CAZypedia - User contributions [en-ca]

Glycoside Hydrolase Family 63

2013-04-08T11:18:34Z

Takashi Tonozuka:

{{CuratorApproved}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of GH63 are exo-acting α-glucosidases. Eukaryotic members of this family are processing α-glucosidase I enzymes (mannosyl-oligosaccharide glucosidase, EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyze the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2, to produce β-glucose and Glc2Man9GlcNAc2. Processing α-glucosidase I thus plays a critical role in the maturation of eukaryotic ''N''-glycans. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been intensively studied <cite>Dhanawansa2002</cite> (also reviewed in <cite>Herscovics1999</cite>).

Genes encoding GH63 enzymes have also been found in archaea and bacteria, but their natural substrates are still unclear, as these organisms are not known to produce eukaryotic ''N''-linked oligosacharides. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, demonstrated the highest activity toward the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among the commercially available sugars tested, but the Km value for nigerose was substantially higher than that for other typical α-glucosidases <cite>Kurakata2008</cite>. In 2013, the substrates of GH63 enzymes from ''Thermus thermophilus'' HB27 and ''Rubrobacter radiotolerans'' RSPS-4 have been identified as α-D-mannopyranosyl-1,2-D-glycerate (mannosylglycerate) and α-D-glucopyranosyl-1,2-D-glycerate (glucosylglycerate) <cite>Alarico2013</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the catalytic (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of [[GH37]] and GH63, both of which belong to [[clan]] GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered to be a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurakata2008</cite>. Although both of the corresponding residues of [[GH15]], which belongs to [[clan]] GH-L, are identified as Glu residues, the positions of the catalytic residues of [[GH15]], [[GH37]], and GH63 are highly conserved <cite>Kurakata2008 Gibson2007</cite>.

== Three-dimensional structures ==
The crystal structures of the bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurakata2008</cite> ([http://www.cazy.org/GH63_structure.html multiple PDB entries]) and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of an (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of [[GH15]], [[GH37]], [[GH65]], and [[GH94]] <cite>Kurakata2008 Gibson2007</cite>. This similarity had been predicted on the basis of sequence comparison, before their crystal structures were available <cite>Stam2005</cite>. The first crystal structure of the eukaryotic processing α-glucosidase I ([{{PDBlink}}4j5t PDB 4j5t]) has been reported in 2013 <cite>Barker2013</cite>.

== Family Firsts ==
;First gene cloning: Human processing α-glucosidase I <cite>Kalz-Fuller1995</cite>.
;First stereochemistry determination: Processing α-glucosidase I from ''Saccharomyces cerevisiae'' (Cwh41p) <cite>Palcic1999</cite>.
;First general acid residue identification: Inferred from structural comparison <cite>Kurakata2008</cite>.
;First general base residue identification: Inferred from structural comparison <cite>Kurakata2008</cite>.
;First 3-D structure: ''Escherichia coli'' YgjK, an enzyme showing the highest activity for the α-1,3-glucosidic linkage of nigerose <cite>Kurakata2008</cite>.
;First 3-D structure of a eukaryotic GH63 enzyme: A transmembrane-deleted form of processing α-glucosidase I from ''Saccharomyces cerevisiae'' <cite>Barker2013</cite>.

== References ==
<biblio>
#Alarico2013 pmid=23273275
#Barker2013 pmid=23536181
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurakata2008 pmid=18586271
#Palcic1999 pmid=10619707
#Gibson2007 pmid=17455176
#Stam2005 pmid=16226731
#Kalz-Fuller1995 pmid=7635146
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2013-04-08T11:04:38Z

Takashi Tonozuka:

{{CuratorApproved}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of GH63 are exo-acting α-glucosidases. Eukaryotic members of this family are processing α-glucosidase I enzymes (mannosyl-oligosaccharide glucosidase, EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyze the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2, to produce β-glucose and Glc2Man9GlcNAc2. Processing α-glucosidase I thus plays a critical role in the maturation of eukaryotic ''N''-glycans. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been intensively studied <cite>Dhanawansa2002</cite> (also reviewed in <cite>Herscovics1999</cite>).

Genes encoding GH63 enzymes have also been found in archaea and bacteria, but their natural substrates are still unclear, as these organisms are not known to produce eukaryotic ''N''-linked oligosacharides. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, demonstrated the highest activity toward the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among the commercially available sugars tested, but the Km value for nigerose was substantially higher than that for other typical α-glucosidases <cite>Kurakata2008</cite>. In 2013, the substrates of GH63 enzymes from ''Thermus thermophilus'' HB27 and ''Rubrobacter radiotolerans'' RSPS-4 have been identified as α-D-mannopyranosyl-1,2-D-glycerate (mannosylglycerate) and α-D-glucopyranosyl-1,2-D-glycerate (glucosylglycerate) <cite>Alarico2013</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the catalytic (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of [[GH37]] and GH63, both of which belong to [[clan]] GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered to be a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurakata2008</cite>. Although both of the corresponding residues of [[GH15]], which belongs to [[clan]] GH-L, are identified as Glu residues, the positions of the catalytic residues of [[GH15]], [[GH37]], and GH63 are highly conserved <cite>Kurakata2008 Gibson2007</cite>.

== Three-dimensional structures ==
The crystal structures of the bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurakata2008</cite> ([http://www.cazy.org/GH63_structure.html multiple PDB entries]) and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of an (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of [[GH15]], [[GH37]], [[GH65]], and [[GH94]] <cite>Kurakata2008 Gibson2007</cite>. This similarity had been predicted on the basis of sequence comparison, before their crystal structures were available <cite>Stam2005</cite>.

== Family Firsts ==
;First gene cloning: Human processing α-glucosidase I <cite>Kalz-Fuller1995</cite>.
;First stereochemistry determination: Processing α-glucosidase I from ''Saccharomyces cerevisiae'' (Cwh41p) <cite>Palcic1999</cite>.
;First general acid residue identification: Inferred from structural comparison <cite>Kurakata2008</cite>.
;First general base residue identification: Inferred from structural comparison <cite>Kurakata2008</cite>.
;First 3-D structure: ''Escherichia coli'' YgjK, an enzyme showing the highest activity for the α-1,3-glucosidic linkage of nigerose <cite>Kurakata2008</cite>.
;First 3-D structure of a eukaryotic GH63 enzyme: A transmembrane-deleted form of processing α-glucosidase I from ''Saccharomyces cerevisiae'' <cite>Barker2013</cite>.

== References ==
<biblio>
#Alarico2013 pmid=23273275
#Barker2013 pmid=23536181
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurakata2008 pmid=18586271
#Palcic1999 pmid=10619707
#Gibson2007 pmid=17455176
#Stam2005 pmid=16226731
#Kalz-Fuller1995 pmid=7635146
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2013-04-08T10:33:57Z

Takashi Tonozuka:

{{CuratorApproved}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of GH63 are exo-acting α-glucosidases. Eukaryotic members of this family are processing α-glucosidase I enzymes (mannosyl-oligosaccharide glucosidase, EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyze the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2, to produce β-glucose and Glc2Man9GlcNAc2. Processing α-glucosidase I thus plays a critical role in the maturation of eukaryotic ''N''-glycans. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been intensively studied <cite>Dhanawansa2002</cite> (also reviewed in <cite>Herscovics1999</cite>).

Genes encoding GH63 enzymes have also been found in archaea and bacteria, but their natural substrates are still unclear, as these organisms are not known to produce eukaryotic ''N''-linked oligosacharides. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, demonstrated the highest activity toward the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among the commercially available sugars tested, but the Km value for nigerose was substantially higher than that for other typical α-glucosidases <cite>Kurakata2008</cite>. In 2013, the substrates of GH63 enzymes from ''Thermus thermophilus'' HB27 and ''Rubrobacter radiotolerans'' RSPS-4 have been identified as α-D-mannopyranosyl-1,2-D-glycerate (mannosylglycerate) and α-D-glucopyranosyl-1,2-D-glycerate (glucosylglycerate) <cite>Alarico2013</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the catalytic (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of [[GH37]] and GH63, both of which belong to [[clan]] GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered to be a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurakata2008</cite>. Although both of the corresponding residues of [[GH15]], which belongs to [[clan]] GH-L, are identified as Glu residues, the positions of the catalytic residues of [[GH15]], [[GH37]], and GH63 are highly conserved <cite>Kurakata2008 Gibson2007</cite>.

== Three-dimensional structures ==
The crystal structures of the bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurakata2008</cite> ([http://www.cazy.org/GH63_structure.html multiple PDB entries]) and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of an (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of [[GH15]], [[GH37]], [[GH65]], and [[GH94]] <cite>Kurakata2008 Gibson2007</cite>. This similarity had been predicted on the basis of sequence comparison, before their crystal structures were available <cite>Stam2005</cite>.

== Family Firsts ==
;First gene cloning: Human processing α-glucosidase I <cite>Kalz-Fuller1995</cite>.
;First stereochemistry determination: Processing α-glucosidase I from ''Saccharomyces cerevisiae'' (Cwh41p) <cite>Palcic1999</cite>.
;First general acid residue identification: Inferred from structural comparison <cite>Kurakata2008</cite>.
;First general base residue identification: Inferred from structural comparison <cite>Kurakata2008</cite>.
;First 3-D structure: ''Escherichia coli'' YgjK, an enzyme showing the highest activity for the α-1,3-glucosidic linkage of nigerose <cite>Kurakata2008</cite>.

== References ==
<biblio>
#Alarico2013 pmid=23273275
#Barker2013 pmid=23536181
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurakata2008 pmid=18586271
#Palcic1999 pmid=10619707
#Gibson2007 pmid=17455176
#Stam2005 pmid=16226731
#Kalz-Fuller1995 pmid=7635146
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2013-04-08T10:31:16Z

Takashi Tonozuka:

{{CuratorApproved}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of GH63 are exo-acting α-glucosidases. Eukaryotic members of this family are processing α-glucosidase I enzymes (mannosyl-oligosaccharide glucosidase, EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyze the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2, to produce β-glucose and Glc2Man9GlcNAc2. Processing α-glucosidase I thus plays a critical role in the maturation of eukaryotic ''N''-glycans. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been intensively studied <cite>Dhanawansa2002</cite> (also reviewed in <cite>Herscovics1999</cite>).

Genes encoding GH63 enzymes have also been found in archaea and bacteria, but their natural substrates are still unclear, as these organisms are not known to produce eukaryotic ''N''-linked oligosacharides. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, demonstrated the highest activity toward the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among the commercially available sugars tested, but the Km value for nigerose was substantially higher than that for other typical α-glucosidases <cite>Kurakata2008</cite>. In 2013, the substrates of GH63 enzymes from "Thermus thermophilus" HB27 and "Rubrobacter radiotolerans" RSPS-4 have been identified as α-D-mannopyranosyl-1,2-D-glycerate (mannosylglycerate) and α-D-glucopyranosyl-1,2-D-glycerate (glucosylglycerate) <cite>Alarico2013</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the catalytic (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of [[GH37]] and GH63, both of which belong to [[clan]] GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered to be a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurakata2008</cite>. Although both of the corresponding residues of [[GH15]], which belongs to [[clan]] GH-L, are identified as Glu residues, the positions of the catalytic residues of [[GH15]], [[GH37]], and GH63 are highly conserved <cite>Kurakata2008 Gibson2007</cite>.

== Three-dimensional structures ==
The crystal structures of the bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurakata2008</cite> ([http://www.cazy.org/GH63_structure.html multiple PDB entries]) and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of an (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of [[GH15]], [[GH37]], [[GH65]], and [[GH94]] <cite>Kurakata2008 Gibson2007</cite>. This similarity had been predicted on the basis of sequence comparison, before their crystal structures were available <cite>Stam2005</cite>.

== Family Firsts ==
;First gene cloning: Human processing α-glucosidase I <cite>Kalz-Fuller1995</cite>.
;First stereochemistry determination: Processing α-glucosidase I from ''Saccharomyces cerevisiae'' (Cwh41p) <cite>Palcic1999</cite>.
;First general acid residue identification: Inferred from structural comparison <cite>Kurakata2008</cite>.
;First general base residue identification: Inferred from structural comparison <cite>Kurakata2008</cite>.
;First 3-D structure: ''Escherichia coli'' YgjK, an enzyme showing the highest activity for the α-1,3-glucosidic linkage of nigerose <cite>Kurakata2008</cite>.

== References ==
<biblio>
#Alarico2013 pmid=23273275
#Barker2013 pmid=23536181
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurakata2008 pmid=18586271
#Palcic1999 pmid=10619707
#Gibson2007 pmid=17455176
#Stam2005 pmid=16226731
#Kalz-Fuller1995 pmid=7635146
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2013-04-08T10:26:29Z

Takashi Tonozuka:

{{CuratorApproved}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of GH63 are exo-acting α-glucosidases. Eukaryotic members of this family are processing α-glucosidase I enzymes (mannosyl-oligosaccharide glucosidase, EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyze the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2, to produce β-glucose and Glc2Man9GlcNAc2. Processing α-glucosidase I thus plays a critical role in the maturation of eukaryotic ''N''-glycans. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been intensively studied <cite>Dhanawansa2002</cite> (also reviewed in <cite>Herscovics1999</cite>).

Genes encoding GH63 enzymes have also been found in archaea and bacteria, but their natural substrates are still unclear, as these organisms are not known to produce eukaryotic ''N''-linked oligosacharides. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, demonstrated the highest activity toward the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among the commercially available sugars tested <cite>Kurakata2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the catalytic (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of [[GH37]] and GH63, both of which belong to [[clan]] GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered to be a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurakata2008</cite>. Although both of the corresponding residues of [[GH15]], which belongs to [[clan]] GH-L, are identified as Glu residues, the positions of the catalytic residues of [[GH15]], [[GH37]], and GH63 are highly conserved <cite>Kurakata2008 Gibson2007</cite>.

== Three-dimensional structures ==
The crystal structures of the bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurakata2008</cite> ([http://www.cazy.org/GH63_structure.html multiple PDB entries]) and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of an (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of [[GH15]], [[GH37]], [[GH65]], and [[GH94]] <cite>Kurakata2008 Gibson2007</cite>. This similarity had been predicted on the basis of sequence comparison, before their crystal structures were available <cite>Stam2005</cite>.

== Family Firsts ==
;First gene cloning: Human processing α-glucosidase I <cite>Kalz-Fuller1995</cite>.
;First stereochemistry determination: Processing α-glucosidase I from ''Saccharomyces cerevisiae'' (Cwh41p) <cite>Palcic1999</cite>.
;First general acid residue identification: Inferred from structural comparison <cite>Kurakata2008</cite>.
;First general base residue identification: Inferred from structural comparison <cite>Kurakata2008</cite>.
;First 3-D structure: ''Escherichia coli'' YgjK, an enzyme showing the highest activity for the α-1,3-glucosidic linkage of nigerose <cite>Kurakata2008</cite>.

== References ==
<biblio>
#Alarico2013 pmid=23273275
#Barker2013 pmid=23536181
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurakata2008 pmid=18586271
#Palcic1999 pmid=10619707
#Gibson2007 pmid=17455176
#Stam2005 pmid=16226731
#Kalz-Fuller1995 pmid=7635146
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2013-04-08T10:23:59Z

Takashi Tonozuka:

{{CuratorApproved}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of GH63 are exo-acting α-glucosidases. Eukaryotic members of this family are processing α-glucosidase I enzymes (mannosyl-oligosaccharide glucosidase, EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyze the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2, to produce β-glucose and Glc2Man9GlcNAc2. Processing α-glucosidase I thus plays a critical role in the maturation of eukaryotic ''N''-glycans. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been intensively studied <cite>Dhanawansa2002</cite> (also reviewed in <cite>Herscovics1999</cite>).

Genes encoding GH63 enzymes have also been found in archaea and bacteria, but their natural substrates are still unclear, as these organisms are not known to produce eukaryotic ''N''-linked oligosacharides. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, demonstrated the highest activity toward the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among the commercially available sugars tested <cite>Kurakata2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the catalytic (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of [[GH37]] and GH63, both of which belong to [[clan]] GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered to be a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurakata2008</cite>. Although both of the corresponding residues of [[GH15]], which belongs to [[clan]] GH-L, are identified as Glu residues, the positions of the catalytic residues of [[GH15]], [[GH37]], and GH63 are highly conserved <cite>Kurakata2008 Gibson2007</cite>.

== Three-dimensional structures ==
The crystal structures of the bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurakata2008</cite> ([http://www.cazy.org/GH63_structure.html multiple PDB entries]) and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of an (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of [[GH15]], [[GH37]], [[GH65]], and [[GH94]] <cite>Kurakata2008 Gibson2007</cite>. This similarity had been predicted on the basis of sequence comparison, before their crystal structures were available <cite>Stam2005</cite>.

== Family Firsts ==
;First gene cloning: Human processing α-glucosidase I <cite>Kalz-Fuller1995</cite>.
;First stereochemistry determination: Processing α-glucosidase I from ''Saccharomyces cerevisiae'' (Cwh41p) <cite>Palcic1999</cite>.
;First general acid residue identification: Inferred from structural comparison <cite>Kurakata2008</cite>.
;First general base residue identification: Inferred from structural comparison <cite>Kurakata2008</cite>.
;First 3-D structure: ''Escherichia coli'' YgjK, an enzyme showing the highest activity for the α-1,3-glucosidic linkage of nigerose <cite>Kurakata2008</cite>.

== References ==
<biblio>
#Alarico2013 pmid=23273275
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurakata2008 pmid=18586271
#Palcic1999 pmid=10619707
#Gibson2007 pmid=17455176
#Stam2005 pmid=16226731
#Kalz-Fuller1995 pmid=7635146
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-28T11:05:17Z

Takashi Tonozuka:

{{CuratorApproved}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of GH63 are exo-acting α-glucosidases. Eukaryotic members of this family are processing α-glucosidase I enzymes (mannosyl-oligosaccharide glucosidase, EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyze the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2, to produce β-glucose and Glc2Man9GlcNAc2. Processing α-glucosidase I thus plays a critical role in the maturation of eukaryotic ''N''-glycans. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been intensively studied <cite>Dhanawansa2002</cite> (also reviewed in <cite>Herscovics1999</cite>).

Genes encoding GH63 enzymes have also been found in archaea and bacteria, but their natural substrates are still unclear, as these organisms are not known to produce eukaryotic ''N''-linked oligosacharides. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, demonstrated the highest activity toward the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among the commercially available sugars tested <cite>Kurakata2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the catalytic (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of [[GH37]] and GH63, both of which belong to [[clan]] GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered to be a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurakata2008</cite>. Although both of the corresponding residues of [[GH15]], which belongs to [[clan]] GH-L, are identified as Glu residues, the positions of the catalytic residues of [[GH15]], [[GH37]], and GH63 are highly conserved <cite>Kurakata2008 Gibson2007</cite>.

== Three-dimensional structures ==
The crystal structures of the bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurakata2008</cite> ([http://www.cazy.org/GH63_structure.html multiple PDB entries]) and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of an (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of [[GH15]], [[GH37]], GH65, and [[GH94]] <cite>Kurakata2008 Gibson2007</cite>. This similarity had been predicted on the basis of sequence comparison, before their crystal structures were available <cite>Stam2005</cite>.

== Family Firsts ==
;First gene cloning: Human processing α-glucosidase I <cite>Kalz-Fuller1995</cite>.
;First stereochemistry determination: Processing α-glucosidase I from ''Saccharomyces cerevisiae'' (Cwh41p) <cite>Palcic1999</cite>.
;First general acid residue identification: Inferred from structural comparison <cite>Kurakata2008</cite>.
;First general base residue identification: Inferred from structural comparison <cite>Kurakata2008</cite>.
;First 3-D structure: ''Escherichia coli'' YgjK, an enzyme showing the highest activity for the α-1,3-glucosidic linkage of nigerose <cite>Kurakata2008</cite>.

== References ==
<biblio>
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurakata2008 pmid=18586271
#Palcic1999 pmid=10619707
#Gibson2007 pmid=17455176
#Stam2005 pmid=16226731
#Kalz-Fuller1995 pmid=7635146
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-28T11:03:51Z

Takashi Tonozuka:

{{CuratorApproved}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of GH63 are exo-acting α-glucosidases. Eukaryotic members of this family are Processing α-Glucosidase I enzymes (mannosyl-oligosaccharide glucosidase, EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyze the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2, to produce β-glucose and Glc2Man9GlcNAc2. Processing α-Glucosidase I thus plays a critical role in the maturation of eukaryotic ''N''-glycans. The enzymatic properties of Cwh41p, a Processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been intensively studied <cite>Dhanawansa2002</cite> (also reviewed in <cite>Herscovics1999</cite>).

Genes encoding GH63 enzymes have also been found in archaea and bacteria, but their natural substrates are still unclear, as these organisms are not known to produce eukaryotic ''N''-linked oligosacharides. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, demonstrated the highest activity toward the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among the commercially available sugars tested <cite>Kurakata2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the catalytic (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of [[GH37]] and GH63, both of which belong to [[clan]] GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered to be a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurakata2008</cite>. Although both of the corresponding residues of [[GH15]], which belongs to [[clan]] GH-L, are identified as Glu residues, the positions of the catalytic residues of [[GH15]], [[GH37]], and GH63 are highly conserved <cite>Kurakata2008 Gibson2007</cite>.

== Three-dimensional structures ==
The crystal structures of the bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurakata2008</cite> ([http://www.cazy.org/GH63_structure.html multiple PDB entries]) and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of an (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of [[GH15]], [[GH37]], GH65, and [[GH94]] <cite>Kurakata2008 Gibson2007</cite>. This similarity had been predicted on the basis of sequence comparison, before their crystal structures were available <cite>Stam2005</cite>.

== Family Firsts ==
;First gene cloning: Human processing α-glucosidase I <cite>Kalz-Fuller1995</cite>.
;First stereochemistry determination: Processing α-glucosidase I from ''Saccharomyces cerevisiae'' (Cwh41p) <cite>Palcic1999</cite>.
;First general acid residue identification: Inferred from structural comparison <cite>Kurakata2008</cite>.
;First general base residue identification: Inferred from structural comparison <cite>Kurakata2008</cite>.
;First 3-D structure: ''Escherichia coli'' YgjK, an enzyme showing the highest activity for the α-1,3-glucosidic linkage of nigerose <cite>Kurakata2008</cite>.

== References ==
<biblio>
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurakata2008 pmid=18586271
#Palcic1999 pmid=10619707
#Gibson2007 pmid=17455176
#Stam2005 pmid=16226731
#Kalz-Fuller1995 pmid=7635146
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-25T03:07:11Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of this family are exo-acting enzymes. The known activity of the eukaryotic enzymes is processing α-glucosidase I (mannosyl-oligosaccharide glucosidase, EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2, to produce β-glucose and Glc2Man9GlcNAc2. Processing α-glucosidase I plays a critical role in the processing of eukaryotic ''N''-glycans. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been intensively studied ( <cite>Dhanawansa2002</cite>, also reviewed in <cite>Herscovics1999</cite> ).

Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic ''N''-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among commercially available sugars <cite>Kurataka2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the catalytic (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of GH37 and GH63, both of which belong to clan GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered as a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurataka2008</cite>. Although both of the two corresponding residues of GH15 (belonging to clan GH-L) are identified as Glu residues, the positions of the catalytic residues of GH15, GH37, and GH63 are highly conserved <cite>Kurataka2008 Gibson2007</cite>.

== Three-dimensional structures ==
The crystal structures of bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurataka2008</cite> and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of an (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of GH15, GH37, GH65, and [[GH94]] <cite>Kurataka2008 Gibson2007</cite>. This similarity had been predicted on the basis of sequence comparison, before their crystal structures were available <cite>Stam2005</cite>.

== Family Firsts ==
;First gene cloning: Human processing α-glucosidase I <cite>Kalz-Fuller1995</cite>.
;First stereochemistry determination: Processing α-glucosidase I from ''Saccharomyces cerevisiae'' (Cwh41p) <cite>Palcic1999</cite>.
;First general acid residue identification: Inferred from structural comparison <cite>Kurataka2008</cite>.
;First general base residue identification: Inferred from structural comparison <cite>Kurataka2008</cite>.
;First 3-D structure: ''Escherichia coli'' YgjK, an enzyme showing the highest activity for the α-1,3-glucosidic linkage of nigerose <cite>Kurataka2008</cite>.

== References ==
<biblio>
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurataka2008 pmid=18586271
#Palcic1999 pmid=10619707
#Gibson2007 pmid=17455176
#Stam2005 pmid=16226731
#Kalz-Fuller1995 pmid=7635146
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-22T12:59:49Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of this family are exo-acting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (mannosyl-oligosaccharide glucosidase, EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2, to produce β-glucose and Glc2Man9GlcNAc2. Processing α-glucosidase I plays a critical role in the processing of eukaryotic ''N''-glycans. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been intensively studied ( <cite>Dhanawansa2002</cite>, also reviewed in <cite>Herscovics1999</cite> ).

Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic ''N''-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among commercially available sugars <cite>Kurataka2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the catalytic (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of GH37 and GH63, both of which belong to clan GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered as a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurataka2008</cite>. Although both of the two corresponding residues of GH15 (belonging to clan GH-L) are identified as Glu residues, the positions of the catalytic residues of GH15, GH37, and GH63 are highly conserved <cite>Kurataka2008 Gibson2007</cite>.

== Three-dimensional structures ==
The crystal structures of bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurataka2008</cite> and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of an (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of GH15, GH37, GH65, and [[GH94]] <cite>Kurataka2008 Gibson2007</cite>. This similarity had been predicted on the basis of sequence comparison, before their crystal structures were available <cite>Stam2005</cite>.

== Family Firsts ==
;First gene cloning: Human processing α-glucosidase I <cite>Kalz-Fuller1995</cite>.
;First stereochemistry determination: Processing α-glucosidase I from ''Saccharomyces cerevisiae'' (Cwh41p) <cite>Palcic1999</cite>.
;First general acid residue identification: Inferred from structural comparison <cite>Kurataka2008</cite>.
;First general base residue identification: Inferred from structural comparison <cite>Kurataka2008</cite>.
;First 3-D structure: ''Escherichia coli'' YgjK, an enzyme showing the highest activity for the α-1,3-glucosidic linkage of nigerose <cite>Kurataka2008</cite>.

== References ==
<biblio>
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurataka2008 pmid=18586271
#Palcic1999 pmid=10619707
#Gibson2007 pmid=17455176
#Stam2005 pmid=16226731
#Kalz-Fuller1995 pmid=7635146
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-22T12:17:39Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of this family are exo-acting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2, to produce β-glucose and Glc2Man9GlcNAc2. Processing α-glucosidase I plays a critical role in the processing of eukaryotic ''N''-glycans. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been intensively studied ( <cite>Dhanawansa2002</cite>, also reviewed in <cite>Herscovics1999</cite> ).

Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic ''N''-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among commercially available sugars <cite>Kurataka2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the catalytic (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of GH37 and GH63, both of which belong to clan GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered as a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurataka2008</cite>. Although both of the two corresponding residues of GH15 (belonging to clan GH-L) are identified as Glu residues, the positions of the catalytic residues of GH15, GH37, and GH63 are highly conserved <cite>Kurataka2008 Gibson2007</cite>.

== Three-dimensional structures ==
The crystal structures of bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurataka2008</cite> and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of an (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of GH15, GH37, GH65, and [[GH94]] <cite>Kurataka2008 Gibson2007</cite>. This similarity had been predicted on the basis of sequence comparison, before their crystal structures were available <cite>Stam2005</cite>.

== Family Firsts ==
;First gene cloning: Human processing α-glucosidase I <cite>Kalz-Fuller1995</cite>.
;First stereochemistry determination: Processing α-glucosidase I from ''Saccharomyces cerevisiae'' (Cwh41p) <cite>Palcic1999</cite>.
;First general acid residue identification: Inferred from structural comparison <cite>Kurataka2008</cite>.
;First general base residue identification: Inferred from structural comparison <cite>Kurataka2008</cite>.
;First 3-D structure: ''Escherichia coli'' YgjK, an enzyme showing the highest activity for the α-1,3-glucosidic linkage of nigerose <cite>Kurataka2008</cite>.

== References ==
<biblio>
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurataka2008 pmid=18586271
#Palcic1999 pmid=10619707
#Gibson2007 pmid=17455176
#Stam2005 pmid=16226731
#Kalz-Fuller1995 pmid=7635146
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-22T10:24:04Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of this family are exo-acting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2, to produce β-glucose and Glc2Man9GlcNAc2. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been most intensively studied ( <cite>Dhanawansa2002</cite>, also reviewed in <cite>Herscovics1999</cite> ).

Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic ''N''-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among commercially available sugars <cite>Kurataka2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of GH37 and GH63, both of which belong to clan GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered as a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurataka2008</cite>. Although the two corresponding residues of GH15 (belonging to clan GH-L) are identified as two Glu residues, the positions of the catalytic residues of GH15, GH37, and GH63 are highly conserved <cite>Kurataka2008 Gibson2007</cite>.

== Three-dimensional structures ==
The crystal structures of bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurataka2008</cite> and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of a (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of GH15, GH37, GH65, and [[GH94]] <cite>Kurataka2008 Gibson2007</cite>. This similarity had been predicted on the basis of sequence comparison, before their crystal structures were available <cite>Stam2005</cite>.

== Family Firsts ==
;First stereochemistry determination: Processing α-glucosidase I from ''Saccharomyces cerevisiae'' (Cwh41p) <cite>Palcic1999</cite>.
;First general acid residue identification: Inferred from structural comparison <cite>Kurataka2008</cite>.
;First general base residue identification: Inferred from structural comparison <cite>Kurataka2008</cite>.
;First 3-D structure: ''Escherichia coli'' YgjK, an enzyme showing the highest activity for the α-1,3-glucosidic linkage of nigerose <cite>Kurataka2008</cite>.

== References ==
<biblio>
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurataka2008 pmid=18586271
#Palcic1999 pmid=10619707
#Gibson2007 pmid=17455176
#Stam2005 pmid=16226731
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-22T10:21:49Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of this family are exo-acting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2, to produce β-glucose and Glc2Man9GlcNAc2. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been most intensively studied ( <cite>Dhanawansa2002</cite>, also reviewed in <cite>Herscovics1999</cite> ).

Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic ''N''-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among commercially available sugars <cite>Kurataka2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of GH37 and GH63, both of which belong to clan GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered as a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurataka2008</cite>. Although the two corresponding residues of GH15 (belonging to clan GH-L) are identified as two Glu residues, the positions of the catalytic residues of GH15, GH37, and GH63 are highly conserved <cite>Kurataka2008 Gibson2007</cite>.

== Three-dimensional structures ==
The crystal structures of bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurataka2008</cite> and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of a (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of GH15, GH37, GH65, and GH94 <cite>Kurataka2008 Gibson2007</cite>. This similarity had been predicted on the basis of sequence comparison, before their crystal structures were available <cite>Stam2005</cite>.

== Family Firsts ==
;First stereochemistry determination: Processing α-glucosidase I from ''Saccharomyces cerevisiae'' (Cwh41p) <cite>Palcic1999</cite>.
;First general acid residue identification: Inferred from structural comparison <cite>Kurataka2008</cite>.
;First general base residue identification: Inferred from structural comparison <cite>Kurataka2008</cite>.
;First 3-D structure: ''Escherichia coli'' YgjK, an enzyme showing the highest activity for the α-1,3-glucosidic linkage of nigerose <cite>Kurataka2008</cite>.

== References ==
<biblio>
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurataka2008 pmid=18586271
#Palcic1999 pmid=10619707
#Gibson2007 pmid=17455176
#Stam2005 pmid=16226731
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-22T10:00:35Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of this family are exo-acting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been most intensively studied ( <cite>Dhanawansa2002</cite>, also reviewed in <cite>Herscovics1999</cite> ).

Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic ''N''-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among commercially available sugars <cite>Kurataka2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of GH37 and GH63, both of which belong to clan GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered as a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurataka2008</cite>. Although the two corresponding residues of GH15 (belonging to clan GH-L) are identified as two Glu residues, the positions of the catalytic residues of GH15, GH37, and GH63 are highly conserved <cite>Kurataka2008 Gibson2007</cite>.

== Three-dimensional structures ==
The crystal structures of bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurataka2008</cite> and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of a (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of GH15, GH37, GH65, and GH94 <cite>Kurataka2008 Gibson2007</cite>. This similarity had been predicted on the basis of sequence comparison, before their crystal structures were available <cite>Stam2005</cite>.

== Family Firsts ==
;First stereochemistry determination: Processing α-glucosidase I from ''Saccharomyces cerevisiae'' <cite>Palcic1999</cite>.
;First general acid residue identification: Inferred from structural comparison <cite>Kurataka2008</cite>.
;First general base residue identification: Inferred from structural comparison <cite>Kurataka2008</cite>.
;First 3-D structure: ''Escherichia coli'' YgjK, an enzyme showing the highest activity for the α-1,3-glucosidic linkage of nigerose <cite>Kurataka2008</cite>.

== References ==
<biblio>
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurataka2008 pmid=18586271
#Palcic1999 pmid=10619707
#Gibson2007 pmid=17455176
#Stam2005 pmid=16226731
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-22T09:54:35Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of this family are exo-acting inverting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been most intensively studied ( <cite>Dhanawansa2002</cite>, also reviewed in <cite>Herscovics1999</cite> ).

Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic ''N''-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among commercially available sugars <cite>Kurataka2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of GH37 and GH63, both of which belong to clan GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered as a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurataka2008</cite>. Although the two corresponding residues of GH15 (belonging to clan GH-L) are identified as two Glu residues, the positions of the catalytic residues of GH15, GH37, and GH63 are highly conserved <cite>Kurataka2008 Gibson2007</cite>.

== Three-dimensional structures ==
The crystal structures of bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurataka2008</cite> and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of a (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of GH15, GH37, GH65, and GH94 <cite>Kurataka2008 Gibson2007</cite>. This similarity had been predicted on the basis of sequence comparison, before their crystal structures were available <cite>Stam2005</cite>.

== Family Firsts ==
;First stereochemistry determination: Processing α-glucosidase I from ''Saccharomyces cerevisiae'' <cite>Palcic1999</cite>.
;First general acid residue identification: Inferred from structural comparison <cite>Kurataka2008</cite>.
;First general base residue identification: Inferred from structural comparison <cite>Kurataka2008</cite>.
;First 3-D structure: ''Escherichia coli'' YgjK, an enzyme showing the highest activity for the α-1,3-glucosidic linkage of nigerose <cite>Kurataka2008</cite>.

== References ==
<biblio>
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurataka2008 pmid=18586271
#Palcic1999 pmid=10619707
#Gibson2007 pmid=17455176
#Stam2005 pmid=16226731
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-22T09:42:34Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of this family are exo-acting inverting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been most intensively studied ( <cite>Dhanawansa2002</cite>, also reviewed in <cite>Herscovics1999</cite> ).

Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic ''N''-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among commercially available sugars <cite>Kurataka2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of GH37 and GH63, both of which belong to clan GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered as a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurataka2008</cite>. Although the two corresponding residues of GH15 (belonging to clan GH-L) are identified as two Glu residues, the positions of the catalytic residues of GH15, GH37, and GH63 are highly conserved <cite>Gibson2007 Kurataka2008</cite>.

== Three-dimensional structures ==
The crystal structures of bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurataka2008</cite> and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of a (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of GH15, GH37, GH65, and GH94. The similarity had been predicted, before their crystal structures were available <cite>Stam2005</cite>.

== Family Firsts ==
;First stereochemistry determination: Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'' <cite>Palcic1999</cite>.
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.

== References ==
<biblio>
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurataka2008 pmid=18586271
#Palcic1999 pmid=10619707
#Gibson2007 pmid=17455176
#Stam2005 pmid=16226731
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-21T12:26:33Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
Glycoside hydrolases of this family are exo-acting inverting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been most intensively studied ( <cite>Dhanawansa2002</cite>, also reviewed in <cite>Herscovics1999</cite> ).

Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic ''N''-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among commercially available sugars <cite>Kurataka2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of GH37 and GH63, both of which belong to clan GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered as a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurataka2008</cite>. Although the two corresponding residues of GH15 (belonging to clan GH-L) are identified as two Glu residues, the positions of the catalytic residues of GH15, GH37, and GH63 are highly conserved.

== Three-dimensional structures ==
The crystal structures of bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurataka2008</cite> and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of a (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of GH15, GH37, GH65, and GH94. This similarity was predicted before their crystal structures were available <cite>#Stam2005</cite>.

== Family Firsts ==
;First stereochemistry determination: Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'' <cite>Palcic1999</cite>.
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.

== References ==
<biblio>
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurataka2008 pmid=18586271
#Palcic1999 pmid=10619707
#Stam2005 pmid=16226731
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-21T12:20:50Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
Glycoside hydrolases of this family are exo-acting inverting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been most intensively studied ( <cite>Dhanawansa2002</cite>, also reviewed in <cite>Herscovics1999</cite> ).

Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic ''N''-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among commercially available sugars <cite>Kurataka2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of GH37 and GH63, both of which belong to clan GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered as a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurataka2008</cite>. Although the two corresponding residues of GH15 (belonging to clan GH-L) are identified as two Glu residues, the positions of the catalytic residues of GH15, GH37, and GH63 are highly conserved.

== Three-dimensional structures ==
The crystal structures of two bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurataka2008</cite> and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of a (α/α)6 barrel fold. The main chain of the (α/α)6 barrel domain shares high structural similarity with those of GH15, GH37, GH65, and GH94. This similarity was predicted before their crystal structures were available <cite>#Stam2005</cite>.

== Family Firsts ==
;First stereochemistry determination: Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'' <cite>Palcic1999</cite>.
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.

== References ==
<biblio>
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurataka2008 pmid=18586271
#Palcic1999 pmid=10619707
#Stam2005 pmid=16226731
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-21T11:43:51Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
Glycoside hydrolases of this family are exo-acting inverting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been most intensively studied ( <cite>Dhanawansa2002</cite>, also reviewed in <cite>Herscovics1999</cite> ).

Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic ''N''-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among commercially available sugars <cite>Kurataka2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of [[GH15]] and [[GH37]] enzymes. In the case of GH37 and GH63, both of which belong to clan GH-G, the catalytic [[general acid]] is predicted as an Asp residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered as a Glu residue (Glu727 in ''E. coli'' YgjK) <cite>Kurataka2008</cite>. Although the two corresponding residues of GH15 (belonging to clan GH-L) are identified as two Glu residues, the positions of the catalytic residues of GH15, GH37, and GH63 are highly conserved.

== Three-dimensional structures ==
The crystal structures of two bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurataka2008</cite> and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of a (α/α)6 barrel fold.

== Family Firsts ==
;First stereochemistry determination: Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'' <cite>Palcic1999</cite>.
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.

== References ==
<biblio>
#Dhanawansa2002 pmid=11971867
#Herscovics1999 pmid=9878780
#Kurataka2008 pmid=18586271
#Palcic1999 pmid=10619707
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-21T07:32:46Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
Glycoside hydrolases of this family are exo-acting inverting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been most intensively studied.

Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic ''N''-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among commercially available sugars <cite>Kurataka2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of GH15 and GH37 enzymes. The catalytic [[general acid]] is predicted as an aspartate residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered as a glutamate residue (Glu727 in ''E. coli'' YgjK) <cite>Kurataka2008</cite>.

== Three-dimensional structures ==
The crystal structures of two bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurataka2008</cite> and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of a (α/α)6 barrel fold.

== Family Firsts ==
;First stereochemistry determination: Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'' <cite>Palcic1999</cite>.
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.

== References ==
<biblio>
#Kurataka2008 pmid=18586271
#Palcic1999 pmid=10619707
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-21T07:31:00Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
Glycoside hydrolases of this family are exo-acting inverting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been most intensively studied.

Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic ''N''-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among commercially available sugars <cite>Kurataka2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of GH15 and GH37 enzymes. The catalytic [[general acid]] is predicted as an aspartate residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered as a glutamate residue (Glu727 in ''E. coli'' YgjK) <cite>Kurataka2008</cite>.

== Three-dimensional structures ==
The crystal structures of two bacterial GH63 proteins, ''E. coli'' YgjK <cite>Kurataka2008</cite> and ''Thermus thermophilus'' uncharacterised protein TTHA0978 ([{{PDBlink}}2z07 PDB 2z07]), have been reported. The catalytic domain consists of (α/α)6 barrel fold.

== Family Firsts ==
;First stereochemistry determination: Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'' <cite>Palcic1999</cite>.
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.

== References ==
<biblio>
#Kurataka2008 pmid=18586271
#Palcic1999 pmid=10619707
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-21T05:43:27Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
Glycoside hydrolases of this family are exo-acting inverting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosaccharide precursor, Glc3Man9GlcNAc2. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been most intensively studied.

Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic ''N''-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among commercially available sugars <cite>Kurataka2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''S. cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of GH15 and GH37 enzymes. The catalytic [[general acid]] is predicted as an aspartate residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered as a glutamate residue (Glu727 in ''E. coli'' YgjK) <cite>Kurataka2008</cite>.

== Three-dimensional structures ==
Content is to be added here.

== Family Firsts ==
;First stereochemistry determination: Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'' <cite>Palcic1999</cite>.
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.

== References ==
<biblio>
#Kurataka2008 pmid=18586271
#Palcic1999 pmid=10619707
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-21T05:37:50Z

Takashi Tonozuka:

Glycoside Hydrolase Family 63

2011-04-21T05:36:45Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
Glycoside hydrolases of this family are exo-acting inverting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosacharide precursor, Glc3Man9GlcNAc2. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been most intensively studied.

Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic ''N''-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among commercially available sugars <cite>Kurataka2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''Saccharomyces cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of GH15 and GH37 enzymes. The catalytic [[general acid]] is predicted as an aspartate residue (Asp501 in ''E. coli'' YgjK), and the [[general base]] is considered as a glutamate residue (Glu727 in ''E. coli'' YgjK) <cite>Kurataka2008</cite>.

== Three-dimensional structures ==
Content is to be added here.

== Family Firsts ==
;First stereochemistry determination: Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'' <cite>Palcic1999</cite>.
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.

== References ==
<biblio>
#Kurataka2008 pmid=18586271
#Palcic1999 pmid=10619707
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 49

2011-04-21T05:35:20Z

Takashi Tonozuka:

{{CuratorApproved}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''
|-
|'''Clan'''
|GH-N
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/GH49.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of family 49 cleave α-1,6-glucosidic linkages or α-1,4-glucosidic linkages of polysaccharides containing α-1,6-glucosidic linkages, dextran and pullulan. The major activities reported for this family of glycoside hydrolases are dextranase (EC [{{EClink}}3.2.1.11 3.2.1.11]), and a dextranase from ''Penicillium minioluteum'', Dex49A, is currently the most characterised enzyme. Dextran 1,6-α-isomaltotriosidase (EC [{{EClink}}3.2.1.95 3.2.1.95]) <cite>REF1</cite> and isopullulanase (EC [{{EClink}}3.2.1.57 3.2.1.57]) activities have also been described.

== Kinetics and Mechanism ==
Family GH49 α-glycosidases are [[inverting]] enzymes, as first shown by NMR on a dextranase Dex49A from ''Penicillium minioluteum'' <cite>REF2</cite> .

== Catalytic Residues ==
Three Asp residues (Asp376, Asp395, and Asp396 in Dex49A) are conserved in the catalytic centre of members of clan GH-N, GH49 and [[GH28]] enzymes <cite>REF2 REF3</cite>, and all three of the Asp mutants of a GH49 enzyme, isopullulanase, lost their activities <cite>REF4</cite>. The [[general acid]] was first identified in Dex49A from ''Penicillium minioluteum'' as Asp395 following the three-dimensional structure determination. To date, it is unclear whether either (or both) of the Asp residues (Asp376 and Asp396 in Dex49A) acts as a [[general base]] in the reaction of GH49 and [[GH28]] enzymes <cite>REF2 REF5 REF6</cite>.

== Three-dimensional structures ==
Two structures of GH49 enzymes are available so far <cite>REF2 REF3</cite>, and they display a two domain structure. The N-terminal domain is a β-sandwich and the C-terminal domain adopts a right-handed parallel β-helix. The similarity of the β-helix fold between GH49 and [[GH28]] enzymes has been described, although almost none of the amino acid residues other than the three catalytic Asp residues is conserved between the two families <cite>REF2 REF3</cite>. Each coil forming the cylindrical β-helix fold is composed of three β-sheets, which are named PB1, PB2, and PB3, following the original definition for a PL1 enzyme, pectate lyase C <cite>REF7</cite>.

== Family Firsts ==
;First gene cloning: Dextranase from ''Arthrobacter'' sp. CB-8 <cite>REF8</cite>.
;First sterochemistry determination: Dextranase (Dex49A) from ''Penicillium minioluteum'' <cite>REF2</cite>.
;First general acid residue identification: Dextranase (Dex49A) from ''Penicillium minioluteum'' <cite>REF2</cite>.
;First 3-D structure: Dextranase (Dex49A) from ''Penicillium minioluteum'' by X-ray crystallography (PDB ID [{{PDBlink}}1ogm 1ogm]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=10540747
#REF2 pmid=12962629
#REF3 pmid=18155243
#REF4 pmid=15560783
#REF5 pmid=10521427
#REF6 pmid=12022868
#REF7 pmid=8502994
#REF8 pmid=1859672
</biblio>

[[Category:Glycoside Hydrolase Families|GH049]]

Glycoside Hydrolase Family 63

2011-04-21T05:33:38Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH63'''
|-
|'''Clan'''
|GH-G
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|Inferred
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH63.html
|}
</div>


== Substrate specificities ==
Glycoside hydrolases of this family are exo-acting inverting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC [{{EClink}}3.2.1.106 3.2.1.106]), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosacharide precursor, Glc3Man9GlcNAc2. The enzymatic properties of Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'', have been most intensively studied.

Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic ''N''-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, ''Escherichia coli'' YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose (Glc-α-1,3-Glc) among commercially available sugars <cite>Kurataka2008</cite>.

== Kinetics and Mechanism ==
Family GH63 enzymes are [[inverting]] enzymes, as first shown by NMR on a processing α-glucosidase I from ''Saccharomyces cerevisiae'' <cite>Palcic1999</cite>.

== Catalytic Residues ==
The catalytic residues were inferred by comparing the (α/α)6 barrel domain of the GH63 enzyme, ''E. coli'' YgjK, with those of GH15 and GH37 enzymes. The catalytic general acid is predicted as an aspartate residue (Asp501 in ''E. coli'' YgjK), and the general base is considered as a glutamate residue (Glu727 in ''E. coli'' YgjK) <cite>Kurataka2008</cite>.

== Three-dimensional structures ==
Content is to be added here.

== Family Firsts ==
;First stereochemistry determination: Cwh41p, a processing α-glucosidase I from ''Saccharomyces cerevisiae'' <cite>Palcic1999</cite>.
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Kurataka2008</cite>.

== References ==
<biblio>
#Kurataka2008 pmid=18586271
#Palcic1999 pmid=10619707
</biblio>

[[Category:Glycoside Hydrolase Families|GH063]]

Glycoside Hydrolase Family 63

2011-04-21T05:32:12Z

Takashi Tonozuka:

Glycoside Hydrolase Family 63

2011-04-21T05:28:29Z

Takashi Tonozuka:

Glycoside Hydrolase Family 63

2011-04-21T05:21:34Z

Takashi Tonozuka:

Glycoside Hydrolase Family 63

2011-04-21T05:20:22Z

Takashi Tonozuka:

Glycoside Hydrolase Family 63

2011-04-21T03:41:45Z

Takashi Tonozuka:

Glycoside Hydrolase Family 63

2011-04-20T11:19:20Z

Takashi Tonozuka:

Glycoside Hydrolase Family 63

2011-04-20T11:17:24Z

Takashi Tonozuka:

Glycoside Hydrolase Family 63

2011-04-20T11:15:59Z

Takashi Tonozuka:

Glycoside Hydrolase Family 63

2011-04-20T10:20:43Z

Takashi Tonozuka:

Glycoside Hydrolase Family 63

2011-04-20T10:20:05Z

Takashi Tonozuka:

Glycoside Hydrolase Family 63

2011-04-20T10:19:02Z

Takashi Tonozuka:

Glycoside Hydrolase Family 63

2011-04-20T10:13:58Z

Takashi Tonozuka:

Glycoside Hydrolase Family 63

2011-04-20T10:12:40Z

Takashi Tonozuka:

Glycoside Hydrolase Family 49

2011-01-05T12:01:37Z

Takashi Tonozuka:

{{CuratorApproved}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''
|-
|'''Clan'''
|GH-N
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/GH49.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of family 49 cleave α-1,6-glucosidic linkages or α-1,4-glucosidic linkages of polysaccharides containing α-1,6-glucosidic linkages, dextran and pullulan. The major activities reported for this family of glycoside hydrolases are dextranase (EC [{{EClink}}3.2.1.11 3.2.1.11]), and a dextranase from ''Penicillium minioluteum'', Dex49A, is currently the most characterised enzyme. Dextran 1,6-α-isomaltotriosidase (EC [{{EClink}}3.2.1.95 3.2.1.95]) <cite>REF1</cite> and isopullulanase (EC [{{EClink}}3.2.1.57 3.2.1.57]) activities have also been described.

== Kinetics and Mechanism ==
Family GH49 α-glycosidases are [[inverting]] enzymes, as first shown by NMR on a dextranase Dex49A from ''Penicillium minioluteum'' <cite>REF2</cite> .

== Catalytic Residues ==
Three Asp residues (Asp376, Asp395, and Asp396 in Dex49A) are conserved in the catalytic centre of members of Clan GH-N, GH49 and [[GH28]] enzymes <cite>REF2 REF3</cite>, and all three of the Asp mutants of a GH49 enzyme, isopullulanase, lost their activities <cite>REF4</cite>. The [[general acid]] was first identified in Dex49A from ''Penicillium minioluteum'' as Asp395 following the three-dimensional structure determination. To date, it is unclear whether either (or both) of the Asp residues (Asp376 and Asp396 in Dex49A) acts as a [[general base]] in the reaction of GH49 and [[GH28]] enzymes <cite>REF2 REF5 REF6</cite>.

== Three-dimensional structures ==
Two structures of GH49 enzymes are available so far <cite>REF2 REF3</cite>, and they display a two domain structure. The N-terminal domain is a β-sandwich and the C-terminal domain adopts a right-handed parallel β-helix. The similarity of the β-helix fold between GH49 and [[GH28]] enzymes has been described, although almost none of the amino acid residues other than the three catalytic Asp residues is conserved between the two families <cite>REF2 REF3</cite>. Each coil forming the cylindrical β-helix fold is composed of three β-sheets, which are named PB1, PB2, and PB3, following the original definition for a PL1 enzyme, pectate lyase C <cite>REF7</cite>.

== Family Firsts ==
;First gene cloning: Dextranase from ''Arthrobacter'' sp. CB-8 <cite>REF8</cite>.
;First sterochemistry determination: Dextranase (Dex49A) from ''Penicillium minioluteum'' <cite>REF2</cite>.
;First general acid residue identification: Dextranase (Dex49A) from ''Penicillium minioluteum'' <cite>REF2</cite>.
;First 3-D structure: Dextranase (Dex49A) from ''Penicillium minioluteum'' by X-ray crystallography (PDB ID [{{PDBlink}}1ogm 1ogm]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=10540747
#REF2 pmid=12962629
#REF3 pmid=18155243
#REF4 pmid=15560783
#REF5 pmid=10521427
#REF6 pmid=12022868
#REF7 pmid=8502994
#REF8 pmid=1859672
</biblio>

[[Category:Glycoside Hydrolase Families|GH049]]

Glycoside Hydrolase Family 49

2010-05-18T06:16:00Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''
|-
|'''Clan'''
|GH-N
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/GH49.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of family 49 cleave α-1,6-glucosidic linkages or α-1,4-glucosidic linkages of polysaccharides containing α-1,6-glucosidic linkages, dextran and pullulan. The major activities reported for this family of glycoside hydrolases are dextranase (EC [{{EClink}}3.2.1.11 3.2.1.11]), and a dextranase from ''Penicillium minioluteum'', Dex49A, is currently the most characterised enzyme. Dextran 1,6-α-isomaltotriosidase (EC [{{EClink}}3.2.1.95 3.2.1.95]) <cite>REF1</cite> and isopullulanase (EC [{{EClink}}3.2.1.57 3.2.1.57]) activities have also been described.

== Kinetics and Mechanism ==
Family GH49 α-glycosidases are [[inverting]] enzymes, as first shown by NMR on a dextranase Dex49A from ''Penicillium minioluteum'' <cite>REF2</cite> .

== Catalytic Residues ==
Three Asp residues (Asp376, Asp395, and Asp396 in Dex49A) are conserved in the catalytic centre of members of Clan GH-N, GH49 and [[GH28]] enzymes <cite>REF2 REF3</cite>, and all three of the Asp mutants of a GH49 enzyme, isopullulanase, lost their activities <cite>REF4</cite>. The [[general acid]] was first identified in Dex49A from ''Penicillium minioluteum'' as Asp395 following the three-dimensional structure determination. To date, it is unclear whether either (or both) of the Asp residues (Asp376 and Asp396 in Dex49A) acts as a [[general base]] in the reaction of GH49 and [[GH28]] enzymes <cite>REF2 REF5 REF6</cite>.

== Three-dimensional structures ==
Two structures of GH49 enzymes are available so far <cite>REF2 REF3</cite>, and they display a two domain structure. The N-terminal domain is a β-sandwich and the C-terminal domain adopts a right-handed parallel β-helix. The similarity of the β-helix fold between GH49 and [[GH28]] enzymes has been described, although almost none of the amino acid residues other than the three catalytic Asp residues is conserved between the two families <cite>REF2 REF3</cite>. Each coil forming the cylindrical β-helix fold is composed of three β-sheets, which are named PB1, PB2, and PB3, following the original definition for a [[GH28]] enzyme, pectate lyase C <cite>REF7</cite>.

== Family Firsts ==
;First gene cloning: Dextranase from ''Arthrobacter'' sp. CB-8 <cite>REF8</cite>.
;First sterochemistry determination: Dextranase (Dex49A) from ''Penicillium minioluteum'' <cite>REF2</cite>.
;First general acid residue identification: Dextranase (Dex49A) from ''Penicillium minioluteum'' <cite>REF2</cite>.
;First 3-D structure: Dextranase (Dex49A) from ''Penicillium minioluteum'' by X-ray crystallography (PDB ID [{{PDBlink}}1ogm 1ogm]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=10540747
#REF2 pmid=12962629
#REF3 pmid=18155243
#REF4 pmid=15560783
#REF5 pmid=10521427
#REF6 pmid=12022868
#REF7 pmid=8502994
#REF8 pmid=1859672
</biblio>

[[Category:Glycoside Hydrolase Families|GH049]]

Glycoside Hydrolase Family 49

2010-05-18T06:02:40Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''
|-
|'''Clan'''
|GH-N
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/GH49.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of family 49 cleave α-1,6-glucosidic linkages or α-1,4-glucosidic linkages of polysaccharides containing α-1,6-glucosidic linkages, dextran and pullulan. The major activities reported for this family of glycoside hydrolases are dextranase (EC [{{EClink}}3.2.1.11 3.2.1.11]), and a dextranase from ''Penicillium minioluteum'', Dex49A, is currently the most characterised enzyme. Dextran 1,6-α-isomaltotriosidase (EC [{{EClink}}3.2.1.95 3.2.1.95]) <cite>REF1</cite> and isopullulanase (EC [{{EClink}}3.2.1.57 3.2.1.57]) activities have also been described.

== Kinetics and Mechanism ==
Family GH49 α-glycosidases are [[inverting]] enzymes, as first shown by NMR on a dextranase Dex49A from ''Penicillium minioluteum'' <cite>REF2</cite> .

== Catalytic Residues ==
Three Asp residues (Asp376, Asp395, and Asp396 in Dex49A) are conserved in the catalytic centre of members of Clan GH-N, GH49 and GH28 enzymes <cite>REF2 REF3</cite>, and all three of the Asp mutants of a GH49 enzyme, isopullulanase, lost their activities <cite>REF4</cite>. The [[general acid]] was first identified in Dex49A from ''Penicillium minioluteum'' as Asp395 following the three-dimensional structure determination. To date, it is unclear whether either (or both) of the Asp residues (Asp376 and Asp396 in Dex49A) acts as a [[general base]] in the reaction of GH49 and GH28 enzymes <cite>REF2 REF5 REF6</cite>.

== Three-dimensional structures ==
Two structures of GH49 enzymes are available so far <cite>REF2 REF3</cite>, and they display a two domain structure. The N-terminal domain is a β-sandwich and the C-terminal domain adopts a right-handed parallel β-helix. The similarity of the β-helix fold between GH49 and GH28 enzymes has been described, although almost none of the amino acid residues other than the three catalytic Asp residues is conserved between the two families <cite>REF2 REF3</cite>. Each coil forming the cylindrical β-helix fold is composed of three β-sheets, which are named PB1, PB2, and PB3, following the original definition for a GH28 enzyme, pectate lyase C <cite>REF7</cite>.

== Family Firsts ==
;First gene cloning: Dextranase from ''Arthrobacter'' sp. CB-8 <cite>REF8</cite>.
;First sterochemistry determination: Dextranase (Dex49A) from ''Penicillium minioluteum'' <cite>REF2</cite>.
;First general acid residue identification: Dextranase (Dex49A) from ''Penicillium minioluteum'' <cite>REF2</cite>.
;First 3-D structure: Dextranase (Dex49A) from ''Penicillium minioluteum'' by X-ray crystallography (PDB ID [{{PDBlink}}1ogm 1ogm]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=10540747
#REF2 pmid=12962629
#REF3 pmid=18155243
#REF4 pmid=15560783
#REF5 pmid=10521427
#REF6 pmid=12022868
#REF7 pmid=8502994
#REF8 pmid=1859672
</biblio>

[[Category:Glycoside Hydrolase Families|GH049]]

Glycoside Hydrolase Family 49

2010-05-18T05:50:31Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''
|-
|'''Clan'''
|GH-N
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/GH49.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of family 49 cleave α-1,6-glucosidic linkages or α-1,4-glucosidic linkages of polysaccharides containing α-1,6-glucosidic linkages, dextran and pullulan. The major activities reported for this family of glycoside hydrolases are dextranase (EC [{{EClink}}3.2.1.11 3.2.1.11]), and a dextranase from ''Penicillium minioluteum'', Dex49A, is currently the most characterised enzyme. Dextran 1,6-α-isomaltotriosidase (EC [{{EClink}}3.2.1.95 3.2.1.95]) <cite>REF1</cite> and isopullulanase (EC [{{EClink}}3.2.1.57 3.2.1.57]) activities have also been described.

== Kinetics and Mechanism ==
Family GH49 α-glycosidases are [[inverting]] enzymes, as first shown by NMR on a dextranase Dex49A from ''Penicillium minioluteum'' <cite>REF2</cite> .

== Catalytic Residues ==
Three Asp residues (Asp376, Asp395, and Asp396 in Dex49A) are conserved in the catalytic centre of members of Clan GH-N, GH49 and GH28 enzymes <cite>REF2 REF3</cite>, and all three of the Asp mutants of a GH49 enzyme, isopullulanase, lost their activities <cite>REF4</cite>. The [[general acid]] was first identified in Dex49A from ''Penicillium minioluteum'' as Asp395 following the three-dimensional structure determination. To date, it is unclear whether either of the Asp residues (Asp376 and Asp396 in Dex49A) acts as a [[general base]] in the reaction of both GH49 and GH28 enzymes <cite>REF2 REF5 REF6</cite>.

== Three-dimensional structures ==
Two structures of GH49 enzymes are available so far <cite>REF2 REF3</cite>, and they display a two domain structure. The N-terminal domain is a β-sandwich and the C-terminal domain adopts a right-handed parallel β-helix. The similarity of the β-helix fold between GH49 and GH28 enzymes has been described, although almost none of the amino acid residues other than the three catalytic Asp residues is conserved between the two families <cite>REF2 REF3</cite>. Each coil forming the cylindrical β-helix fold is composed of three β-sheets, which are named PB1, PB2, and PB3, following the original definition for a GH28 enzyme, pectate lyase C <cite>REF7</cite>.

== Family Firsts ==
;First gene cloning: Dextranase from ''Arthrobacter'' sp. CB-8 <cite>REF8</cite>.
;First sterochemistry determination: Dextranase (Dex49A) from ''Penicillium minioluteum'' <cite>REF2</cite>.
;First general acid residue identification: Dextranase (Dex49A) from ''Penicillium minioluteum'' <cite>REF2</cite>.
;First 3-D structure: Dextranase (Dex49A) from ''Penicillium minioluteum'' by X-ray crystallography (PDB ID [{{PDBlink}}1ogm 1ogm]) <cite>REF2</cite>.

== References ==
<biblio>

#REF1 pmid=10540747
#REF2 pmid=12962629
#REF3 pmid=18155243
#REF4 pmid=15560783
#REF5 pmid=10521427
#REF6 pmid=12022868
#REF7 pmid=8502994
#REF8 pmid=1859672

</biblio>

[[Category:Glycoside Hydrolase Families|GH049]]

Glycoside Hydrolase Family 49

2010-05-18T05:47:41Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''
|-
|'''Clan'''
|GH-N
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GHnn.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of family 49 cleave α-1,6-glucosidic linkages or α-1,4-glucosidic linkages of polysaccharides containing α-1,6-glucosidic linkages, dextran and pullulan. The major activities reported for this family of glycoside hydrolases are dextranase (EC [{{EClink}}3.2.1.11 3.2.1.11]), and a dextranase from ''Penicillium minioluteum'', Dex49A, is currently the most characterised enzyme. Dextran 1,6-α-isomaltotriosidase (EC [{{EClink}}3.2.1.95 3.2.1.95]) <cite>REF1</cite> and isopullulanase (EC [{{EClink}}3.2.1.57 3.2.1.57]) activities have also been described.

== Kinetics and Mechanism ==
Family GH49 α-glycosidases are [[inverting]] enzymes, as first shown by NMR on a dextranase Dex49A from ''Penicillium minioluteum'' <cite>REF2</cite> .

== Catalytic Residues ==
Three Asp residues (Asp376, Asp395, and Asp396 in Dex49A) are conserved in the catalytic centre of members of Clan GH-N, GH49 and GH28 enzymes <cite>REF2 REF3</cite>, and all three of the Asp mutants of a GH49 enzyme, isopullulanase, lost their activities <cite>REF4</cite>. The [[general acid]] was first identified in Dex49A from ''Penicillium minioluteum'' as Asp395 following the three-dimensional structure determination. To date, it is unclear whether either of the Asp residues (Asp376 and Asp396 in Dex49A) acts as a [[general base]] in the reaction of both GH49 and GH28 enzymes <cite>REF2 REF5 REF6</cite>.

== Three-dimensional structures ==
Two structures of GH49 enzymes are available so far <cite>REF2 REF3</cite>, and they display a two domain structure. The N-terminal domain is a β-sandwich and the C-terminal domain adopts a right-handed parallel β-helix. The similarity of the β-helix fold between GH49 and GH28 enzymes has been described, although almost none of the amino acid residues other than the three catalytic Asp residues is conserved between the two families <cite>REF2 REF3</cite>. Each coil forming the cylindrical β-helix fold is composed of three β-sheets, which are named PB1, PB2, and PB3, following the original definition for a GH28 enzyme, pectate lyase C <cite>REF7</cite>.

== Family Firsts ==
;First gene cloning: Dextranase from ''Arthrobacter'' sp. CB-8 <cite>REF8</cite>.
;First sterochemistry determination: Dextranase (Dex49A) from ''Penicillium minioluteum'' <cite>REF2</cite>.
;First general acid residue identification: Dextranase (Dex49A) from ''Penicillium minioluteum'' <cite>REF2</cite>.
;First 3-D structure: Dextranase (Dex49A) from ''Penicillium minioluteum'' by X-ray crystallography (PDB ID [{{PDBlink}}1ogm 1ogm]) <cite>REF2</cite>.

== References ==
<biblio>

#REF1 pmid=10540747
#REF2 pmid=12962629
#REF3 pmid=18155243
#REF4 pmid=15560783
#REF5 pmid=10521427
#REF6 pmid=12022868
#REF7 pmid=8502994
#REF8 pmid=1859672

</biblio>

[[Category:Glycoside Hydrolase Families|GH049]]

Glycoside Hydrolase Family 49

2010-05-18T05:39:18Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''
|-
|'''Clan'''
|GH-N
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GHnn.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of family 49 cleave α-1,6-linkages or α-1,4-linkages of polysaccharides containing α-1,6-glucosidic linkages, dextran and pullulan. The major activities reported for this family of glycoside hydrolases are dextranase (EC [{{EClink}}3.2.1.11 3.2.1.11]), and a dextranase from ''Penicillium minioluteum'', Dex49A, is currently the most characterised enzyme.　Dextran 1,6-α-isomaltotriosidase (EC [{{EClink}}3.2.1.95 3.2.1.95]) <cite>REF1</cite> and isopullulanase (EC [{{EClink}}3.2.1.57 3.2.1.57]) activities have also been described.

== Kinetics and Mechanism ==
Family GH49 α-glycosidases are [[inverting]] enzymes, as first shown by NMR on a dextranase Dex49A from ''Penicillium minioluteum'' <cite>REF2</cite> .

== Catalytic Residues ==
Three Asp residues (Asp376, Asp395, and Asp396 in Dex49A) are conserved in the catalytic centre of members of Clan GH-N, GH49 and GH28 enzymes <cite>REF2 REF3</cite>, and all three of the Asp mutants of a GH49 enzyme, isopullulanase, lost their activities <cite>REF4</cite>. The [[general acid]] was first identified in Dex49A from ''Penicillium minioluteum'' as Asp395 following the three-dimensional structure determination. To date, it is unclear whether either of the Asp residues (Asp376 and Asp396 in Dex49A) acts as a [[general base]] in the reaction of both GH49 and GH28 enzymes <cite>REF2 REF5 REF6</cite>.

== Three-dimensional structures ==
Two structures of GH49 enzymes are available so far <cite>REF2 REF3</cite>, and they display a two domain structure. The N-terminal domain is a β-sandwich and the C-terminal domain adopts a right-handed parallel β-helix. The similarity of the β-helix fold between GH49 and GH28 enzymes has been described, although almost none of the amino acid residues other than the three catalytic Asp residues is conserved between the two families <cite>REF2 REF3</cite>. Each coil forming the cylindrical β-helix fold is composed of three β-sheets, which are named PB1, PB2, and PB3, following the original definition for a GH28 enzyme, pectate lyase C <cite>REF7</cite>.

== Family Firsts ==
;First gene cloning: Dextranase from ''Arthrobacter'' sp. CB-8 <cite>REF8</cite>.
;First sterochemistry determination: Dextranase (Dex49A) from ''Penicillium minioluteum'' <cite>REF2</cite>.
;First general acid residue identification: Dextranase (Dex49A) from ''Penicillium minioluteum'' <cite>REF2</cite>.
;First 3-D structure: Dextranase (Dex49A) from ''Penicillium minioluteum'' by X-ray crystallography (PDB ID [{{PDBlink}}1ogm 1ogm]) <cite>REF2</cite>.

== References ==
<biblio>

#REF1 pmid=10540747
#REF2 pmid=12962629
#REF3 pmid=18155243
#REF4 pmid=15560783
#REF5 pmid=10521427
#REF6 pmid=12022868
#REF7 pmid=8502994
#REF8 pmid=1859672

</biblio>

[[Category:Glycoside Hydrolase Families|GH049]]

Glycoside Hydrolase Family 49

2010-05-18T05:25:48Z

Takashi Tonozuka:

{{UnderConstruction}}
* [[Author]]: ^^^Takashi Tonozuka^^^
* [[Responsible Curator]]: ^^^Takashi Tonozuka^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''
|-
|'''Clan'''
|GH-N
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GHnn.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of family 49 cleave α-1,6-linkages or α-1,4-linkages of polysaccharides containing α-1,6-glucosidic linkages, dextran and pullulan. The major activities reported for this family of glycoside hydrolases are dextranase (EC [{{EClink}}3.2.1.11 3.2.1.11]), and a dextranase from ''Penicillium minioluteum'', Dex49A, is currently the most characterised enzyme.　Dextran 1,6-α-isomaltotriosidase (EC [{{EClink}}3.2.1.95 3.2.1.95]) <cite>1</cite> and isopullulanase (EC [{{EClink}}3.2.1.57 3.2.1.57]) activities have also been described.

== Kinetics and Mechanism ==
Family GH49 α-glycosidases are [[inverting]] enzymes, as first shown by NMR on a dextranase Dex49A from ''Penicillium minioluteum'' <cite>2</cite> .

== Catalytic Residues ==
Three Asp residues (Asp376, Asp395, and Asp396 in Dex49A) are conserved in the catalytic centre of members of Clan GH-N, GH49 and GH28 enzymes <cite>2</cite>, and all three of the Asp mutants of a GH49 enzyme, isopullulanase, lost their activities <cite>3</cite>. The [[general acid]] was first identified in Dex49A from ''Penicillium minioluteum'' as Asp395 following the three-dimensional structure determination. To date, it is unclear whether either of the Asp residues (Asp376 and Asp396 in Dex49A) acts as a [[general base]] in the reaction of both GH49 and GH28 enzymes <cite>2 4 5</cite>.

== Three-dimensional structures ==
Two structures of GH49 enzymes are available so far <cite>2 6</cite>, and they display a two domain structure. The N-terminal domain is a β-sandwich and the C-terminal domain adopts a right-handed parallel β-helix. The similarity of the β-helix fold between GH49 and GH28 enzymes has been described, although almost none of the amino acid residues other than the three catalytic Asp residues is conserved between the two families <cite>2 6</cite>. Each coil forming the cylindrical β-helix fold is composed of three β-sheets, which are named PB1, PB2, and PB3, following the original definition for a GH28 enzyme, pectate lyase C <cite>7</cite>.

== Family Firsts ==
;First gene cloning: Dextranase from ''Arthrobacter'' sp. CB-8 <cite>8</cite>.
;First sterochemistry determination: Dextranase (Dex49A) from ''Penicillium minioluteum'' <cite>2</cite>.
;First general acid residue identification: Dextranase (Dex49A) from ''Penicillium minioluteum'' <cite>2</cite>.
;First 3-D structure: Dextranase (Dex49A) from ''Penicillium minioluteum'' by X-ray crystallography (PDB ID [{{PDBlink}}1ogm 1ogm]) <cite>2</cite>.

== References ==
<biblio>

#1 pmid=10540747
#2 pmid=12962629
#3 pmid=15560783
#4 pmid= Normal 0 0 2 false false false EN-US JA X-NONE MicrosoftInternetExplorer4 10521427
#5 pmid=12022868
#6 pmid=18155243
#7 pmid=8502994
#8 pmid=1859672

</biblio>

[[Category:Glycoside Hydrolase Families|GH049]]

Glycoside Hydrolase Family 49

2010-05-17T11:58:57Z

Takashi Tonozuka:

Glycoside Hydrolase Family 49

2010-05-17T11:51:44Z

Takashi Tonozuka:

Glycoside Hydrolase Family 49

2010-05-13T12:40:43Z

Takashi Tonozuka:

Glycoside Hydrolase Family 49

2010-05-13T12:31:09Z

Takashi Tonozuka: