CAZypedia - User contributions [en-ca]

Glycoside Hydrolase Family 79

2012-03-21T14:08:01Z

Hitomi Ichinose:

{{CuratorApproved}}
* [[Author]]: ^^^Hitomi Ichinose^^^ and ^^^Satoshi Kaneko^^^
* [[Responsible Curator]]: ^^^Satoshi Kaneko^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH79'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH79.html
|}
</div>


== Substrate specificities ==
Family GH79 enzymes are found widely distributed in bacteria and eukaryota including fungi, plants, and animals. The characterized activities of this family include β-glucuronidase (EC [{{EClink}}3.2.1.31 3.2.1.31]) <cite> Eudes2008 </cite>, β-4-''O''-methyl-glucuronidase (EC 3.2.1.-) <cite>Kuroyama2001</cite>, baicalin β-glucuronidase (EC [{{EClink}}3.2.1.167 3.2.1.167]) <cite> Sasaki2000 </cite>, heparanase (EC 3.2.1.166) <cite> Vlodavsky1999 Toyoshima1999 Kussie1999 Hulett1999 Fairbanks1999 </cite> and hyaluronidase (EC 3.2.1.-) <cite> Nardella2004 </cite>. GH79s are involved in the metabolism of proteoglycans, such as heparan sulfate proteoglycan, chondroitin sulfate proteoglycan, and hyaluronan from animals and arabinogalactan-proteins from higher plants.

Some β-glucuronidases have been shown to release both glucuronic acid (GlcA) and 4-''O''-methyl-GlcA from arabinogalactan proteins <cite> Kuroyama2001 Konishi2008 </cite>. The ''Aspergillus niger'' enzyme shows high activity for 4-''O''-methyl-GlcA residues <cite> Kuroyama2001 </cite>. ''Scutellaria baicalensis'' β-glucuronidase hydrolyzes baicalein 7-''O''-β-glucuronide, which is a major flavone of ''S. baicalensis'' <cite> Sasaki2000 </cite>. Heparanase is an endo-β-glucuronidase that degrades the heparan sulfate side chains of heparan sulfate proteoglycans. Heparanases are found in mammals such as human, mouse (''Mus musculus''), rat (''Rattus norvegicus''), cattle (''Bos indicus''), and chicken (''Gallus gallus'').

== Kinetics and Mechanism ==
GH79 β-glucuronidases are retaining enzymes, as first demonstrated by proton-NMR studies of the hydrolysis of p-nitrophenyl β-glucuronide by a β-glucuronidase from ''Acidobacterium capsulatum'' <cite> Michikawa2012 </cite>.

== Catalytic Residues ==
The catalytic residues were first identified in the ''A. capsulatum'' β-glucuronidase as Glu173 (acid/base) and Glu287 (nucleophile) by trapping of the 2-fluoroglucuronyl-enzyme intermediate and site-directed mutagenesis studies <cite> Michikawa2012 </cite>.

== Three-dimensional structures ==
The three-dimensional structure of ''A. capsulatum'' β-glucuronidase solved using X-ray crystallography represented the first structure of an enzyme of GH79 (PDB IDs [{{PDBlink}}3vny 3vny], [{{PDBlink}}3vnz 3vnz], [{{PDBlink}}3vo0 3vo0]) <cite> Michikawa2012 </cite>. The catalytic domain of the enzyme is a (β/α)8 TIM-barrel fold as members of clan GH-A.

== Family Firsts ==
;First stereochemistry determination: ''Acidobacterium capsulatum'' β-glucuronidase by 1H-NMR <cite> Michikawa2012 </cite>.
;First catalytic nucleophile identification: ''A. capsulatum'' β-glucuronidase by 2-fluoroglucuroic acid labeling and the mutagenesis study <cite> Michikawa2012 </cite>.
;First general acid/base residue identification: ''A. capsulatum'' β-glucuronidase by structural identification and the mutagenesis study <cite> Michikawa2012 </cite>.
;First 3-D structure: ''A. capsulatum'' β-glucuronidase (PDB IDs [{{PDBlink}}3vny 3vny], [{{PDBlink}}3vnz 3vnz], [{{PDBlink}}3vo0 3vo0]) <cite> Michikawa2012 </cite>.

== References ==
<biblio>
#Eudes2008 pmid=18667448
#Kuroyama2001 pmid=11423108
#Konishi2008 pmid=18377882
#Sasaki2000 pmid=10858442
#Michikawa2012 Michikawa M, Ichinose H, Momma M, Biely P, Jongkees S, Yoshida M, Kotake T, Tsumuraya Y, Withers S, Fujimoto Z, Kaneko S. ''Structural and biochemical characterization of glycoside hydrolase family 79 β-glucuronidase from Acidobacterium capsulatum.'' J. Biol. Chem. in press. //''Note: Due to a problem with PubMed data, this reference is not automatically formatted. Please see these links out:'' [http://dx.doi.org/10.1074/jbc.M112.346288 DOI:10.1074/jbc.M112.346288] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=22367201 PMID: 22367201]
#Vlodavsky1999 pmid=10395325
#Toyoshima1999 pmid=10446189
#Kussie1999 pmid=10405343
#Hulett1999 pmid=10395326
#Fairbanks1999 pmid=10514423
#Nardella2004 pmid=14967027
</biblio>

[[Category:Glycoside Hydrolase Families|GH079]]

User:Hitomi Ichinose

2012-03-16T11:33:57Z

Hitomi Ichinose:

Hitomi Ichinose is a postdoctoral fellow in the National Food Research Institute (NFRI), National Agriculture and Food Research Organization, Japan.
She obtained her BSc degree in science from Rikkyo (St. Paul’s) University in Tokyo (1999). She moved to Tsukuba, and she started working on GHs in the group of Dr. Satoshi Kaneko (2000).
She joined the group (2000-2012), working on hemicellulases such as arabinogalactan-proteins, arabinan, and xylan-degrading enzymes.
She obtained PhD degree from Graduate School of Science in the Rikkyo University (2012). She contributed to finding and characterization of beta-L-arabinopyranosidase (GH27) <cite> Ichinose2009 </cite>, and also contributed to characterization of endo-beta-1,6-galactanase (GH30) <cite> Ichinose2008 </cite> and exo-beta-1,3-galactanase (GH43) <cite> Ichinose2005 </cite>.

----
<biblio>
#Ichinose2009 pmid=19608743
#Ichinose2008 pmid=18310439
#Ichinose2005 pmid=15866877
</biblio>

Glycoside Hydrolase Family 79

2012-03-06T13:00:12Z

Hitomi Ichinose:

{{UnderConstruction}}
* [[Author]]: ^^^Hitomi Ichinose^^^ and ^^^Satoshi Kaneko^^^
* [[Responsible Curator]]: ^^^Satoshi Kaneko^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH79'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH79.html
|}
</div>


== Substrate specificities ==
Family GH79 enzymes are found widely distributed in bacteria and eukaryota including fungi, plants, and animals. The characterized activities of this family include β-glucuronidase (E.C. 3.2.1.31) <cite> Eudes2008 </cite>, β-4-''O''-methyl-glucuronidase (E.C. 3.2.1.-) <cite> Kuroyama2001 </cite>, baicalin β-glucuronidase (E.C. 3.2.1.167) <cite> Sasaki2000 </cite>, heparanase (E.C. 3.2.1.-) <cite> Vlodavsky1999 Toyoshima1999 Kussie1999 Hulett1999 Fairbanks1999 </cite> and hyaluronidase (E.C. 3.2.1.-) <cite> Nardella2004 </cite>. GH79s are involved in the metabolism of proteoglycans, such as heparan sulfate proteoglycan, chondroitin sulfate proteoglycan, and hyaluronan from animals and arabinogalactan-proteins from higher plants.
Some β-glucuronidases have been shown to release both glucuronic acid (GlcA) and 4-''O''-methyl-GlcA from arabinogalactan proteins <cite> Kuroyama2001 Konishi2008 </cite>. The ''Aspergillus niger'' enzyme shows high activity for 4-''O''-methyl-GlcA residues <cite> Kuroyama2001 </cite>. ''Scutellaria baicalensis'' β-glucuronidase hydrolyzes baicalein 7-''O''-β-glucuronide, which is a major flavone of ''S. baicalensis'' <cite> Sasaki2000 </cite> Heparanase is an endo-β-glucuronidase that degrades heparan sulfate side chains of heparan sulfate proteoglycans. Heparanases are found in mammals such as human, mouse (''Mus musculus''), rat (''Rattus norvegicus''), cattle (''Bos indicus''), and chicken (''Gallus gallus'').

== Kinetics and Mechanism ==
GH79 β-glucuronidases are retaining enzymes, as first demonstrated by proton-NMR studies of the hydrolysis of p-nitrophenyl β-glucuronide by a β-glucuronidase from ''Acidobacterium capsulatum'' <cite> Michikawa2012 </cite>.

== Catalytic Residues ==
The catalytic residues were first identified in the ''A. capsulatum'' β-glucuronidase as Glu173 (acid/base) and Glu287 (nucleophile) by trapping of the 2-fluoroglucuronyl-enzyme intermediate and the mutagenesis studies <cite> Michikawa2012 </cite>.

== Three-dimensional structures ==
The three-dimensional structure of ''A. capsulatum'' β-glucuronidase solved using X-ray crystallography represented the first structure of an enzyme of GH79 <cite> Michikawa2012 </cite>. The catalytic domain of the enzyme is a (β/α)8 TIM-barrel fold as members of clan GH-A.

== Family Firsts ==
;First stereochemistry determination: ''Acidobacterium capsulatum'' β-glucuronidase by 1H-NMR <cite> Michikawa2012 </cite>.
;First catalytic nucleophile identification: ''A. capsulatum'' β-glucuronidase by 2-fluoroglucuroic acid labeling and the mutagenesis study <cite> Michikawa2012 </cite>.
;First general acid/base residue identification: ''A. capsulatum'' β-glucuronidase by structural identification and the mutagenesis study <cite> Michikawa2012 </cite>.
;First 3-D structure: ''A. capsulatum'' β-glucuronidase <cite> Michikawa2012 </cite>.

== References ==
<biblio>
#Eudes2008 pmid=18667448
#Kuroyama2001 pmid=11423108
#Konishi2008 pmid=18377882
#Sasaki2000 pmid=10858442
#Michikawa2012 (2012) Michikawa M, Ichinose H, Mitsuru M, Peter Biely, Seino Jongkees, Makoto Yoshida, Toshihisa Kotake, Yoichi Tsumuraya, Stephen Withers, Zui Fujimoto, and Satoshi Kaneko. Structural and biochemical characterization of glycoside hydrolase family 79 β-glucuronidase from Acidobacterium capsulatum. J Biol Chem. in press.
#Vlodavsky1999 pmid=10395325
#Toyoshima1999 pmid=10446189
#Kussie1999 pmid=10405343
#Hulett1999 pmid=10395326
#Fairbanks1999 pmid=10514423
#Nardella2004 pmid=14967027
</biblio>

[[Category:Glycoside Hydrolase Families|GH079]]

Glycoside Hydrolase Family 79

2012-03-02T03:02:55Z

Hitomi Ichinose:

{{UnderConstruction}}
* [[Author]]: ^^^Satoshi Kaneko^^^
* [[Responsible Curator]]: ^^^Satoshi Kaneko^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH79'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH79.html
|}
</div>


== Substrate specificities ==
Family GH79 enzymes are found widely distributed in bacteria and eukaryota including fungi, plants, and animals. The characterized activities of this family include β-glucuronidase (E.C. 3.2.1.31) <cite> Eudes2008 </cite>, β-4-O-methyl-glucuronidase (E.C. 3.2.1.-) <cite> Kuroyama2001 </cite>, baicalin β-glucuronidase (E.C. 3.2.1.167) <cite> Sasaki2000 </cite>, heparanase (E.C. 3.2.1.-) <cite> Vlodavsky1999 Toyoshima1999 Kussie1999 Hulett1999 Fairbanks1999 </cite> and hyaluronidase (E.C. 3.2.1.-). GH79s are involved in the metabolism of proteoglycans, such as heparan sulfate proteoglycan, chondroitin sulfate proteoglycan, and hyaluronan from animals and arabinogalactan-proteins from higher plants.
Some β-glucuronidases have been shown to release both glucuronic acid (GlcA) and 4-O-methyl-GlcA from arabinogalactan proteins <cite> Kuroyama2001 Konishi2008 </cite>. The Aspergillus niger enzyme shows high activity for 4-O-methyl-GlcA residues <cite> Kuroyama2001 </cite>. Scutellaria baicalensis β-glucuronidase hydrolyzes baicalein 7-O-β-glucuronide, which is a major flavone of S. baicalensis <cite> Sasaki2000 </cite> Heparanase is an endo-β-glucuronidase that degrades heparan sulfate side chains of heparan sulfate proteoglycans. Heparanases are found in mammals such as human, mouse (Mus musculus), rat (Rattus norvegicus), cattle (Bos indicus), and chicken (Gallus gallus).

== Kinetics and Mechanism ==
GH79 β-glucuronidases are retaining enzymes, as first demonstrated by proton-NMR studies of the hydrolysis of p-nitrophenyl β-glucuronide by a β-glucuronidase from Acidobacterium capsulatum <cite> Michikawa2012 </cite>.

== Catalytic Residues ==
The catalytic residues were first identified in the A. capsulatum β-glucuronidase as Glu173 (acid/base) and Glu287 (nucleophile) by trapping of the 2-fluoroglucuronyl-enzyme intermediate and the mutagenesis studies <cite> Michikawa2012 </cite>.

== Three-dimensional structures ==
The three-dimensional structure of A. capsulatum β-glucuronidase solved using X-ray crystallography represented the first structure of an enzyme of GH79 <cite> Michikawa2012 </cite>. The catalytic domain of the enzyme is a (β/α)8 TIM-barrel fold as members of clan GH-A.

== Family Firsts ==
;First stereochemistry determination: Acidobacterium capsulatum β-glucuronidase by 1H-NMR <cite> Michikawa2012 </cite>.
;First catalytic nucleophile identification: A. capsulatum β-glucuronidase by 2-fluoroglucuroic acid labeling and the mutagenesis study <cite> Michikawa2012 </cite>.
;First general acid/base residue identification: A. capsulatum β-glucuronidase by structural identification and the mutagenesis study <cite> Michikawa2012 </cite>.
;First 3-D structure: A. capsulatum β-glucuronidase <cite> Michikawa2012 </cite>.

== References ==
<biblio>
#Eudes2008 pmid=18667448
#Kuroyama2001 pmid=11423108
#Konishi2008 pmid=18377882
#Sasaki2000 pmid=10858442
#Michikawa2012 (2012) Michikawa M, Ichinose H, Mitsuru M, Peter Biely, Seino Jongkees, Makoto Yoshida, Toshihisa Kotake, Yoichi Tsumuraya, Stephen Withers, Zui Fujimoto, and Satoshi Kaneko. Structural and biochemical characterization of glycoside hydrolase family 79 β-glucuronidase from Acidobacterium capsulatum. J Biol Chem. in press.
#Vlodavsky1999 pmid=10395325
#Toyoshima1999 pmid=10446189
#Kussie1999 pmid=10405343
#Hulett1999 pmid=10395326
#Fairbanks1999 pmid=10514423
</biblio>

[[Category:Glycoside Hydrolase Families|GH079]]

Glycoside Hydrolase Family 79

2012-03-02T02:03:08Z

Hitomi Ichinose:

{{UnderConstruction}}
* [[Author]]: ^^^Satoshi Kaneko^^^
* [[Responsible Curator]]: ^^^Satoshi Kaneko^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH79'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH79.html
|}
</div>


== Substrate specificities ==
Family GH79 enzymes are found widely distributed in bacteria and eukaryota including fungi, plants, and animals. The characterized activities of this family include β-glucuronidase (E.C. 3.2.1.31) <cite> Eudes2008 </cite>, β-4-O-methyl-glucuronidase (E.C. 3.2.1.-) <cite> Kuroyama2001 </cite>, baicalin β-glucuronidase (E.C. 3.2.1.167) <cite> Sasaki2000 </cite>, heparanase (E.C. 3.2.1.-) <cite> Vlodavsky1999 Toyoshima1999 Kussie1999 Hulett1999 Fairbanks1999 </cite> and hyaluronidase (E.C. 3.2.1.-).GH79s are involved in the metabolism of proteoglycans, such as heparan sulfate proteoglycan, chondroitin sulfate proteoglycan, and hyaluronan from animals and arabinogalactan-proteins from higher plants.
Some β-glucuronidases have been shown to release both glucuronic acid (GlcA) and 4-O-methyl-GlcA from arabinogalactan proteins <cite> Kuroyama2001 Konishi2008 </cite>. The Aspergillus niger enzyme shows high activity for 4-O-methyl-GlcA residues <cite> Kuroyama2001 </cite>. Scutellaria baicalensis β-glucuronidase hydrolyzes baicalein 7-O-β-glucuronide, which is a major flavone of S. baicalensis <cite> Sasaki2000 </cite> Heparanase is an endo-β-glucuronidase that degrades heparan sulfate side chains of heparan sulfate proteoglycans. Heparanases are found in mammals such as human, mouse (Mus musculus), rat (Rattus norvegicus), cattle (Bos indicus), and chicken (Gallus gallus). At present, only one heparanase is found in mammals.

== Kinetics and Mechanism ==
GH79 β-glucuronidases are retaining enzymes, as first demonstrated by proton-NMR studies of the hydrolysis of p-nitrophenyl β-glucuronide by a β-glucuronidase from Acidobacterium capsulatum <cite> Michikawa2012 </cite>.

== Catalytic Residues ==
The catalytic residues were first identified in the A. capsulatum β-glucuronidase as Glu173 (acid/base) and Glu287 (nucleophile) by trapping of the 2-fluoroglucuronyl-enzyme intermediate and the mutagenesis studies <cite> Michikawa2012 </cite>.

== Three-dimensional structures ==
The three-dimensional structure of A. capsulatum β-glucuronidase solved using X-ray crystallography represented the first structure of an enzyme of GH79 <cite> Michikawa2012 </cite>. The catalytic domain of the enzyme is a (β/α)8 TIM-barrel fold as members of clan GH-A.

== Family Firsts ==
;First stereochemistry determination: Acidobacterium capsulatum β-glucuronidase by 1H-NMR <cite> Michikawa2012 </cite>.
;First catalytic nucleophile identification: A. capsulatum β-glucuronidase by 2-fluoroglucuroic acid labeling and the mutagenesis study <cite> Michikawa2012 </cite>.
;First general acid/base residue identification: A. capsulatum β-glucuronidase by structural identification and the mutagenesis study <cite> Michikawa2012 </cite>.
;First 3-D structure: A. capsulatum β-glucuronidase <cite> Michikawa2012 </cite>.

== References ==
<biblio>
#Eudes2008 pmid=18667448
#Kuroyama2001 pmid=11423108
#Konishi2008 pmid=18377882
#Sasaki2000 pmid=10858442
#Michikawa2012 (2012) Michikawa M, Ichinose H, Mitsuru M, Peter Biely, Seino Jongkees, Makoto Yoshida, Toshihisa Kotake, Yoichi Tsumuraya, Stephen Withers, Zui Fujimoto, and Satoshi Kaneko. Structural and biochemical characterization of glycoside hydrolase family 79 β-glucuronidase from Acidobacterium capsulatum. J Biol Chem. in press.
#Vlodavsky1999 pmid=10395325
#Toyoshima1999 pmid=10446189
#Kussie1999 pmid=10405343
#Hulett1999 pmid=10395326
#Fairbanks1999 pmid=10514423
</biblio>

[[Category:Glycoside Hydrolase Families|GH079]]

Glycoside Hydrolase Family 79

2012-03-02T00:35:05Z

Hitomi Ichinose:

{{UnderConstruction}}
* [[Author]]: ^^^Satoshi Kaneko^^^
* [[Responsible Curator]]: ^^^Satoshi Kaneko^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH79'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH79.html
|}
</div>


== Substrate specificities ==
Family GH79 enzymes are found widely distributed in bacteria and eukaryota including fungi, plants, and animals. The characterized activities of this family include β-glucuronidase (E.C. 3.2.1.31) <cite> Eudes2008 </cite>, β-4-O-methyl-glucuronidase (E.C. 3.2.1.-) <cite> Kuroyama2001 </cite>, baicalin β-glucuronidase (E.C. 3.2.1.167) <cite> Sasaki2000 </cite>, heparanase (E.C. 3.2.1.-) <cite> </cite> and hyaluronidase (E.C. 3.2.1.-) <cite> </cite>.
Some β-glucuronidase have been shown to release both glucuronic acid (GlcA) and 4-O-methyl-GlcA from arabinogalactan proteins <cite> Kuroyama2001 Konishi2008 </cite>. The Aspergillus niger enzyme shows high activity for 4-O-methyl-GlcA residues <cite> Kuroyama2001 </cite>. Scutellaria baicalensis β-glucuronidase hydrolyzes baicalein 7-O-β-glucuronide, which is a major flavone of S. baicalensis <cite> Sasaki2000 </cite>.

== Kinetics and Mechanism ==
GH79 β-glucuronidases are retaining enzymes, as first demonstrated by proton-NMR studies of the hydrolysis of p-nitrophenyl β-glucuronide by a β-glucuronidase from Acidobacterium capsulatum <cite> Michikawa2012 </cite>.

== Catalytic Residues ==
The catalytic residues were first identified in the A. capsulatum β-glucuronidase as Glu173 (acid/base) and Glu287 (nucleophile) by trapping of the 2-fluoroglucuronyl-enzyme intermediate and the mutagenesis studies <cite> Michikawa2012 </cite>.

== Three-dimensional structures ==
The three-dimensional structure of A. capsulatum β-glucuronidase solved using X-ray crystallography represented the first structure of an enzyme of GH79 <cite> Michikawa2012 </cite>. The catalytic domain of the enzyme is a (β/α)8 TIM-barrel fold as members of clan GH-A.

== Family Firsts ==
;First stereochemistry determination: Acidobacterium capsulatum β-glucuronidase by 1H-NMR <cite> Michikawa2012 </cite>.
;First catalytic nucleophile identification: A. capsulatum β-glucuronidase by 2-fluoroglucuroic acid labeling and the mutagenesis study <cite> Michikawa2012 </cite>.
;First general acid/base residue identification: A. capsulatum β-glucuronidase by structural identification and the mutagenesis study <cite> Michikawa2012 </cite>.
;First 3-D structure: A. capsulatum β-glucuronidase <cite> Michikawa2012 </cite>.

== References ==
<biblio>
#Eudes2008 pmid=18667448
#Kuroyama2001 pmid=11423108
#Konishi2008 pmid=18377882
#Sasaki2000 pmid=10858442
#Michikawa2012 (2012) Michikawa M, Ichinose H, Mitsuru M, Peter Biely, Seino Jongkees, Makoto Yoshida, Toshihisa Kotake, Yoichi Tsumuraya, Stephen Withers, Zui Fujimoto, and Satoshi Kaneko. Structural and biochemical characterization of glycoside hydrolase family 79 β-glucuronidase from Acidobacterium capsulatum. J Biol Chem. in press.

</biblio>

[[Category:Glycoside Hydrolase Families|GH079]]

User:Hitomi Ichinose

2012-03-02T00:29:31Z

Hitomi Ichinose: Created page with "Hitomi Ichinose is a postdoctoral fellow in the National Food Research Institute, National Agriculture and Food Research Organization, Japan. She joined the group of Dr. Satoshi ..."

Hitomi Ichinose is a postdoctoral fellow in the National Food Research Institute, National Agriculture and Food Research Organization, Japan. She joined the group of Dr. Satoshi Kaneko (2000-2012). She has been working on GHs, especially working on hemicellulases such as arabinogalactan-proteins, arabinan, and xylan-degrading enzymes.

Glycoside Hydrolase Family 79

2012-03-01T14:28:04Z

Hitomi Ichinose:

{{UnderConstruction}}
* [[Author]]: ^^^Satoshi Kaneko^^^
* [[Responsible Curator]]: ^^^Satoshi Kaneko^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH79'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH79.html
|}
</div>


== Substrate specificities ==
Family GH79 enzymes are found widely distributed in bacteria and eukaryota including fungi, plants, and animals. The characterized activities of this family include β-glucuronidase (E.C. 3.2.1.31) <cite> Eudes2008 </cite>, β-4-O-methyl-glucuronidase (E.C. 3.2.1.-) <cite> Kuroyama2001 </cite>, baicalin β-glucuronidase (E.C. 3.2.1.167) <cite> Sasaki2000 </cite>, heparanase (E.C. 3.2.1.-) and hyaluronidase (E.C. 3.2.1.-).
Some β-glucuronidase have been shown to release both glucuronic acid (GlcA) and 4-O-methyl-GlcA from arabinogalactan proteins. The Aspergillus niger enzyme shows high activity for 4-O-methyl-GlcA residues. Scutellaria baicalensis β-glucuronidase hydrolyzes baicalein 7-O-β-glucuronide, which is a major flavone of S. baicalensis.

== Kinetics and Mechanism ==
GH79 β-glucuronidases are retaining enzymes, as first demonstrated by proton-NMR studies of the hydrolysis of p-nitrophenyl β-glucuronide by a β-glucuronidase from Acidobacterium capsulatum <cite> Michikawa2012 </cite>.

== Catalytic Residues ==
The catalytic residues were first identified in the A. capsulatum β-glucuronidase as Glu173 (acid/base) and Glu287 (nucleophile) by trapping of the 2-fluoroglucuronyl-enzyme intermediate and the mutagenesis studies <cite> Michikawa2012 </cite>.

== Three-dimensional structures ==
The three-dimensional structure of A. capsulatum β-glucuronidase solved using X-ray crystallography represented the first structure of an enzyme of GH79 <cite> Michikawa2012 </cite>. The catalytic domain of the enzyme is a (β/α)8 TIM-barrel fold as members of clan GH-A.

== Family Firsts ==
;First stereochemistry determination: Acidobacterium capsulatum β-glucuronidase by 1H-NMR <cite> Michikawa2012 </cite>.
;First catalytic nucleophile identification: A. capsulatum β-glucuronidase by 2-fluoroglucuroic acid labeling and the mutagenesis study <cite> Michikawa2012 </cite>.
;First general acid/base residue identification: A. capsulatum β-glucuronidase by structural identification and the mutagenesis study <cite> Michikawa2012 </cite>.
;First 3-D structure: A. capsulatum β-glucuronidase <cite> Michikawa2012 </cite>.

== References ==
<biblio>
#Eudes2008 pmid=18667448
#Kuroyama2001 pmid=11423108
#Konishi2008 pmid=18377882
#Sasaki2000 pmid=10858442
#Michikawa2012 (2012) Michikawa M, Ichinose H, Mitsuru M, Peter Biely, Seino Jongkees, Makoto Yoshida, Toshihisa Kotake, Yoichi Tsumuraya, Stephen Withers, Zui Fujimoto, and Satoshi Kaneko. Structural and biochemical characterization of glycoside hydrolase family 79 β-glucuronidase from Acidobacterium capsulatum. J Biol Chem. in press.
</biblio>

[[Category:Glycoside Hydrolase Families|GH079]]