CAZypedia - User contributions [en-ca]

Glycoside Hydrolase Family 74

2011-05-09T04:17:37Z

Katsuro Yaoi:

{{CuratorApproved}}
* [[Author]]: ^^^Katsuro Yaoi^^^ and ^^^Takuya Ishida^^^
* [[Responsible Curator]]: ^^^Katsuro Yaoi^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH74'''
|-
|'''Clan'''
|none, 7-fold β-propeller
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/GH74.html
|}
</div>


== Substrate specificities ==
Glycoside hydrolases of this family hydrolyze β-1,4-linkages of various glucans. With the exception of Cel74 from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=2336 ''Thermotoga maritima''], all biochemically characterized enzymes are specific toward xyloglucans and/or xyloglucan-oligosaccharides. Cel74 from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=2336 ''Thermotoga maritima''] exhibits the highest activity on barley β-glucan, with relative activity of 20% toward xyloglucan <cite>Chhabra2002</cite>. A wide diversity in the modes of action by GH74 enzymes has been reported. "Oligoxyloglucan reducing end-specific cellobiohydrolase (OXG-RCBH, EC [{{EClink}}3.2.1.150 3.2.1.150])" from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=203496 ''Geotrichum sp. M128''] <cite>Yaoi2002</cite> and "oligoxyloglucan reducing end-specific xyloglucanobiohydrolase (OREX)" from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=162425 ''Emericella nidulans''] (formerly known as ''Aspergillus nidulans'') <cite>Bauer2005</cite> are active on only xyloglucan oligosaccharides and have essentially no ability to degrade xyloglucan polysaccharides. They release oligosaccharides with two glucose units from non-reducing end of xyloglucan oligosaccharides. On the other hand, GH74 enzymes designated as xyloglucanase; xyloglucan specific endo-β-1,4-glucanases: XEG; and xyloglucan hydrolases: Xgh, (EC [{{EClink}}3.2.1.151 3.2.1.151]), exhibit endo-type activity on xyloglucan from tamarind seed, a readily available and well-investigated xyloglucan <cite>York1993</cite>. Many GH74 xyloglucanases hydrolyze the glycosidic linkage of unbranched glucose residues, but several members including ''Geotrichum sp.'' OXG-RCBH <cite>Yaoi2002</cite>, ''E. nidulans'' OREX <cite>Bauer2005</cite>, and [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=51453''Hypocrea jecorina''] (formerly known as ''Trichoderma reesei'') Cel74A <cite>Desmet2007</cite> accommodate side-chain xylose residues at [[Sub-site nomenclature|subsite]] -1 of the active site.

== Kinetics and Mechanism ==
Family 74 enzymes are [[inverting]] enzymes, as shown by NMR analysis on Xeg74 from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=2021 ''Thermobifida fusca''] <cite>Irwin2003</cite>.

== Catalytic Residues ==
Crystal structure of OXG-RCBH demonstrated that Asp35 and Asp465 are located in the middle of the binding cleft, and its crucial roles in hydrolytic activity were experimentally confirmed by site-directed mutagenesis <cite>Yaoi2004b</cite>. The corresponding Asp residues in [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?id=1515 ''Clostridium thermocellum''] xyloglucanase are nicely located between [[Sub-site nomenclature|subsites]] -1 and +1 in the complex structure with xyloglucan-derived oligosaccharides <cite>Martinez-Fleites2006</cite>.

== Three-dimensional structures ==
Overall structures of GH74 enzymes consist of a tandem repeat of two seven-bladed β-propeller domains. The two domains form a substrate binding cleft at the interface. The catalytic residues are located in the middle of this cleft. One side of the binding cleft of OXG-RCBH is blocked by a so-called 'exo-loop' which is found only in exo-acting enzymes in this family <cite>Yaoi2004b</cite>. A crystal structure of a complex with xyloglucan-derived oligosaccharides elucidated the interaction with the side-chains of the substrate by these enzymes <cite>Martinez-Fleites2006</cite>.

== Family Firsts ==
;First stereochemistry determination:Xeg74 from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=2021 ''Thermobifida fusca''] by <sup>1</sup>H-NMR <cite>Irwin2003</cite>.
;First gene cloning:AviIII from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=5053 ''Aspergillus aculeatus''] <cite>Takada1999</cite> and EglC from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=5061 ''Aspergillus niger''] <cite>Hasper2002</cite>.
;First general acid residue identification: OXG-RCBH from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=203496 ''Geotrichum sp. M128''] <cite>Yaoi2004</cite>.
;First general base residue identification: OXG-RCBH from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=203496 ''Geotrichum sp. M128''] <cite>Yaoi2004</cite>.
;First 3-D structure: OXG-RCBH from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=203496 ''Geotrichum sp. M128''] <cite>Yaoi2004</cite>.

== References ==
<biblio>
#Hasper2002 pmid=11916668
#Yaoi2002 pmid=12374797
#Irwin2003 pmid=12846842
#Yaoi2004 pmid=15242597
#Martinez-Fleites2006 pmid=16772298
#York1993 pmid=8252539
#Desmet2007 pmid=17229143
#Bauer2005 pmid=16214120
#Chhabra2002 pmid=12417345
#Takada1999 Takada G, Kawagushi T, Yoneda T, Kawasaki M, Sumitani JI, and Arai M. ''Molecular cloning and expression of the celluloytic system of Aspergillus aculeatus'', p. 364-373. ''In'' Ohmiya K, Hayashi K, Sakka K, Kobayashi Y, Karita S, and Kimura T (ed.), ''Genetics, biochemistry and ecology of cellulose degradation.'' 1999 Uni Publishers, Tokyo, Japan, ISBN 4-946450-17-3.
</biblio>

[[Category:Glycoside Hydrolase Families|GH074]]

Glycoside Hydrolase Family 74

2011-05-09T02:23:09Z

Katsuro Yaoi:

{{UnderConstruction}}
* [[Author]]: ^^^Katsuro Yaoi^^^ and ^^^Takuya Ishida^^^
* [[Responsible Curator]]: ^^^Katsuro Yaoi^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH74'''
|-
|'''Clan'''
|none, 7-fold β-propeller
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/GH74.html
|}
</div>


== Substrate specificities ==
Glycoside hydrolases of this family hydrolyze β-1,4-linkages of various glucans. With the exception of Cel74 from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=2336 ''Thermotoga maritima''], all biochemically characterized enzymes are specific toward xyloglucans and/or xyloglucan-oligosaccharides. Cel74 from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=2336 ''Thermotoga maritima''] exhibits the highest activity on barley β-glucan, with relative activity of 20% toward xyloglucan <cite>Chhabra2002</cite>. A wide diversity in the modes of action by GH74 enzymes has been reported. "Oligoxyloglucan reducing end-specific cellobiohydrolase (OXG-RCBH, EC [{{EClink}}3.2.1.150 3.2.1.150])" from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=203496 ''Geotrichum sp. M128''] <cite>Yaoi2002</cite> and "oligoxyloglucan reducing end-specific xyloglucanobiohydrolase (OREX)" from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=162425 ''Emericella nidulans''] (formerly known as ''Aspergillus nidulans'') <cite>Bauer2005</cite> are active on only xyloglucan oligosaccharides and have essentially no ability to degrade xyloglucan polysaccharides. They release oligosaccharides with two glucose units from non-reducing end of xyloglucan oligosaccharides. On the other hand, GH74 enzymes designated as xyloglucanase; xyloglucan specific endo-β-1,4-glucanases: XEG; and xyloglucan hydrolases: Xgh, (EC [{{EClink}}3.2.1.151 3.2.1.151]), exhibit endo-type activity on xyloglucan from tamarind seed, a readily available and well-investigated xyloglucan <cite>York1993</cite>. Many GH74 xyloglucanases hydrolyze the glycosidic linkage of unbranched glucose residues, but several members including ''Geotrichum sp.'' OXG-RCBH <cite>Yaoi2002</cite>, ''E. nidulans'' OREX <cite>Bauer2005</cite>, and [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=51453''Hypocrea jecorina''] (formerly known as ''Trichoderma reesei'') Cel74A <cite>Desmet2007</cite> accommodate side-chain xylose residues at [[Sub-site nomenclature|subsite]] -1 of the active site.

== Kinetics and Mechanism ==
Family 74 enzymes are [[inverting]] enzymes, as shown by NMR analysis on Xeg74 from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=2021 ''Thermobifida fusca''] <cite>Irwin2003</cite>.

== Catalytic Residues ==
Crystal structure of OXG-RCBH demonstrated that Asp35 and Asp465 are located in the middle of the binding cleft, and its crucial roles in hydrolytic activity were experimentally confirmed by site-directed mutagenesis <cite>Yaoi2004b</cite>. The corresponding Asp residues in [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?id=1515 ''Clostridium thermocellum''] xyloglucanase are nicely located between [[Sub-site nomenclature|subsites]] -1 and +1 in the complex structure with xyloglucan-derived oligosaccharides <cite>Martinez-Fleites2006</cite>.

== Three-dimensional structures ==
Overall structures of GH74 enzymes consist of a tandem repeat of two seven-bladed β-propeller domains. The two domains form a substrate binding cleft at the interface. The catalytic residues are located in the middle of this cleft. One side of the binding cleft of OXG-RCBH is blocked by a so-called 'exo-loop' which is found only in exo-acting enzymes in this family <cite>Yaoi2004b</cite>. A crystal structure of a complex with xyloglucan-derived oligosaccharides elucidated the interaction with the side-chains of the substrate by these enzymes <cite>Martinez-Fleites2006</cite>.

== Family Firsts ==
;First stereochemistry determination:Xeg74 from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=2021 ''Thermobifida fusca''] by <sup>1</sup>H-NMR <cite>Irwin2003</cite>.
;First gene cloning:AviIII from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=5053 ''Aspergillus aculeatus''] <cite>Takada1999</cite> and EglC from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=5061 ''Aspergillus niger''] <cite>Hasper2002</cite>.
;First general acid residue identification: OXG-RCBH from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=203496 ''Geotrichum sp. M128''] <cite>Yaoi2004</cite>.
;First general base residue identification: OXG-RCBH from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=203496 ''Geotrichum sp. M128''] <cite>Yaoi2004</cite>.
;First 3-D structure: OXG-RCBH from [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=203496 ''Geotrichum sp. M128''] <cite>Yaoi2004</cite>.

== References ==
<biblio>
#Hasper2002 pmid=11916668
#Yaoi2002 pmid=12374797
#Irwin2003 pmid=12846842
#Yaoi2004 pmid=15242597
#Martinez-Fleites2006 pmid=16772298
#York1993 pmid=8252539
#Desmet2007 pmid=17229143
#Bauer2005 pmid=16214120
#Chhabra2002 pmid=12417345
#Takada1999 Takada G, Kawagushi T, Yoneda T, Kawasaki M, Sumitani JI, and Arai M. ''Molecular cloning and expression of the celluloytic system of Aspergillus aculeatus'', p. 364-373. ''In'' Ohmiya K, Hayashi K, Sakka K, Kobayashi Y, Karita S, and Kimura T (ed.), ''Genetics, biochemistry and ecology of cellulose degradation.'' 1999 Uni Publishers, Tokyo, Japan, ISBN 4-946450-17-3.
</biblio>

[[Category:Glycoside Hydrolase Families|GH074]]

User:Katsuro Yaoi

2010-05-27T01:23:44Z

Katsuro Yaoi:

[[Image:yaoi.JPG|right]]

Katsuro Yaoi is a senior research scientist at National Institute of Advanced Industrial Science and Technology (AIST) in Japan.
He received his academic training in Tokyo University of Agriculture and Technology. He finished his graduate work with M.S. (1996) and Ph.D. (1999) degrees. He did his postdoctoral work at the same laboratory (1999-2001). In 2001, he moved to AIST. His major interest is understanding the mode of action of GH74 xyloglucan hydrolases <cite>REF1 REF2 REF3</cite> (for which [[GH74]] has been created).

He loves baseball, and his son and daughter belong to a little league baseball team. Their dreams are playing in the Little League World Series in Williamsport, USA.
----
<biblio>
#REF1 pmid=15242597
#REF2 pmid=17498741
#REF3 pmid=19682300

</biblio>

[[Category:Contributors|Yaoi, Katsuro]]

User:Katsuro Yaoi

2010-05-24T06:36:20Z

Katsuro Yaoi:

[[Image:yaoi.JPG|right]]

Katsuro Yaoi is a senior researcher at National Institute of Advanced Industrial Science and Technology (AIST) in Japan.
He received his academic training in Tokyo University of Agriculture and Technology. He finished his graduate work with M.S. (1996) and Ph.D. (1999) degrees. He did his postdoctoral work at the same laboratory (1999-2001). In 2001, he moved to AIST. His major interest is understanding the mode of action of GH74 xyloglucan hydrolases <cite>REF1</cite><cite>REF2</cite><cite>REF3</cite>(for which [[GH74]] has been created).

He loves baseball, and his son and daughter belong to a little league baseball team. Their dreams are playing in the Little League World Series in Williamsport, USA.
----
<biblio>
#REF1 pmid= 15242597
#REF2 pmid=17498741
#REF3 pmid= 19682300

</biblio>

[[Category:Contributors|Yaoi, Katsuro]]

User:Katsuro Yaoi

2010-05-24T05:26:19Z

Katsuro Yaoi:

[[Image:yaoi.JPG|right]]

Katsuro Yaoi is a senior researcher at National Institute of Advanced Industrial Science and Technology (AIST) in Japan.
He received his academic training in Tokyo University of Agriculture and Technology. He finished his graduate work with M.S. (1996) and Ph.D. (1999) degrees. He did his postdoctoral work at the same laboratory (1999-2001). In 2001, he moved to AIST. His major interest is understanding the mode of action of GH74 xyloglucan hydrolases <cite>REF1</cite><cite>REF2</cite><cite>REF3</cite>(for which [[GH74]] has been created).

He loves baseball, and his son and daughter belong to a little league baseball team. Their dreams are to participate in the Little League World Series in Williamsport, USA!!
----
<biblio>
#REF1 pmid= 15242597
#REF2 pmid=17498741
#REF3 pmid= 19682300

</biblio>

[[Category:Contributors|Yaoi, Katsuro]]

Glycoside Hydrolase Family 74

2010-05-24T02:15:18Z

Katsuro Yaoi:

User:Katsuro Yaoi

2010-05-24T01:58:43Z

Katsuro Yaoi:

[[Image:yaoi.JPG|right]]

Katsuro Yaoi is a senior researcher at National Institute of Advanced Industrial Science and Technology (AIST) in Japan.
He received his academic training in Tokyo University of Agriculture and Technology. He finished his graduate work with M.S. (1996) and Ph.D. (1999) degrees. He did his postdoctoral work at the same laboratory (1999-2001). In 2001, he moved to AIST. His major interests are understanding the mode of action of xyloglucan hydrolases <cite>REF1</cite><cite>REF2</cite><cite>REF3</cite>(for which [[GH74]] has been created), and kids' little league baseball in weekend.
----
<biblio>
#REF1 pmid= 15242597
#REF2 pmid=17498741
#REF3 pmid= 19682300

</biblio>

[[Category:Contributors|Yaoi, Katsuro]]

File:Yaoi.JPG

2010-05-24T01:57:39Z

Katsuro Yaoi: uploaded a new version of "File:Yaoi.JPG"

Katsuro Yaoi

File:Yaoi.JPG

2010-05-24T01:51:11Z

Katsuro Yaoi: Katsuro Yaoi

Katsuro Yaoi

User:Katsuro Yaoi

2010-05-24T01:49:43Z

Katsuro Yaoi: Created page with 'Katsuro Yaoi is a senior researcher at National Institute of Advanced Industrial Science and Technology (AIST) in Japan. He received his academic training in Tokyo University of …'

Katsuro Yaoi is a senior researcher at National Institute of Advanced Industrial Science and Technology (AIST) in Japan.
He received his academic training in Tokyo University of Agriculture and Technology. He finished his graduate work with M.S. (1996) and Ph.D. (1999) degrees. He did his postdoctoral work at the same laboratory (1999-2001). In 2001, he moved to AIST. His major interests are understanding the mode of action of xyloglucan hydrolases <cite>REF1</cite><cite>REF2</cite><cite>REF3</cite>(for which [[GH74]] has been created), and kids' little league baseball in weekend.
----
<biblio>
#REF1 pmid= 15242597
#REF2 pmid=17498741
#REF3 pmid= 19682300

</biblio>

[[Category:Contributors|Yaoi, Katsuro]]