, GT-B, GT-C, lysozyme-type, GT101, or GT108 folds (Fig. 2B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 2A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite substantial primary sequence divergence <cite>Kinch2009</cite>.<br />
<br />
[[File:GT138-Fig1-V3.png|thumb|1250px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left, image from <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
== Family members ==<br />
AvrB is the only well-studied member so far in the GT138 family <cite>Peng2024</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB (Fig. 1A) <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_47&diff=19716Glycosyltransferase Family 472026-01-25T18:11:52Z<p>Harry Brumer: fixed broken cite tags</p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Daniel Tehrani|Daniel Tehrani]] and [[User:Charlie Corulli|Charlie Corulli]]<br />
* [[Responsible Curator]]: [[User:Breeanna Urbanowicz|Breeanna Urbanowicz]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT47'''<br />
|-<br />
|'''Fold''' <br />
| GT-B<br />
|-<br />
|'''Mechanism'''<br />
| Inverting<br />
|-<br />
|'''Active site residues'''<br />
| Known/unknown<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT47.html<br />
|}<br />
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<!-- This is the end of the table --><br />
<br />
== Substrate specificities ==<br />
Glycosyltransferases in GT47 catalyze the transfer of a wide variety of monosaccharides from activated donor sugar nucleotides onto a diversity of acceptor substrates found in plants, animals, insects, and bacteria <cite>Zhang2023</cite>. Donor sugar nucleotides for discrete clades of GT47 enzymes include UDP-Arabinofuranose (UDP-Araf), UDP-Arabinopyranose (UDP-Arap), UDP-Xylose (UDP-Xyl), UDP-Galactose (UDP-Gal), UDP-Galacturonic acid (UDP-GalA), and UDP-Glucuronic acid (UDP-GlcA, i.e. EXT1) <cite>Zhang2023 LiX2004 Harholt2006 Wu2009 Madson2003 Pena2012 LiH2023</cite>. Genes encoding members of the GT47 family are found across all domains of life, and known biochemical pathways GT47 enzymes include diverse plant cell wall polysaccharides and glycoproteins and the heparan sulfate backbone <cite>Zhang2023 LiH2023</cite>.<br />
<br />
=== Plants ===<br />
<br />
The GT47 family is highly diversified in plants, having an association with the biosynthesis of almost every class of plant cell wall polysaccharide <cite>Zhang2023</cite>. Although the enzymatic functions for the vast majority of plant GT47s are currently unknown, analysis of plant mutants has identified members predicted to use UDP-GalA, UDP-Gal, UDP-Arap, UDP-Araf, and UDP-Xyl as activated sugar donors. Known acceptor polysaccharide substrates include xyloglucan, xylan, galacto-glucomannan, xylo-galacturonan, cell wall extensins, and rhamnogalacturonan I. Most members of GT47 from plants have been identified through analysis of mutants.<br />
<br />
==== Xyloglucan ====<br />
Xyloglucan is a hemicellulose and a major component of primary cell walls of dicots <cite>Zabotina2012</cite>. Xyloglucan forms polymer-polymer interactions with cellulose that can be influenced by the diversity of sidechains found on xyloglucan that vary depending on plant species, tissue, and stage of growth <cite>Schultink2014</cite>. Various members of the GT47 family have been reported to contribute to the synthesis of the numerous sidechains found on xyloglucan, with the two most notable being the xyloglucan-modifying galactosyltransferases MURUS3 (MUR3) and Xyloglucan L-Side Chain Galactosyltransferase2 (XLT2). These enzymes catalyze the regiospecific addition of β-D-Gal forming the Gal-β1,2-Xyl-α- (‘L) sidechains of xyloglucan <cite>Madson2003 Jensen2012</cite>. XyG “S”-Side Chain Transferase1 (XST1) and Xyloglucan “D”‐Side Chain Transferase (XDT)are reported to transfer UDP-Araf and UDP-Arap respectively to the 3rd, reducing end, xylose of xyloglucan, forming the Araf-α1,2-Xyl-α- (‘S) and Arap-α1,2- Xyl-α- (‘D) sidechain motifs <cite>Schultink2013 ZhuL2018</cite>. Xyloglucan-Specific Galacturonosyltransferase1 (XUT1) is reported to transfer UDP-GalA, forming the GalA-β1,2-Xyl-α- (‘Y) sidechain <cite>Pena2012</cite>. More recently, Xyloglucan Beta-Xylopyranosyltransferase (XBT) has been identified to transfer UDP-Xyl to form the Xyl-β1,2-Xyl-α-(‘U) sidechain <cite>Immelmann2023</cite>. Taken together, the quantity of GT47s identified to act on xyloglucan to date is indicative of the important role this family has in contributing to the diversity of this polymer.<br />
<br />
==== Xylan ====<br />
Unlike the previously mentioned sidechain modifications of xyloglucan, GT47s can additionally contribute to the synthesis of polymer backbones as observed with xylan. Xylan is a hemicellulosic polysaccharide and a major component of plant secondary cell walls. This polysaccharide is composed of a β1,4-Xyl backbone that is directly synthesized by Xylan Synthase (XYS) enzymes. They are thought to function in a complex with two other members of GT43 <cite>Zhang2023 Brown2009 Brown2007</cite>. This xylan synthase complex (XSC) contributes to the synthesis of the xylan backbone, although XYS is the only enzyme in the complex which displays an enzymatic function in extending xylan in vivo. Loss of function mutations have additionally identified Irregular Xylem7 (IRX7) as another potential xylan modifying GT47, hypothesized to participate in synthesis of the reducing end tetrasaccharide β-D-Xyl-1,4-[β-D-Xyl-1,3-α-l-Rha-1,2-α-D-GalA-1,4-D-Xyl] present in xylans from dicots, although more evidence is required to elucidate this function <cite>Brown2009 Brown2007</cite>.<br />
<br />
==== Mannan====<br />
Mannan is a hemicellulosic polysaccharide prominently found in the plant primary cell wall. Galactoglucomannan is a classification of mannan with a backbone interspersed with β1,4-Glc which can be further substituted with α1,6-Gal residues. Recently, it was shown that the α1,6-Gal residues of this polymer can additionally be substituted with β1,2-Gal. Loss of function mutations in Arabidopsis have identified the mannan β-galactosyltransferase (MBGT) as the most likely candidate in synthesizing the Galβ-1,2-Galα-1,6- sidechains, catalyzing addition of the terminal galactose to the structure <cite>Yu2022</cite>.<br />
<br />
==== Pectin ====<br />
Pectin encompasses a diverse group of polymers which include homogalacturonan, rhamnogalacturonan I, rhamnogalacturonan II, and xylogalacturonan. Pectic polysaccharides play many crucial roles in plants such as intercellular adhesion, stress response, seed germination, morphogenesis, and cell communication <cite>Zhang2023 Shin2021</cite>. Loss of function mutations in Arabidopsis have identified Xylogalacturonan Deficient1 (XGD1) as a xylosyltransferase catalyzing the addition of β1,4-Xyl residues onto homogalacturonan backbone to form xylogalacturonan <cite>Jensen2008</cite>. Arabinan Deficient 1 (ARAD1) likely contributes to the synthesis of arabinan sidechains of rhamnogalacturonan I, and was identified via analysis of isolated RG-I from arad1 Arabidopsis mutants <cite>Harholt2006</cite>.<br />
<br />
==== Extensin ==== <br />
Unlike the previously mentioned polysaccharides, extensins are rod-like hydroxyproline rich glycoproteins (HRGP) that form crosslinked networks in the plant cell wall. These networks are reported to play a crucial role in regulating cell wall growth and development <cite>Showalter2016</cite>. A unique member of the GT47 family, Extensin Arabinose Deficient transferase (ExAD), is reported to synthesize the addition of the fourth arabinofuranose (Araf) on Araf substituted C4-hydroxyprolines (Hyps) creating Hyp-Araf4, a unique feature found on extensins <cite>Moller2017 Showalter2016</cite>. <br />
<br />
=== Animals ===<br />
<br />
The abundance of GT47 family enzymes in mammals is more restricted and includes only members of the Exostosin (EXT) and Exostoslin-Like (EXTL) family of enzymes involved in heparan sulfate biosynthesis. Heparan sulfate is comprised of a repeat disaccharide polymer of ( GlcAβ1,4GlcNAcα1,4-)n that is further elaborated with extensive sulfation along the polymer chain. The disaccharide backbone repeat is elongated by the co-polymerase activity of the heterodimeric EXT1-EXT2 complex <cite>LiH2023</cite>. EXT1 and EXT2 are homologous two domain enzymes, and each protein chain contains a GT47 β1,4-GlcA transferase-like and a GT64 α1,4GlcNAc transferase-like domain. Surprisingly, only the GT47 domain of EXT1 and GT64 domain of EXT2 exhibit catalytic activity, while the other domains in each subunit are nonfunctional <cite>LiH2023</cite>. Additional EXT homologs include the EXTL proteins, EXTL1-3. EXTL1 and EXTL3 are two domain proteins, each harboring a GT47 and GT64 domain like EXT1 and EXT2. However, only the GT64 domains exhibit α1,4GlcNAc transferase activity, while their corresponding GT47 domains are inactive. In contrast, EXTL2 is a single GT64 domain enzyme with a α1,4GlcNAc transferase activity, while the corresponding GT47 domain present in other EXTs is missing. Thus, among the five mammalian EXT or EXTL homologs, only EXT1 contains a functional GT47 domain exhibiting β1,4-GlcA transferase activity.<br />
<br />
== Kinetics and Mechanism ==<br />
[[File:GT47_mechanism_V7.jpg|thumb|600px|right|'''Figure 1: Proposed Mechanism of GT47 Domain in EXT1.''' GT47 enzymes employ an inverting catalytic mechanism through two potential inverting mechanisms. A) In the SN2 inverting mechanism, the hydroxyl group of an acceptor substrate (shown as GlcNAc) acts as nucleophile in a single displacement reaction leading to inversion in anomeric configuration of the transferred sugar. B) The lack of an appropriately positioned ionizable group to act as catalytic base in the EXT1 structure suggested a non-canonical SN1-like mechanism for the GT47 domain of EXT1. A similar SN1-like mechanism may also occur for other GT47 enzymes.]]<br />
GT47 enzymes employ an inverting catalytic mechanism where the hydroxyl group of an acceptor substrate presumably acts as a nucleophile in a SN2 single displacement reaction. The result is an inversion of the anomeric configuration of the transferred sugar from an α-linked sugar nucleotide donor to form a β-linked extended glycan product. While an SN2 mechanism would predict the deprotonation of the acceptor nucleophile by an enzyme associated catalytic base, the structure of the EXT1 active site did not appear to contain an appropriately positioned ionizable group to act as catalytic base <cite>LiH2023</cite>. Similar structural studies on the inverting GT-B fold glycosyltransferases, POFUT1 <cite>LiZ2017 Lira2018 Lira2011</cite> and AtFUT1 <cite>Urbanowicz2017</cite>, also indicated the lack of an appropriately positioned catalytic base for deprotonation. In these latter cases a non-canonical SN1-like mechanism was proposed. A similar SN1-like mechanism may also occur for the GT47 enzymes <cite>Zhang2023 Moremen2019</cite>.<br />
== Catalytic Residues ==<br />
Unlike GT-A fold enzymes, GT-B fold enzymes like GT47s lack the predictable catalytic features, such as a DxD motif, G-loop, xED, and C-term His, that are involved in sugar nucleotide and divalent cation interactions <cite>#Taujale2020</cite>. In place of the bridging interactions between the nucleotide sugar donor diphosphate residues and an enzyme bound divalent cation as found in GT-A fold enzymes, GT-B fold glycosyltransferases employ basic Lys and Arg side chains for interaction with the diphosphate <cite>Zhang2023 Moremen2019 Rini2022</cite>. Mutation of the active site Lys and Arg residues in the GT47 domain of EXT1 completely eliminated β1,4-GlcA transferase activity as well as co-polymerase activity for extension of heparan sulfate backbone synthesis <cite>LiH2023</cite>. Additional residues involved in donor and acceptor interactions were identified in the EXT1:UDP:acceptor complex during structural studies, but further mutagenesis studies were not performed to test function <cite>LiH2023</cite>. Analogous Lys and Arg residues can be identified in the putative donor binding sites in AlphaFold models plant GT47 enzymes, but their roles in catalysis have not been tested.<br />
<br />
== Three-dimensional structures ==<br />
<br />
[[File:EXT1EXT2 GT47 structure rendering figure 2 V5.jpg|thumb|400px|right|'''Figure 2: GT47 Domain of EXT1 in EXT1-2 Heterocomplex.''' A) Cartoon representation of EXT1 (Salmon and Green) and EXT2 (Gray) in the EXT1-2 heparan sulfate co-polymerase heterocomplex. The GT47 domain of EXT1 is highlighted in green, while the remaining GT47 domain is highlighted in salmon. The nucleotide bound to the active site shown is shown in pink, and the 4-mer heparan sulfate oligosaccharide acceptor is shown in cyan. B) Enlargement of the GT47 domain in EXT1, highlighting the two Rossman folds of the GT-B glycosyltransferase domain (β-strands of N-Term and C-Term Rossman Folds shown in yellow).]]<br />
<br />
GT47 enzymes are characterized by GT-B fold architecture comprised of two linked Rossmann-fold domains with a cleft between the domains containing the active site. GT47 enzymes bind their nucleotide sugar donor through interactions with the C-terminal Rossmann fold domain, while the acceptor substrate generally binds either in the cleft between the two domains or exclusively with the N-terminal Rossmann fold domain. The binding sites for donor and acceptor residues are generally comprised of loop regions extending from the respective Rossmann fold domains facing toward the cleft between the two domains <cite>Zhang2023 Moremen2019 Rini2022</cite>. <br />
== Family Firsts ==<br />
The first structure of a CAZy family GT47 was the cryo-EM structure of the human EXTL3, two domain protein that contained an active GT64 domain involved in adding the initial priming GlcNAc of the heparan sulfate biosynthesis pathway and a catalytically inactive GT47 domain <cite>WilsonL2022</cite>. Following this discovery, two cryo-EM structures of the EXT1-2 heterocomplex were elucidated <cite>LiH2023 LeisicoF2022</cite>. EXT1 contains a GT47 β1,4-GlcA transferase domain and an inactive GT64 α1,4GlcNAc transferase-like domain of EXT1, while EXT2 contains an inactive GT47 β1,4-GlcA transferase-like domain along with an active GT64 α1,4GlcNAc transferase domain <cite>LiH2023</cite>. Structures of UDP and acceptor co-complexes were determined for each of the enzyme active sites to map substrate interactions. The structures provided insight into the overall enzyme fold (GT-B) and catalytic site structure and mechanism (inverting) as a framework for studies on the other CAZy GT47 enzymes, especially the GT47s in plants that lack empirical structures.<br />
<br />
== References ==<br />
<biblio><br />
#Brown2007 pmid=17944810<br />
#Zhang2023 Zhang L, Prabhakar Pradeep K, Bharadwaj Vivek S, Bomble Yannick J, Peña Maria J, Urbanowicz Breeanna R. (2023) Glycosyltransferase family 47 (GT47) proteins in plants and animals. Essays in Biochemistry. 2023;67(3):639-52.[https://doi.org/10.1042/EBC20220152 DOI:10.1042/EBC20220152].<br />
#LiX2004 pmid=15020758<br />
#Harholt2006 pmid=16377743<br />
#Wu2009 pmid=18980649<br />
#Madson2003 pmid=12837954<br />
#Pena2012 pmid=23175743<br />
#LiH2023 pmid=36593275<br />
#Zabotina2012 pmid=22737157<br />
#Schultink2014 pmid=27135518<br />
#Immelmann2023 pmid=37502316<br />
#Brown2009 pmid=18980662<br />
#Yu2022 pmid=35929080<br />
#Jensen2008 pmid=18460606<br />
#Jensen2012 Jensen JK, Schultink A, Keegstra K, Wilkerson CG, Pauly M. (2012) RNA-Seq Analysis of Developing Nasturtium Seeds (Tropaeolum majus): Identification and Characterization of an Additional Galactosyltransferase Involved in Xyloglucan Biosynthesis. Molecular Plant. 2012;5(5):984-92.[https://doi.org/10.1093/mp/sss032 DOI:10.1093/mp/sss032].<br />
#Shin2021 pmid=34451757<br />
#Showalter2016 pmid=27379116<br />
#Moller2017 pmid=28358137<br />
#LiZ2017 pmid=28530709<br />
#Lira2018 pmid=30084393<br />
#Lira2011 pmid=21966509<br />
#Urbanowicz2017 pmid=28670741<br />
#Moremen2019 pmid=31427814<br />
#Taujale2020 Taujale R, Venkat A, Huang L-C, Zhou Z, Yeung W, Rasheed KM, Li S, Edison AS, Moremen KW, Kannan N. (2020) Deep evolutionary analysis reveals the design principles of fold A glycosyltransferases. eLife. 2020;9:e54532.[https://doi.org/10.7554/eLife.54532 DOI:10.7554/eLife.54532].<br />
#Rini2022 Rini JM, Moremen KW, Davis BG, Esko JD. (2022) Glycosyltransferases and Glycan-Processing Enzymes. In: Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M, Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL, Seeberger PH, editors. Essentials of Glycobiology. 4th ed. Cold Spring Harbor (NY)2022. p. 67-78.[https://www.ncbi.nlm.nih.gov/pubmed/35536929 DOI 10.1101/glycobiology.4e.6].<br />
#Schultink2013 Schultink A, Cheng K, Park YB, Cosgrove DJ, Pauly M. (2013) The Identification of Two Arabinosyltransferases from Tomato Reveals Functional Equivalency of Xyloglucan Side Chain Substituents. Plant Physiology. 2013;163(1):86-94.[https://doi.org/10.1104/pp.113.221788 DOI: 10.1104/pp.113.221788]<br />
#ZhuL2018 pmid=31245712<br />
#LeisicoF2022 pmid=36402845<br />
#WilsonL2022 pmid=35676258<br />
</biblio><br />
<br />
<br />
<!-- Do not delete this Category tag --><br />
<br />
[[Category:Glycosyltransferase Families|GT047]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Template:News&diff=19715Template:News2026-01-25T17:55:56Z<p>Harry Brumer: </p>
<hr />
<div>'''23 January 2026:''' ''An oldie, but a goodie:'' As our first page of the new year, the '''[[Glycoside Hydrolase Family 71]]''' page, written by '''[[User:Antonielle Vieira Monclaro|Antonielle Vieira Monclaro]]''', was [[Curator Approved]] by '''[[User:Johan Larsbrink|Johan Larsbrink]]''' today. '''[[GH71]]''' is a family of mostly fungal alpha-1,3-glucanases that was established and subjected to mechanistic characterization in the early 2000s. More recently in 2025, the Yano and [[User:Johan Larsbrink|Larsbrink]] groups independently presented the first crystal structures of '''[[GH71]]''' members (from ''Schizosaccharomyces'' and ''Aspergillus'', respectively). ''[[User:Antonielle Vieira Monclaro|Antonielle]] wrote an excellent overview of '''[[GH71]]''', which you should definitely check out '''[[GH71|here]]'''.''<br />
----<br />
'''8 December 2025:''' ''Just in time for the holidays:'' The '''[[Glycosyltransferase Family 138]]''' page by [[Author]] '''[[User:Wei Peng|Wei Peng]]''' and [[Responsible Curator]] '''[[User:Kim Orth|Kim Orth]]''' was [[Curator Approved]] today. '''[[GT138]]''' is small family of plant-associated bacterial members. The archetype from ''Pseudomonas syringae'', AvrB, is a rhamnosyl transferase that glycosylates the plant host protein RIN4 to effect programmed cell death (hypersensitive response). Also notable, AvrB has an unusual protein fold among [[glycosyltransferases]], based upon a "Fido" domain." '''''[[GT138]]''' represents one of a small, but hopefully growing, number of [[Glycosyltransferases|GT]] pages in ''CAZypedia'', whose unique features you should read more about '''[[GT138|here]]'''.''<br />
----<br />
'''31 October 2025:''' ''A spooktacular addition to the CAZypedia family!'' Come and say 'Boo!' to the frighteningly well written '''[[CBM13]]''' ''CAZypedia'' page. The '''[[CBM13]]''' family is a '''[[Carbohydrate-binding_modules#Blurred Lines: CBMs, Lectins and Outliers|lectin-like CBM family]]'''. Its first characterized members were lectins, including the B chain from the highly toxic [https://en.wikipedia.org/wiki/Ricin ricin] toxin from ''Ricinus communis''. This spine tingling read was authored by '''[[User:Scott Mazurkewich|Scott Mazurkewich]]''' and '''[[User:Lauren McKee|Lauren McKee]]''' who also acted as responsible curator. ''Come and visit the scariest of ''CAZypedia'' CBM pages, '''[[CBM13|here!]]'''... if you dare...'' <br />
----<br />
'''29 July 2025:''' ''[[CBM91]] is in the news!'' The xylan binding '''[[CBM91]]''' family ''CAZypedia'' page is up and running. Appended to mainly [[GH43]] xylanases this [[CBM91]] family drives interaction with substrate. The [[CBM91]] page was authored by '''[[User:Daichi Ito|Daichi Ito]]''' who also discovered the initial xylan-binding function which resulted in the creation of the [[CBM91]] CAZy family. ''Read up on this industrially interesting '''[[CBM91]]''' family '''[[CBM91|here]]'''.''<br />
----</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Template:News&diff=19714Template:News2026-01-25T10:05:31Z<p>Harry Brumer: </p>
<hr />
<div>'''23 January 2026:''' ''An oldie, but a goodie:'' As our first page of the new year, the '''[[Glycoside Hydrolase Family 71]]''' page, written by '''[[User:Antonielle Vieira Monclaro|Antonielle Vieira Monclaro]]''', was [[Curator Approved]] by '''[[User:Johan Larsbrink|Johan Larsbrink]]''' today. '''[[GH71]]''' is a family of mostly fungal alpha-1,3-glucanases that was established and subjected to mechanistic characterization in the early 2000s. More recently in 2025, the Yano and [[User:Johan Larsbrink|Larsbrink]] groups independently presented the first crystal structures of '''[[GH71]]''' members (from ''Schizosaccharomyces'' and ''Aspergillus'', resepctively). ''[[User:Antonielle Vieira Monclaro|Antonielle]] wrote an excellent overview of '''[[GH71]]''', which you should definitely check out '''[[GH71|here]]'''.''<br />
----<br />
'''8 December 2025:''' ''Just in time for the holidays:'' The '''[[Glycosyltransferase Family 138]]''' page by [[Author]] '''[[User:Wei Peng|Wei Peng]]''' and [[Responsible Curator]] '''[[User:Kim Orth|Kim Orth]]''' was [[Curator Approved]] today. '''[[GT138]]''' is small family of plant-associated bacterial members. The archetype from ''Pseudomonas syringae'', AvrB, is a rhamnosyl transferase that glycosylates the plant host protein RIN4 to effect programmed cell death (hypersensitive response). Also notable, AvrB has an unusual protein fold among [[glycosyltransferases]], based upon a "Fido" domain." '''''[[GT138]]''' represents one of a small, but hopefully growing, number of [[Glycosyltransferases|GT]] pages in ''CAZypedia'', whose unique features you should read more about '''[[GT138|here]]'''.''<br />
----<br />
'''31 October 2025:''' ''A spooktacular addition to the CAZypedia family!'' Come and say 'Boo!' to the frighteningly well written '''[[CBM13]]''' ''CAZypedia'' page. The '''[[CBM13]]''' family is a '''[[Carbohydrate-binding_modules#Blurred Lines: CBMs, Lectins and Outliers|lectin-like CBM family]]'''. Its first characterized members were lectins, including the B chain from the highly toxic [https://en.wikipedia.org/wiki/Ricin ricin] toxin from ''Ricinus communis''. This spine tingling read was authored by '''[[User:Scott Mazurkewich|Scott Mazurkewich]]''' and '''[[User:Lauren McKee|Lauren McKee]]''' who also acted as responsible curator. ''Come and visit the scariest of ''CAZypedia'' CBM pages, '''[[CBM13|here!]]'''... if you dare...'' <br />
----<br />
'''29 July 2025:''' ''[[CBM91]] is in the news!'' The xylan binding '''[[CBM91]]''' family ''CAZypedia'' page is up and running. Appended to mainly [[GH43]] xylanases this [[CBM91]] family drives interaction with substrate. The [[CBM91]] page was authored by '''[[User:Daichi Ito|Daichi Ito]]''' who also discovered the initial xylan-binding function which resulted in the creation of the [[CBM91]] CAZy family. ''Read up on this industrially interesting '''[[CBM91]]''' family '''[[CBM91|here]]'''.''<br />
----</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycosyltransferase_Family_138&diff=19713Glycosyltransferase Family 1382026-01-25T09:45:42Z<p>Harry Brumer: /* Substrate specificities */</p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Wei Peng|Wei Peng]]<br />
* [[Responsible Curator]]: [[User:Kim Orth|Kim Orth]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT138'''<br />
|-<br />
|'''Clan''' <br />
|Fido fold<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GT138.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Family features ==<br />
'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite>. AvrB contains a '''Fido''' domain (Fig. 1A) <cite>Lee2004, Kinch2009</cite>, different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B) <cite>Varki2022, Lairson2008, Zhang2014, Sernee2019</cite>. <br />
<br />
Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Hence, AvrB is a unique Fido protein that functions as a glycosyltransferase.<br />
[[File:GT138-Fig1-V3.png|thumb|1250px|center|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left, image from <cite>Kinch2009</cite>) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]]<br />
<br />
== Substrate specificities ==<br />
As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', AvrB utilizes host UDP-rhamnose (or dTDP-rhamnose ''in vitro'') as a co-substrate to rhamnosylate the host protein RIN4, and causes the programmed cell death (namely hypersensitive response) <cite>Peng2024, Mackey2002</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
In the reaction, rhamnose is directly transferred to the side chain of a threonine of RIN4, T166 (Fig. 2) <cite>Peng2024</cite>. The rhamnosylation reaction catalyzed by AvrB does not require divalent cations (e.g., Mg<sup>2+</sup>) <cite>Peng2024</cite>. <br />
[[File:GT138-figure-2.png|thumb|900px|center|'''Figure 2. Catalysis mechanisms for RIN4 rhamnosylation by AvrB supported by crystal structures (image from''' <cite>Peng2024</cite>''').''' ('''A''') AvrB bound with RIN4. ('''B''') UDP-rhamnose bound with AvrB and RIN4. ('''C''') Rhamnose transferred to T166 of RIN4. ('''D''') Release of rhamnosylated RIN4.]]<br />
<br />
== Catalytic Residues ==<br />
A threonine (T166) from the protein substrate directly attacks the rhamnose moiety in the co-substrate, UDP-rhamnose (Fig. 2) <cite>Peng2024</cite>. The threonine is close to a histidine and a threonine in AvrB, which may stabilize the acceptor. UDP-rhamnose is stabilized by a few residues in the pocket (Fig. 2) <cite>Peng2024</cite>.<br />
<br />
== Three-dimensional structures ==<br />
AvrB represents the prototype for glycosyltransferases of Fido fold (Fig. 1A) <cite>Peng2024</cite>. AvrB contains a large internal domain between helix α2 and helix α3 (Fig. 1A) <cite>Lee2004, Desveaux2007, Kinch2009, Peng2024</cite>. AvrB shares similar structural features with other Fido proteins despite the primary sequences are divergent <cite>Kinch2009</cite>.<br />
<br />
== Family members ==<br />
AvrB is the only well-studied member so far in the GT138 family <cite>Peng2024</cite>.<br />
<br />
== Family Firsts ==<br />
The first member of GT138 family shown to be a glycosyltransferase is AvrB <cite>Peng2024</cite>.<br />
<br />
The first structure of GT138 family is AvrB (Fig. 1A) <cite>Lee2004</cite>. A few AvrB structures are available to reveal the catalysis mechanisms <cite>Lee2004, Desveaux2007, Peng2024</cite><br />
<br />
== References ==<br />
<biblio><br />
<br />
#Peng2024 pmid=38354245<br />
#Kinch2009 pmid=19503829<br />
#Yarbrough2009 pmid=19039103<br />
#Castro-Roa2013 pmid=24141193<br />
#Feng2012 pmid=22504181<br />
#Mukherjee2011 pmid=21822290<br />
#Campanacci2013 pmid=23572077<br />
#Varki2022 pmid=35536922<br />
#Lairson2008 pmid=18518825<br />
#Zhang2014 pmid=25023666<br />
#Sernee2019 pmid=31513773<br />
#Mackey2002 pmid=11955429<br />
#Lee2004 pmid=15016364<br />
#Desveaux2007 pmid=17397263<br />
<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycosyltransferase Families|GT138]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Template:News&diff=19712Template:News2026-01-25T09:40:15Z<p>Harry Brumer: </p>
<hr />
<div>'''23 January 2026:''' ''An oldie, but a goodie:'' As our first page of the new year, the '''[[Glycoside Hydrolase Family 71]]''' page, written by '''[[User:Antonielle Vieira Monclaro|Antonielle Vieira Monclaro]]''', was [[Curator Approved]] by '''[[User:Johan Larsbrink|Johan Larsbrink]]''' today. '''[[GH71]]''' is a family of mostly fungal alpha-1,3-glucanases that was established and subjected to mechanistic characterization in the early 2000s. More recently in 2025, the Yano and [[User:Johan Larsbrink|Larsbrink]] groups independently presented the first crystal structures of '''[[GH71]]''' members (from ''Schizosaccharomyces'' and ''Aspergillus'', resepctively). ''[[User:Antonielle Vieira Monclaro|Antonielle]] wrote an excellent overview of '''[[GH71]]''', which you should definitely check out [[GH71|here]]'''.''<br />
----<br />
'''31 October 2025:''' ''A spooktacular addition to the CAZypedia family!'' Come and say 'Boo!' to the frighteningly well written '''[[CBM13]]''' ''CAZypedia'' page. The '''[[CBM13]]''' family is a '''[[Carbohydrate-binding_modules#Blurred Lines: CBMs, Lectins and Outliers|lectin-like CBM family]]'''. Its first characterized members were lectins, including the B chain from the highly toxic [https://en.wikipedia.org/wiki/Ricin ricin] toxin from ''Ricinus communis''. This spine tingling read was authored by '''[[User:Scott Mazurkewich|Scott Mazurkewich]]''' and '''[[User:Lauren McKee|Lauren McKee]]''' who also acted as responsible curator. ''Come and visit the scariest of ''CAZypedia'' CBM pages, '''[[CBM13|here!]]'''... if you dare...'' <br />
<br />
----<br />
'''29 July 2025:''' ''[[CBM91]] is in the news!'' The xylan binding '''[[CBM91]]''' family ''CAZypedia'' page is up and running. Appended to mainly [[GH43]] xylanases this [[CBM91]] family drives interaction with substrate. The [[CBM91]] page was authored by '''[[User:Daichi Ito|Daichi Ito]]''' who also discovered the initial xylan-binding function which resulted in the creation of the [[CBM91]] CAZy family. ''Read up on this industrially interesting '''[[CBM91]]''' family '''[[CBM91|here]]'''.''<br />
----</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Template:News&diff=19711Template:News2026-01-25T09:39:36Z<p>Harry Brumer: </p>
<hr />
<div>'''23 January 2026:''' ''An oldie, but a goodie:'' As our first page of the new year, the '''[[Glycoside Hydrolase Family 71]]''' page, written by '''[[User:Antonielle Vieira Monclaro|Antonielle Vieira Monclaro]]''', was [[Curator Approved]] by '''[[User:Johan Larsbrink|Johan Larsbrink]]''' today. '''[[GH71]]''' is a family of mostly fungal alpha-1,3-glucanases that was established and subjected to mechanistic characterization in the early 2000s. More recently in 2025, the Yano and [[User:Johan Larsbrink|Larsbrink]] groups independently presented the first crystal structures of '''[[GH71]]''' members (from Schizosaccharomyces and Aspergillus, resepctively). ''[[User:Antonielle Vieira Monclaro|Antonielle]] wrote an excellent overview of '''[[GH71]]''', which you should definitely check out [[GH71|here]]'''.''<br />
----<br />
'''31 October 2025:''' ''A spooktacular addition to the CAZypedia family!'' Come and say 'Boo!' to the frighteningly well written '''[[CBM13]]''' ''CAZypedia'' page. The '''[[CBM13]]''' family is a '''[[Carbohydrate-binding_modules#Blurred Lines: CBMs, Lectins and Outliers|lectin-like CBM family]]'''. Its first characterized members were lectins, including the B chain from the highly toxic [https://en.wikipedia.org/wiki/Ricin ricin] toxin from ''Ricinus communis''. This spine tingling read was authored by '''[[User:Scott Mazurkewich|Scott Mazurkewich]]''' and '''[[User:Lauren McKee|Lauren McKee]]''' who also acted as responsible curator. ''Come and visit the scariest of ''CAZypedia'' CBM pages, '''[[CBM13|here!]]'''... if you dare...'' <br />
<br />
----<br />
'''29 July 2025:''' ''[[CBM91]] is in the news!'' The xylan binding '''[[CBM91]]''' family ''CAZypedia'' page is up and running. Appended to mainly [[GH43]] xylanases this [[CBM91]] family drives interaction with substrate. The [[CBM91]] page was authored by '''[[User:Daichi Ito|Daichi Ito]]''' who also discovered the initial xylan-binding function which resulted in the creation of the [[CBM91]] CAZy family. ''Read up on this industrially interesting '''[[CBM91]]''' family '''[[CBM91|here]]'''.''<br />
----</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=User:Antonielle_Vieira_Monclaro&diff=19710User:Antonielle Vieira Monclaro2026-01-23T09:47:57Z<p>Harry Brumer: added intrawiki links</p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
Antonielle completed her PhD in 2018 at the University of Brasília (UnB), with a research secondment at the Norwegian University of Life Sciences (NMBU). She has worked as a scientific collaborator at EMBRAPA (Brazilian Agricultural Research Corporation), at Université Libre de Bruxelles (ULB), at Ghent University (UGent), and at the Center for Plant Biotechnology and Genomics (CBGP).<br />
<br />
She is currently a postdoctoral researcher at UGent, and a collaborating researcher at UnB. Her research focuses on carbohydrate-active enzymes (CAZymes), mainly from filamentous fungi, including [[AA9]], [[GH5]], [[GH7]], [[GH11]], [[GH12]], [[GH45]] and others, for lignocellulosic biomass degradation and biotechnological applications.<br />
<br />
<br />
<br />
----<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|VieiraMonclaro,Antonielle]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_71&diff=19709Glycoside Hydrolase Family 712026-01-23T09:46:25Z<p>Harry Brumer: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Antonielle Vieira Monclaro|Antonielle Vieira Monclaro]]<br />
* [[Responsible Curator]]: [[User:Johan Larsbrink|Johan Larsbrink]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH71'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|inverting<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH71.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Substrate specificities ==<br />
<br />
GH71 comprises enzymes with α-1,3-glucanase activity (EC 3.2.1.59), often referred to as mutanases, based on mutan being an alternative name for α-1,3-glucan (from ''Streptococcus mutans''). Early studies demonstrated that these enzymes hydrolyze pure α-1,3-glucans while remaining inactive toward α-glucans containing mixed α-1,3/α-1,4 linkages <cite>Zonneveld1972</cite>. Subsequent work showed that GH71 enzymes act on a broader range of α-1,3-linked glucans, including pseudonigeran and soluble carboxymethylated α-1,3-glucan, but display no activity toward other tested α- or β-linked glycans <cite>Imai1977 Fuglsang2000 VillalobosDuno2013 AitLahsen2001 Dekker2004 Mazurkewich2025</cite>.<br />
<br />
Depending on the enzyme, GH71 α-1,3-glucanases may exhibit exo- or endo-type hydrolytic activity. Some enzymes with exo activity, such as Agn13.1 from ''Trichoderma harzianum'', showed a 1:1 correlation between glucose released and reducing sugars, typical of exo hydrolysis, and was unable to cleave periodate-oxidized S-glucan, which is resistant to exo-α-1,3-glucanases <cite>AitLahsen2001</cite>. Endo-acting GH71 enzymes include Agn1p from ''Schizosaccharomyces pombe'' which does not hydrolyze pNP-α-glucose, and is not inhibited by classical exo-glycosidase inhibitors such as 1-deoxynojirimycin, castanospermine, or D-glucono-1,5-lactone <cite>Dekker2004</cite>. MutAp from ''T. harzianum'', an endo-hydrolytic α-1,3-glucanase, is suggested to act processively from the non-reducing end, repeatedly releasing glucose before dissociating <cite>Grun2006 Sinitsyna2025</cite>. Its insensitivity to multiple exo-glycosidase inhibitors, and experiments with reduced oligosaccharides (e.g., G5-ol) further yield no products compatible with exo activity (e.g., G4-ol). The minimum chain-length requirement for MutAp has been shown to be a tetrasaccharide.<br />
<br />
The ''Aspergillus nidulans'' enzymes AnGH71B and AnGH71C display distinct behaviors when acting on reduced oligosaccharides (nigeropentaose and nigerohexaose), reflecting different cleavage mechanisms <cite>Mazurkewich2025</cite>. AnGH71C exhibits a pattern consistent with endo-cleavage, evidenced by the diverse products generated from reduced nigerohexaose. In contrast, AnGH71B displays exo-processive characteristics despite the absence of released reduced glucose, explained by the inability of subsite +1 to accommodate the reduced unit and therefore preventing classical terminal cleavage.<br />
<br />
Overall, GH71 enzymes exhibit strict specificity for continuous regions of α-1,3-glycosidic linkages, with no tolerance for alternating segments containing α-1,4 linkages <cite>Zonneveld1972 AitLahsen2001</cite>, as found in the polysaccharide nigeran (α-1,3/1,4-glucan). End products range from glucose (e.g. from endo-acting processive action), to nigerooligosaccharides with DP 2–7 <cite>VillalobosDuno2013 Dekker2004 Sinitsyna2025</cite>. Nigerotriose has been found as a final product together with glucose from endo-acting processive GH71 enzymes <cite>Mazurkewich2025 Grun2006</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
The anomeric configuration of the products released by α-1,3-glucanases has been elucidated by complementary NMR and crystallography approaches. In the case of MutAp from ''T. harzianum'', the hydrolysis of carboxymethylated α-1,3-glucan was monitored by ¹H NMR, revealing the appearance of β-Glc signals and the complete absence of α-Glc, demonstrating inversion of the anomeric configuration <cite>Grun2006</cite>. NMR studies of AnGH71B and AnGH71C from ''A. nidulans'' likewise showed inversion of products, and structures including the inverted anomer of the product nigerose further supports these findings <cite>Mazurkewich2025</cite>.<br />
<br />
== Catalytic Residues ==<br />
Three conserved acidic residues (Asp69, Asp237, and Glu240) were identified in the active site of Agn1p by Horaguchi et al. <cite>Horaguchi2025</cite>. Individual substitutions of these residues (D69N, D237A/N, E240A/Q) led to drastic reductions in activity on α-1,3-glucan.<br />
<br />
Structure-guided mutational studies of AnGH71B and AnGH71C directly identified the catalytic residues Asp265 (general base) and Glu268 (general acid), functionally separating subsites −4 to +3 of the enzymes <cite>Mazurkewich2025</cite>. The simultaneous observation of the α-linked substrate nigerotetraose and β-anomer of nigerotriose as product in the active site, together with an arrangement of a water molecule positioned ~3.2 Å from the anomeric carbon of the substrate, supported a classic inverting mechanism, in which Asp265 activates the nucleophilic water and Glu268 protonates the leaving group. Substitution of these residues resulted in 200- to 15,000-fold reductions in activity, confirming their catalytic role.<br />
<br />
== Three-dimensional structures ==<br />
<br />
[[File: AnGH71C.png|thumb|right|400px|'''Figure 1. Structure of ''An''GH71C from ''Aspergillus nidulans''.''' The structure solved with nigerooligosaccharides as ligand is shown (PDB ID [{{PDBlink}}9fnh 9FNH]), with one protein molecule and oligosaccharides from different chains that together span the active site, as blue sticks. The core catalytic (α/β)8 barrel is shown in silver, the C-terminal β-sheet domain in pale orange, and the catalytic residues in green.]]<br />
<br />
The three-dimensional structure of GH71 enzymes has been elucidated through two independent crystallographic studies, both revealing that members of this family adopt a classic (β/α)₈ TIM-barrel core, closely associated with a C-terminal β-sandwich accessory domain <cite>Horaguchi2025 Mazurkewich2025</cite>.<br />
<br />
The first structural description, obtained for ''S. pombe'' Agn1p, showed that its TIM barrel forms a deep cavity accessible to the solvent, consistent with the catalytic cleft observed in other glycoside hydrolases. Structural work on ''A. nidulans'' AnGH71C corroborated this overall fold and showed that the β-sandwich closely resembles an Ig-like fibronectin III domain, compacting closely against the TIM barrel to form a long substrate-binding cleft comprising at least seven subsites (−4 to +3). The structures of ligand complexes revealed minimal protein rearrangement upon binding but highlighted a conformational packing of the β6–α6 loop over subsites +1 to +3, contributing to substrate stabilization.<br />
<br />
Simulations and geometries of the bound state further indicated that GH71 enzymes exploit the intrinsic low-energy conformations of α-1,3-linked oligosaccharides, while a high-energy configuration around the −1/+1 region likely prepares the glycosidic bond for cleavage.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: The stereochemistry of GH71 enzymes has been resolved by monitoring the anomeric configuration of the released glucose using ¹H NMR spectroscopy, confirming that the enzymes operate through the inversion mechanism <cite>Grun2006</cite>.<br />
;First general acid/base residue identification: In AnGH71C, the catalytic residues have been identified as a dyad, with an aspartate residue (Asp265) acting as a general base that activates the catalytic water molecule, and a glutamate residue (Glu268) acting as a general acid that protonates the leaving group <cite>Mazurkewich2025</cite>.<br />
;First 3-D structure: The first solved structure of a GH71 enzyme was of Agn1p from ''S. pombe'', published in June 2025 by Horaguchi et al. <cite>Horaguchi2025</cite>, which demonstrated that members of the GH71 family possess a classic (β/α)₈ TIM-barrel core closely associated with a C-terminal β-sandwich accessory domain. In August the same year, Mazurkewich et al. published the structure of AnGH71C from ''A. nidulans'', which additionally included structures with glucose and nigerooligosaccharides bound in the active site, respectively <cite>Mazurkewich2025</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Zonneveld1972 pmid=4622000<br />
<br />
#Imai1977 Imai K, Kobayashi M, Matsuda K. (1977). ''Properties of an α-1,3-glucanase from Streptomyces sp. KI-8''. ''Agric Biol Chem''. 1977;'''41'''(10);1889-95. [https://doi.org/10.1080/00021369.1977.10862782 DOI: 10.1080/00021369.1977.10862782]<br />
<br />
#Fuglsang2000 pmid=10636904<br />
<br />
#VillalobosDuno2013 pmid=23825576<br />
#AitLahsen2001 pmid=11722942<br />
<br />
#Dekker2004 pmid=15194814<br />
<br />
#Mazurkewich2025 pmid=40877455<br />
<br />
#Grun2006 pmid=16780840<br />
<br />
#Sinitsyna2025 pmid=39846749<br />
<br />
#Horaguchi2025 pmid=40306164<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycoside Hydrolase Families|GH071]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_71&diff=19691Glycoside Hydrolase Family 712026-01-14T07:41:40Z<p>Harry Brumer: Changed ref. 1 to use PMID</p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Antonielle Vieira Monclaro|Antonielle Vieira Monclaro]]<br />
* [[Responsible Curator]]: [[User:Johan Larsbrink|Johan Larsbrink]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH71'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|inverting<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH71.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
GH71 comprises enzymes with α-1,3-glucanase activity (EC 3.2.1.59), often referred to as mutanases, based on mutan being an alternative name for α-1,3-glucan ((from ''Streptococcus mutans''). Early studies demonstrated that these enzymes hydrolyze pure α-1,3-glucans while remaining inactive toward α-glucans containing mixed α-1,3/α-1,4 linkages <cite>Zonneveld1972</cite>. Subsequent work showed that GH71 enzymes act on a broader range of α-1,3-linked glucans, including pseudonigeran and soluble carboxymethylated α-1,3-glucan, but display no activity toward other tested α- or β-linked glycans <cite>Imai1977 Fuglsang2000 VillalobosDuno2013 AitLahsen2001 Dekker2004 Mazurkewich2025</cite>.<br />
<br />
Depending on the enzyme, GH71 α-1,3-glucanases may exhibit exo- or endo-type hydrolytic activity. Some enzymes with exo activity, such as Agn13.1 from ''Trichoderma harzianum'', showed a 1:1 correlation between glucose released and reducing sugars, typical of exo hydrolysis, and was unable to cleave periodate-oxidized S-glucan, which is resistant to exo-α-1,3-glucanases <cite>AitLahsen2001</cite>. Endo-acting GH71 enzymes include Agn1p from ''Schizosaccharomyces pombe'' which does not hydrolyze pNP-α-glucose, and is not inhibited by classical exo-glycosidase inhibitors such as 1-deoxynojirimycin, castanospermine, or D-glucono-1,5-lactone <cite>Dekker2004</cite>. MutAp from ''Trichoderma harzianum'', an endo-hydrolytic α-1,3-glucanase, is suggested to act processively from the non-reducing end, repeatedly releasing glucose before dissociating <cite>Grun2006 Sinitsyna2025</cite>. Its insensitivity to multiple exo-glycosidase inhibitors, and experiments with reduced oligosaccharides (e.g., G5-ol) further yield no products compatible with exo activity (e.g., G4-ol). The minimum chain-length requirement for MutAp has been shown to be a tetrasaccharide.<br />
<br />
The ''Aspergillus nidulans'' enzymes AnGH71B and AnGH71C display distinct behaviors when acting on reduced oligosaccharides (nigeropentaose and nigerohexaose), reflecting different cleavage mechanisms <cite>Mazurkewich2025</cite>. AnGH71C exhibits a pattern consistent with endo-cleavage, evidenced by the diverse products generated from reduced nigerohexaose. In contrast, AnGH71B displays exo-processive characteristics despite the absence of released reduced glucose, explained by the inability of subsite +1 to accommodate the reduced unit and therefore preventing classical terminal cleavage.<br />
<br />
Overall, GH71 enzymes exhibit strict specificity for continuous regions of α-1,3-glycosidic linkages, with no tolerance for alternating segments containing α-1,4 linkages <cite>Zonneveld1972 AitLahsen2001</cite>, as found in the polysaccharide nigeran (α-1,3/1,4-glucan). End products range from glucose (e.g. from endo-acting processive action), to nigerooligosaccharides with DP 2–7 <cite>VillalobosDuno2013 Dekker2004 Sinitsyna2025</cite>. Nigerotriose has been found as a final product together with glucose from endo-acting processive GH71 enzymes <cite>Mazurkewich2025 Grun2006</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
The anomeric configuration of the products released by α-1,3-glucanases has been elucidated by complementary NMR and crystallography approaches. In the case of MutAp from ''Trichoderma harzianum'', the hydrolysis of carboxymethylated α-1,3-glucan was monitored by ¹H NMR, revealing the appearance of β-Glc signals and the complete absence of α-Glc, demonstrating inversion of the anomeric configuration <cite>Grun2006</cite>. NMR studies of AnGH71B and AnGH71C from ''Aspergillus nidulans'' likewise showed inversion of products, and structures including the inverted product nigerose further supports these findings <cite>Mazurkewich2025</cite><br />
<br />
== Catalytic Residues ==<br />
Three conserved acidic residues (Asp69, Asp237, and Glu240) were identified in the active site of Agn1p by Horaguchi et al. <cite>Horaguchi2025</cite>. Individual substitutions of these residues (D69N, D237A/N, E240A/Q) led to drastic reductions in activity on α-1,3-glucan.<br />
<br />
Structure-guided mutational studies of AnGH71B and AnGH71C directly identified the catalytic residues Asp265 (general base) and Glu268 (general acid), functionally separating subsites −4 to +3 of the enzymes <cite>Mazurkewich2025</cite>. The simultaneous observation of the α-linked substrate nigerotetraose and β-anomer of nigerotriose as product in the active site, together with an arrangement of a water molecule positioned ~3.2 Å from the anomeric carbon of the substrate, supported a classic inverting mechanism, in which Asp265 activates the nucleophilic water and Glu268 protonates the leaving group. Substitution of these residues resulted in 200- to 15,000-fold reductions in activity, confirming their catalytic role.<br />
<br />
== Three-dimensional structures ==<br />
The three-dimensional structure of GH71 enzymes has been elucidated through two independent crystallographic studies, both revealing that members of this family adopt a classic (β/α)₈ TIM-barrel core, closely associated with a C-terminal β-sandwich accessory domain <cite>Horaguchi2025 Mazurkewich2025</cite>.<br />
<br />
The first structural description, obtained for ''Schizosaccharomyces pombe'' Agn1p, showed that its TIM barrel forms a deep cavity accessible to the solvent, consistent with the catalytic cleft observed in other glycoside hydrolases. Structural work on ''Aspergillus niger'' AnGH71C corroborated this overall fold and showed that the β-sandwich closely resembles an Ig-like fibronectin III domain, compacting closely against the TIM barrel to form a long substrate-binding cleft comprising at least seven subsites (−4 to +3). The structures of ligand complexes revealed minimal protein rearrangement upon binding but highlighted a conformational packing of the β6–α6 loop over subsites +1 to +3, contributing to substrate stabilization.<br />
<br />
Simulations and geometries of the bound state further indicated that GH71 enzymes exploit the intrinsic low-energy conformations of α-1,3-linked oligosaccharides, while a high-energy configuration around the −1/+1 region likely prepares the glycosidic bond for cleavage.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: The stereochemistry of GH71 enzymes has been resolved by monitoring the anomeric configuration of the released glucose using ¹H NMR spectroscopy, confirming that the enzymes operate through the inversion mechanism <cite>Grun2006</cite>.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: In AnGH71C, the catalytic residues have been identified as a dyad, with an aspartate residue (Asp265) acting as a general base that activates the catalytic water molecule, and a glutamate residue (Glu268) acting as a general acid that protonates the leaving group <cite>Mazurkewich2025</cite>.<br />
;First 3-D structure: The first solved structure of a GH71 enzyme was of Agn1p from ''Schizosaccharomyces pombe'', published in June 2025 by Horaguchi et al. <cite>Horaguchi2025</cite>, which demonstrated that members of the GH71 family possess a classic (β/α)₈ TIM-barrel core closely associated with a C-terminal β-sandwich accessory domain. In August the same year, Mazurkewich et al. published the structure of AnGH71C from ''Aspergillus nidulans'', which additionally included structures with glucose and nigerotetraose bound in the active site, respectively <cite>Mazurkewich2025</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Zonneveld1972 pmid=4622000<br />
<br />
#Imai1977 Imai, K., Kobayashi, M. and Matsuda, K. (1977) ‘Properties of an α-1,3-glucanase from Streptomyces sp. KI-8’, Agricultural and Biological Chemistry, 41, pp. 1889–1895. [https://doi.org/10.1080/00021369.1977.10862782 DOI: 10.1080/00021369.1977.10862782]<br />
<br />
#Fuglsang2000 Fuglsang, C.C., Berka, R.M., Wahleithner, J.A., Kauppinen, S., Shuster, J.R., Rasmussen, G., Halkier, T., Dalbøge, H. and Henrissat, B. (2000) ‘Biochemical analysis of recombinant fungal mutanases’, Journal of Biological Chemistry, 275, pp. 2009–2018. [https://doi.org/10.1074/jbc.275.3.2009 DOI: 10.1074/jbc.275.3.2009]<br />
<br />
#VillalobosDuno2013 Villalobos-Duno, H., San-Blas, G., Paulinkevicius, M., Sánchez-Martín, Y. and Nino-Vega, G. (2013) ‘Biochemical characterization of Paracoccidioides brasiliensis α-1,3-glucanase Agn1p, and its functionality by heterologous expression in Schizosaccharomyces pombe’, PLoS ONE, 8, e66853. [https://doi.org/10.1371/journal.pone.0066853 DOI: 10.1371/journal.pone.0066853]<br />
<br />
#AitLahsen2001 Ait-Lahsen, H., Soler, A., Rey, M., De La Cruz, J., Monte, E. and Llobell, A. (2001) ‘An antifungal exo-α-1,3-glucanase (AGN13.1) from the biocontrol fungus Trichoderma harzianum’, Applied and Environmental Microbiology, 67, pp. 5833–5839. [https://doi.org/10.1128/AEM.67.12.5833-5839.2001 DOI: 10.1128/AEM.67.12.5833-5839.2001]<br />
<br />
#Dekker2004 Dekker, N., Speijer, D., Grün, C.H., Van den Berg, M., De Haan, A. and Hochstenbach, F. (2004) ‘Role of the α-glucanase Agn1p in fission-yeast cell separation’, Molecular Biology of the Cell, 15, pp. 3903–3914. [https://doi.org/10.1091/mbc.E04 DOI: 10.1091/mbc.E04]<br />
<br />
#Mazurkewich2025 Mazurkewich, S., Widén, T., Karlsson, H., Evenäs, L., Ramamohan, P., Wohlert, J., Brändén, G. and Larsbrink, J. (2025) ‘Structural and biochemical basis for activity of Aspergillus nidulans α-1,3-glucanases from glycoside hydrolase family 71’, Communications Biology, 8. [https://doi.org/10.1038/s42003-025-08696-3 DOI: 10.1038/s42003-025-08696-3]<br />
<br />
#Grun2006 Grün, C.H., Dekker, N., Nieuwland, A.A., Klis, F.M., Kamerling, J.P., Vliegenthart, J.F.G. and Hochstenbach, F. (2006) ‘Mechanism of action of the endo-(1→3)-α-glucanase MutAp from the mycoparasitic fungus Trichoderma harzianum’, FEBS Letters, 580, pp. 3780–3786. [https://doi.org/10.1016/j.febslet.2006.05.062 DOI: 10.1016/j.febslet.2006.05.062]<br />
<br />
#Sinitsyna2025 Sinitsyna, O.A., Volkov, P.V., Zorov, I.N., Rozhkova, A.M., Emshanov, O.V., Romanova, Y.M., Komarova, B.S., Novikova, N.S., Nifantiev, N.E. and Sinitsyn, A.P. (2025) ‘Physico-chemical properties and substrate specificity of α-(1→3)-D-glucan degrading recombinant mutanase from Trichoderma harzianum expressed in Penicillium verruculosum’, Applied and Environmental Microbiology, 91. [https://doi.org/10.1128/aem.00226-24 DOI: 10.1128/aem.00226-24]<br />
<br />
#Horaguchi2025 Horaguchi, Y., Saitoh, H., Konno, H., Makabe, K. and Yano, S. (2025) ‘Crystal structure of GH71 α-1,3-glucanase Agn1p from Schizosaccharomyces pombe: an enzyme regulating cell division in fission yeast’, Biochemical and Biophysical Research Communications, 766. [https://doi.org/10.1016/j.bbrc.2025.151907 DOI: 10.1016/j.bbrc.2025.151907]<br />
</biblio><br />
<br />
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[[Category:Glycoside Hydrolase Families|GH071]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=GH191&diff=19592GH1912025-12-04T21:56:23Z<p>Harry Brumer: Redirected page to Glycoside Hydrolase Family 191</p>
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<div>#redirect[[Glycoside Hydrolase Family 191]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=GH190&diff=19591GH1902025-12-04T21:56:11Z<p>Harry Brumer: Redirected page to Glycoside Hydrolase Family 190</p>
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<div>#redirect[[Glycoside Hydrolase Family 190]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_191&diff=19590Glycoside Hydrolase Family 1912025-12-04T21:55:52Z<p>Harry Brumer: Created page with "{{UnassignedPage}} <!-- Do not delete this Category tag --> GH191"</p>
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[[Category:Glycoside Hydrolase Families|GH191]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_190&diff=19589Glycoside Hydrolase Family 1902025-12-04T21:55:20Z<p>Harry Brumer: Created page with "{{UnassignedPage}} <!-- Do not delete this Category tag --> GH190"</p>
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[[Category:Glycoside Hydrolase Families|GH190]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=GH192&diff=19588GH1922025-12-04T21:52:39Z<p>Harry Brumer: Redirected page to Glycoside Hydrolase Family 192</p>
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<div>#redirect[[Glycoside Hydrolase Family 192]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=GH193&diff=19587GH1932025-12-04T21:52:27Z<p>Harry Brumer: Redirected page to Glycoside Hydrolase Family 193</p>
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<div>#redirect[[Glycoside Hydrolase Family 193]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=GH194&diff=19586GH1942025-12-04T21:52:14Z<p>Harry Brumer: Redirected page to Glycoside Hydrolase Family 194</p>
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<div>#redirect[[Glycoside Hydrolase Family 194]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_194&diff=19585Glycoside Hydrolase Family 1942025-12-04T21:51:35Z<p>Harry Brumer: Created page with "<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --> {{UnderConstruct..."</p>
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<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Masahiro Nakajima|Masahiro Nakajima]]<br />
* [[Responsible Curator]]: [[User:Masahiro Nakajima|Masahiro Nakajima]]<br />
----<br />
<br />
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<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH194'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH194.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<br />
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br />
<br />
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 DOI:10.1042/BIO03004026].<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycoside Hydrolase Families|GH194]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_193&diff=19584Glycoside Hydrolase Family 1932025-12-04T21:51:07Z<p>Harry Brumer: Created page with "<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --> {{UnderConstruct..."</p>
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<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Masahiro Nakajima|Masahiro Nakajima]]<br />
* [[Responsible Curator]]: [[User:Masahiro Nakajima|Masahiro Nakajima]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH193'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH193.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<br />
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br />
<br />
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 DOI:10.1042/BIO03004026].<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycoside Hydrolase Families|GH193]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_192&diff=19583Glycoside Hydrolase Family 1922025-12-04T21:50:34Z<p>Harry Brumer: Created page with "<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --> {{UnderConstruct..."</p>
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{{UnderConstruction}}<br />
* [[Author]]: [[User:Masahiro Nakajima|Masahiro Nakajima]]<br />
* [[Responsible Curator]]: [[User:Masahiro Nakajima|Masahiro Nakajima]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH192'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH192.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<br />
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br />
<br />
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 DOI:10.1042/BIO03004026].<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycoside Hydrolase Families|GH192]]</div>Harry Brumerhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_71&diff=19582Glycoside Hydrolase Family 712025-11-03T21:33:06Z<p>Harry Brumer: </p>
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<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Antonielle Vieira Monclaro|Antonielle Vieira Monclaro]]<br />
* [[Responsible Curator]]: [[User:Johan Larsbrink|Johan Larsbrink]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH71'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH71.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Content is to be added here.<br />
<br />
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br />
<br />
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 DOI:10.1042/BIO03004026].<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycoside Hydrolase Families|GH071]]</div>Harry Brumer