CAZypedia - User contributions [en-ca]

Glycoside Hydrolase Family 112

2009-09-02T23:58:31Z

Motomitsu Kitaoka: /* Three-dimensional structures */

* [[Author]]: [[User:Motomitsu Kitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family of [[glycoside hydrolases]] contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?2.4.1.211 2.4.1.211]) <cite>REF1</cite> and β-1,4-D-galactosyl-L-rhamnose phosphorylase (EC 2.4.1.-) <cite>REF2</cite>. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) <cite>REF3</cite>, lacto-''N''-biose I phosphorylase (LNBP) <cite>REF4</cite>, and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) <cite>REF1,REF4,REF5</cite> based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) <cite>REF4</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. <cite>REF1</cite> on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for [[inverting]] phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in [[inverting]] [[glycoside hydrolase]] reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' (PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2ZUS 2ZUS], [http://www.rcsb.org/pdb/explore/explore.do?structureId=2ZUT 2ZUT],
[http://www.rcsb.org/pdb/explore/explore.do?structureId=2ZUU 2ZUU], [http://www.rcsb.org/pdb/explore/explore.do?structureId=2ZUV 2ZUV],
[http://www.rcsb.org/pdb/explore/explore.do?structureId=2ZUW 2ZUW]) <cite>REF7</cite>. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of [[Glycoside Hydrolase Family 42]], supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' <cite>REF1</cite>.
;First sequence identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF5</cite>.
;First general acid residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>.
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>.

== References ==
<biblio>
#REF1 pmid=9889079
#REF2 pmid=19491100
#REF3 pmid=18183385
#REF4 pmid=18723650
#REF5 pmid=15933016
#REF6 pmid=17587697
#REF7 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families|GH112]]

Glycoside Hydrolase Family 8

2009-08-19T07:10:30Z

Motomitsu Kitaoka: /* Family Firsts */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]] and [[User:ShinyaFushinobu|Shinya Fushinobu]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 8'''
|-
|'''Clan'''
|GH-M
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH8.html
|}
</div>

== Substrate specificities ==
GH8 enzymes cleave β-1,4 linkages of β-1,4 glucans, xylans (or xylooligosaccharides), chitosans, and lichenans (1,3-1,4-β-D-glucan). All of GH8 members have been found from Bacteria, and there is no members from Eukaryotic or Archaeal origin. The majority of the enzymes are endo-acting enzymes, but one member has an exo-activity that releases β-D-xylose residues from the reducing end of xylooligosaccharides. The substrate specificities found in GH8 are: chitosanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.132 3.2.1.132]), cellulase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.4 3.2.1.4]), licheninase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.73 3.2.1.73]), endo-1,4-β-xylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.8 3.2.1.8]) and reducing-end-xylose releasing exo-oligoxylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.156 3.2.1.156]).

== Kinetics and Mechanism ==
GH8 enzymes are inverting enzymes, as first shown by Fierobe ''et al.'' who monitored the reaction of endoglucanase C from ''Clostridium cellulolyticum'' (CelCCC) using proton NMR spectroscopy <CITE>REF5</CITE>.

== Catalytic Residues ==
The general acid (proton donor to the leaving group) was first identified in CelA from ''C. thermocellum'' as Glu95 <cite>REF2</cite>.
The general base (proton acceptor from the nucleophilic water) of GH8a subfamily was first identified in CelA from ''C. thermocellum'' as Asp278 <cite>REF2</cite>.
The general base of GH8b subfamily was first identified in chitosanase from ''Bacillus'' sp. K17 as Glu309 based on its crystal structure and by making E309Q mutant <cite>REF1</cite>.

== Subfamilies ==
GH8 enzymes are divided into at least three subfamilies, depending on the position of the general base <cite>REF1</cite>.
GH8a has the general base (Asp) at the N-terminal end of α8 helix. GH8a contains cellulases, xylanases and other enzymes.
In GH8b enzymes, the Asp residue is replaced by Asn, and the general base is a Glu residue located in a long loop inserted between α7 and α8 helices. GH8b contains chitosanases, licheninases, cellulases and other enzymes.
The position of the general base in GH8c is unknown.

== Three-dimensional structures ==
Several three-dimensional structures of GH8 members from bacterial origin have been solved. The first solved 3-D structure was endoglucanase CelA from ''Clostridium thermocellum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) in 1996 <cite>REF2</cite>. As members of Clan GH-M they have a (α/α)<sub>6</sub> fold similar to [[Glycoside Hydrolase Family 48]]. The general acid residue is located at the N-terminal end of α4 helix. Position of the general base differ among [[#Subfamilies]]. Atomic (0.94 Å) resolution structure of CelA in complex with substrate ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1KWF PDB 1kwf]) has been determined <cite>REF3</cite>.

== Glycosynthase ==
Reducing-end-xylose releasing exo-oligoxylanase from ''Bacillus halodurans'' C-125 is the first inverting GH that was converted to glycosynthase by mutating the general base residue <cite>REF4</cite>.

== Family Firsts ==
;First sequence identification: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF6</cite>
;First sterochemistry determination: Endoglucanase C from ''Clostridium cellulolyticum'' (CelCCC) <cite>REF5</cite>
;First general acid residue identification: Cellulase (CelA) from ''Clostridium thermocellum'' <cite>REF2</cite>
;First general base residue identification of GH8a: Cellulase (CelA) from ''Clostridium thermocellum'' <cite>REF2</cite>
;First general base residue identification of GH8b: Chitosanase from ''Bacillus'' sp. K17 by crystal structure and a mutant <cite>REF1</cite>.
;First 3-D structure: Endoglucanase CelA from ''Clostridium thermocellum'' by X-ray crystallography ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=15465062
#REF2 pmid=8805535
#REF3 pmid=11884144
#REF4 pmid=16301312
#REF5 pmid=8223599
#REF6 pmid=3980433
</biblio>

[[Category:Glycoside Hydrolase Families|GH008]]

Glycoside Hydrolase Family 112

2009-08-19T07:09:21Z

Motomitsu Kitaoka: /* Family Firsts */

* [[Author]]: [[User:Motomitsu Kitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?2.4.1.211 2.4.1.211]) <cite>REF1</cite> and β-1,4-D-galactosyl-L-rhamnose phosphorylase (EC 2.4.1.-) <cite>REF2</cite>. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) <cite>REF3</cite>, lacto-''N''-biose I phosphorylase (LNBP) <cite>REF4</cite>, and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) <cite>REF1,REF4,REF5</cite> based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) <cite>REF4</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. <cite>REF1</cite> on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of [[Glycoside Hydrolase Family 42]], supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' <cite>REF1</cite>.
;First sequence identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF5</cite>.
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>.
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>.

== References ==
<biblio>
#REF1 pmid=9889079
#REF2 pmid=19491100
#REF3 pmid=18183385
#REF4 pmid=18723650
#REF5 pmid=15933016
#REF6 pmid=17587697
#REF7 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families|GH112]]

Glycoside Hydrolase Family 94

2009-08-06T01:59:17Z

Motomitsu Kitaoka: /* Substrate specificities */

* [[Author]]: [[User:Masafumi_Hidaka|Masafumi Hidaka]]
* [[Responsible Curator]]: [[User:Shinya_Fushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 94'''
|-
|'''Clan'''
|none (similar to GH-L)
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH94.html
|}
</div>

== Substrate specificities ==
This family exclusively contains [[Phosphorylases]] that cleave β-glycosidic bonds. The substrate specificities found in GH94 are: cellobiose (Glc-β1,4-Glc) phosphorylase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?2.4.1.20 2.4.1.20]), cellodextrin ((Glc-β1,4-)<sub>n-1</sub>Glc; n ≥ 3) phosphorylase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?2.4.1.49 2.4.1.49]), and N,N’-diacetyl chitobiose (GlcNAc-β1,4-GlcNAc) phosphorylase. Moreover, a phosphorylase domain belonging to this family is found in cyclic β-1,2-glucan synthase, a modular protein that also contains a glycosyltransferase domain from [[GlycosylTransferase Family 84]] <cite>REF7</cite>. The GH94 domain is thought to phosphorolyze protein-bound β-1,2-glucans synthesized from UDP-glucose by the GT84 domain.<BR>

GH94 enzymes were initially classified in [[GlycosylTransferase Family 36]] because none of them show hydrolytic activity. However because of the evolutionary, structural and mechanistic relatedness with clan GH-L glycoside hydrolases, the family was re-assigned to family GH94 <cite>REF1</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH94 enzymes proceeds with inversion of anomeric configuration, as first shown by Sih and McBee <cite>REF5</cite> on cellobiose phosphorylase from ''Clostridium thermocellum'', i.e. cellobiose (Glc-β1,4-Glc) + Pi ↔ α-glucose 1-phosphate + glucose. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylases is proposed to be similar to that for inverting GHs <cite>REF1</cite>. With the aid of a general acid residue, enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue, as in inverting GH reaction.

== Catalytic Residues ==
The catalytic residue was first elucidated by superimposing the active site structure of chitobiose phosphorylase from ''Vibrio proteolyticus'' with a [[Glycoside Hydrolase Family 15]] enzyme, glucoamylase from ''Thermoanaerobacterium thermosaccharolyticum'' <cite>REF1</cite>. Considering the similarities of the active site structure, Asp492 was identified as the general acid residue. D492A/N mutants of this enzyme showed no detectable activity. A general base residue is not required in the reaction catalyzed by glycoside hydrolase-like inverting phosphorylases.

== Three-dimensional structures ==
The first solved 3-D structure was chitobiose phosphorylase from ''Vibrio proteolyticus'' (PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=1V7V 1V7V], [http://www.rcsb.org/pdb/explore/explore.do?structureId=1V7W 1V7W],
[http://www.rcsb.org/pdb/explore/explore.do?structureId=1V7X 1V7X]) <cite>REF1</cite>. The enzyme has a (α/α)<sub>6</sub> barrel fold that is remarkably similar to clan GH-L. The position of the catalytic general acid is superimposable with Clan GH-L. It should be noted that GH94 enzymes act on β-bonds, whereas clan GH-L enzymes ([[Glycoside Hydrolase Family 15]] and [[Glycoside Hydrolase Family 65]]) act on α-bonds.

== Family Firsts ==
;First sterochemistry determination:
Cellobiose phosphorylase from ''Clostridium thermocellum'' <cite>REF5</cite>
;First gene cloning:
Cellobiose phosphorylase and a cellodextrin phosphorylase from ''Clostridium stercorarium'' <cite>REF6</cite>
;First catalytic nucleophile identification:
The inverting phosphorolytic reaction does not require a catalytic general base residue, since inorganic phosphate acts as a nucleophile.
;First general acid residue identification:
''Vibrio proteolyticus'' chitobiose phosphorylase by kinetic studies with mutants <cite>REF1</cite>
;First 3-D structure:
''Vibrio proteolyticus'' chitobiose phosphorylase <cite>REF1</cite>.

== References ==
<biblio>
#REF1 pmid=15274915
#REF5 Sih CJ, and McBee RH. ''A cellobiose phosphorylase in Clostridium thermocellum.'' Proc Montana Acad Sci 1955, 15, 21-22.

#REF6 pmid=9249035
#REF7 pmid=17921247

</biblio>

[[Category:Glycoside Hydrolase Families|GH094]]

Glycoside Hydrolase Family 8

2009-08-06T01:52:24Z

Motomitsu Kitaoka: /* Family Firsts */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]] and [[User:ShinyaFushinobu|Shinya Fushinobu]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 8'''
|-
|'''Clan'''
|GH-M
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH8.html
|}
</div>

== Substrate specificities ==
GH8 enzymes cleave β-1,4 linkages of β-1,4 glucans, xylans (or xylooligosaccharides), chitosans, and lichenans (1,3-1,4-β-D-glucan). All of GH8 members have been found from Bacteria, and there is no members from Eukaryotic or Archaeal origin. The majority of the enzymes are endo-acting enzymes, but one member has an exo-activity that releases β-D-xylose residues from the reducing end of xylooligosaccharides. The substrate specificities found in GH8 are: chitosanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.132 3.2.1.132]), cellulase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.4 3.2.1.4]), licheninase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.73 3.2.1.73]), endo-1,4-β-xylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.8 3.2.1.8]) and reducing-end-xylose releasing exo-oligoxylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.156 3.2.1.156]).

== Kinetics and Mechanism ==
GH8 enzymes are inverting enzymes, as first shown by Fiebrobe ''et al.'' on endoglucanase C from ''Clostridium cellulolyticum'' (CelCCC) <CITE>REF5</CITE>.

== Catalytic Residues ==
The general acid (proton donor to the leaving group) was first identified in CelA from ''C. thermocellum'' as Glu95 <cite>REF2</cite>.
The general base (proton acceptor from the nucleophilic water) of GH8a subfamily was first identified in CelA from ''C. thermocellum'' as Asp278 <cite>REF2</cite>.
The general base of GH8b subfamily was first identified in chitosanase from ''Bacillus'' sp. K17 as Glu309 based on its crystal structure and by making E309Q mutant <cite>REF1</cite>.

== Subfamilies ==
GH8 enzymes are divided into at least three subfamilies, depending on the position of the general base <cite>REF1</cite>.
GH8a has the general base (Asp) at the N-terminal end of α8 helix. GH8a contains cellulases, xylanases and other enzymes.
In GH8b enzymes, the Asp residue is replaced by Asn, and the general base is a Glu residue located in a long loop inserted between α7 and α8 helices. GH8b contains chitosanases, licheninases, cellulases and other enzymes.
The position of the general base in GH8c is unknown.

== Three-dimensional structures ==
Several three-dimensional structures of GH8 members from bacterial origin have been solved. The first solved 3-D structure was endoglucanase CelA from ''Clostridium thermocellum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) in 1996 <cite>REF2</cite>. As members of Clan GH-M they have a (α/α)<sub>6</sub> fold similar to [[Glycoside Hydrolase Family 48]]. The general acid residue is located at the N-terminal end of α4 helix. Position of the general base differ among [[#Subfamilies]]. Atomic (0.94 Å) resolution structure of CelA in complex with substrate ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1KWF PDB 1kwf]) has been determined <cite>REF3</cite>.

== Glycosynthase ==
Reducing-end-xylose releasing exo-oligoxylanase from ''Bacillus halodurans'' C-125 is the first inverting GH that was converted to glycosynthase by mutating the general base residue <cite>REF4</cite>.

== Family Firsts ==
;First gene cloning: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF6</cite>
;First sterochemistry determination: Endoglucanase C from ''Clostridium cellulolyticum'' (CelCCC) <cite>REF5</cite>
;First general acid residue identification: Cellulase (CelA) from ''Clostridium thermocellum'' <cite>REF2</cite>
;First general base residue identification of GH8a: Cellulase (CelA) from ''Clostridium thermocellum'' <cite>REF2</cite>
;First general base residue identification of GH8b: Chitosanase from ''Bacillus'' sp. K17 by crystal structure and a mutant <cite>REF1</cite>.
;First 3-D structure: Endoglucanase CelA from ''Clostridium thermocellum'' by X-ray crystallography ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=15465062
#REF2 pmid=8805535
#REF3 pmid=11884144
#REF4 pmid=16301312
#REF5 pmid=8223599
#REF6 pmid=3980433
</biblio>

[[Category:Glycoside Hydrolase Families|GH008]]

Glycoside Hydrolase Family 8

2009-08-06T01:49:52Z

Motomitsu Kitaoka: /* Family Firsts */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]] and [[User:ShinyaFushinobu|Shinya Fushinobu]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 8'''
|-
|'''Clan'''
|GH-M
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH8.html
|}
</div>

== Substrate specificities ==
GH8 enzymes cleave β-1,4 linkages of β-1,4 glucans, xylans (or xylooligosaccharides), chitosans, and lichenans (1,3-1,4-β-D-glucan). All of GH8 members have been found from Bacteria, and there is no members from Eukaryotic or Archaeal origin. The majority of the enzymes are endo-acting enzymes, but one member has an exo-activity that releases β-D-xylose residues from the reducing end of xylooligosaccharides. The substrate specificities found in GH8 are: chitosanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.132 3.2.1.132]), cellulase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.4 3.2.1.4]), licheninase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.73 3.2.1.73]), endo-1,4-β-xylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.8 3.2.1.8]) and reducing-end-xylose releasing exo-oligoxylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.156 3.2.1.156]).

== Kinetics and Mechanism ==
GH8 enzymes are inverting enzymes, as first shown by Fiebrobe ''et al.'' on endoglucanase C from ''Clostridium cellulolyticum'' (CelCCC) <CITE>REF5</CITE>.

== Catalytic Residues ==
The general acid (proton donor to the leaving group) was first identified in CelA from ''C. thermocellum'' as Glu95 <cite>REF2</cite>.
The general base (proton acceptor from the nucleophilic water) of GH8a subfamily was first identified in CelA from ''C. thermocellum'' as Asp278 <cite>REF2</cite>.
The general base of GH8b subfamily was first identified in chitosanase from ''Bacillus'' sp. K17 as Glu309 based on its crystal structure and by making E309Q mutant <cite>REF1</cite>.

== Subfamilies ==
GH8 enzymes are divided into at least three subfamilies, depending on the position of the general base <cite>REF1</cite>.
GH8a has the general base (Asp) at the N-terminal end of α8 helix. GH8a contains cellulases, xylanases and other enzymes.
In GH8b enzymes, the Asp residue is replaced by Asn, and the general base is a Glu residue located in a long loop inserted between α7 and α8 helices. GH8b contains chitosanases, licheninases, cellulases and other enzymes.
The position of the general base in GH8c is unknown.

== Three-dimensional structures ==
Several three-dimensional structures of GH8 members from bacterial origin have been solved. The first solved 3-D structure was endoglucanase CelA from ''Clostridium thermocellum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) in 1996 <cite>REF2</cite>. As members of Clan GH-M they have a (α/α)<sub>6</sub> fold similar to [[Glycoside Hydrolase Family 48]]. The general acid residue is located at the N-terminal end of α4 helix. Position of the general base differ among [[#Subfamilies]]. Atomic (0.94 Å) resolution structure of CelA in complex with substrate ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1KWF PDB 1kwf]) has been determined <cite>REF3</cite>.

== Glycosynthase ==
Reducing-end-xylose releasing exo-oligoxylanase from ''Bacillus halodurans'' C-125 is the first inverting GH that was converted to glycosynthase by mutating the general base residue <cite>REF4</cite>.

== Family Firsts ==
;First gene cloning: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF6</cite>
;First sterochemistry determination: Endoglucanase C from ''Clostridium cellulolyticum'' (CelCCC) <cite>REF5</cite>
;First general acid residue identification: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF2</cite>
;First general base residue identification of GH8a: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF2</cite>
;First general base residue identification of GH8b: Chitosanase from ''Bacillus'' sp. K17 by crystal structure and a mutant <cite>REF1</cite>.
;First 3-D structure: Endoglucanase CelA from ''Clostridium thermocellum'' by X-ray crystallography ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=15465062
#REF2 pmid=8805535
#REF3 pmid=11884144
#REF4 pmid=16301312
#REF5 pmid=8223599
#REF6 pmid=3980433
</biblio>

[[Category:Glycoside Hydrolase Families|GH008]]

Glycoside Hydrolase Family 8

2009-08-06T01:48:59Z

Motomitsu Kitaoka: /* Family Firsts */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]] and [[User:ShinyaFushinobu|Shinya Fushinobu]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 8'''
|-
|'''Clan'''
|GH-M
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH8.html
|}
</div>

== Substrate specificities ==
GH8 enzymes cleave β-1,4 linkages of β-1,4 glucans, xylans (or xylooligosaccharides), chitosans, and lichenans (1,3-1,4-β-D-glucan). All of GH8 members have been found from Bacteria, and there is no members from Eukaryotic or Archaeal origin. The majority of the enzymes are endo-acting enzymes, but one member has an exo-activity that releases β-D-xylose residues from the reducing end of xylooligosaccharides. The substrate specificities found in GH8 are: chitosanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.132 3.2.1.132]), cellulase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.4 3.2.1.4]), licheninase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.73 3.2.1.73]), endo-1,4-β-xylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.8 3.2.1.8]) and reducing-end-xylose releasing exo-oligoxylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.156 3.2.1.156]).

== Kinetics and Mechanism ==
GH8 enzymes are inverting enzymes, as first shown by Fiebrobe ''et al.'' on endoglucanase C from ''Clostridium cellulolyticum'' (CelCCC) <CITE>REF5</CITE>.

== Catalytic Residues ==
The general acid (proton donor to the leaving group) was first identified in CelA from ''C. thermocellum'' as Glu95 <cite>REF2</cite>.
The general base (proton acceptor from the nucleophilic water) of GH8a subfamily was first identified in CelA from ''C. thermocellum'' as Asp278 <cite>REF2</cite>.
The general base of GH8b subfamily was first identified in chitosanase from ''Bacillus'' sp. K17 as Glu309 based on its crystal structure and by making E309Q mutant <cite>REF1</cite>.

== Subfamilies ==
GH8 enzymes are divided into at least three subfamilies, depending on the position of the general base <cite>REF1</cite>.
GH8a has the general base (Asp) at the N-terminal end of α8 helix. GH8a contains cellulases, xylanases and other enzymes.
In GH8b enzymes, the Asp residue is replaced by Asn, and the general base is a Glu residue located in a long loop inserted between α7 and α8 helices. GH8b contains chitosanases, licheninases, cellulases and other enzymes.
The position of the general base in GH8c is unknown.

== Three-dimensional structures ==
Several three-dimensional structures of GH8 members from bacterial origin have been solved. The first solved 3-D structure was endoglucanase CelA from ''Clostridium thermocellum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) in 1996 <cite>REF2</cite>. As members of Clan GH-M they have a (α/α)<sub>6</sub> fold similar to [[Glycoside Hydrolase Family 48]]. The general acid residue is located at the N-terminal end of α4 helix. Position of the general base differ among [[#Subfamilies]]. Atomic (0.94 Å) resolution structure of CelA in complex with substrate ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1KWF PDB 1kwf]) has been determined <cite>REF3</cite>.

== Glycosynthase ==
Reducing-end-xylose releasing exo-oligoxylanase from ''Bacillus halodurans'' C-125 is the first inverting GH that was converted to glycosynthase by mutating the general base residue <cite>REF4</cite>.

== Family Firsts ==
;First gene cloning: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF6</cite>
;First sterochemistry determination: Endoglucanase C from ''Clostridium cellulolyticum'' (CelCCC) <cite>REF4</cite>
;First general acid residue identification: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF6</cite>
;First general base residue identification of GH8a: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF6</cite>
;First general base residue identification of GH8b: Chitosanase from ''Bacillus'' sp. K17 by crystal structure and a mutant <cite>REF1</cite>.
;First 3-D structure: Endoglucanase CelA from ''Clostridium thermocellum'' by X-ray crystallography ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=15465062
#REF2 pmid=8805535
#REF3 pmid=11884144
#REF4 pmid=16301312
#REF5 pmid=8223599
#REF6 pmid=3980433
</biblio>

[[Category:Glycoside Hydrolase Families|GH008]]

Glycoside Hydrolase Family 8

2009-08-06T01:46:09Z

Motomitsu Kitaoka: /* Catalytic Residues */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]] and [[User:ShinyaFushinobu|Shinya Fushinobu]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 8'''
|-
|'''Clan'''
|GH-M
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH8.html
|}
</div>

== Substrate specificities ==
GH8 enzymes cleave β-1,4 linkages of β-1,4 glucans, xylans (or xylooligosaccharides), chitosans, and lichenans (1,3-1,4-β-D-glucan). All of GH8 members have been found from Bacteria, and there is no members from Eukaryotic or Archaeal origin. The majority of the enzymes are endo-acting enzymes, but one member has an exo-activity that releases β-D-xylose residues from the reducing end of xylooligosaccharides. The substrate specificities found in GH8 are: chitosanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.132 3.2.1.132]), cellulase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.4 3.2.1.4]), licheninase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.73 3.2.1.73]), endo-1,4-β-xylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.8 3.2.1.8]) and reducing-end-xylose releasing exo-oligoxylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.156 3.2.1.156]).

== Kinetics and Mechanism ==
GH8 enzymes are inverting enzymes, as first shown by Fiebrobe ''et al.'' on endoglucanase C from ''Clostridium cellulolyticum'' (CelCCC) <CITE>REF5</CITE>.

== Catalytic Residues ==
The general acid (proton donor to the leaving group) was first identified in CelA from ''C. thermocellum'' as Glu95 <cite>REF2</cite>.
The general base (proton acceptor from the nucleophilic water) of GH8a subfamily was first identified in CelA from ''C. thermocellum'' as Asp278 <cite>REF2</cite>.
The general base of GH8b subfamily was first identified in chitosanase from ''Bacillus'' sp. K17 as Glu309 based on its crystal structure and by making E309Q mutant <cite>REF1</cite>.

== Subfamilies ==
GH8 enzymes are divided into at least three subfamilies, depending on the position of the general base <cite>REF1</cite>.
GH8a has the general base (Asp) at the N-terminal end of α8 helix. GH8a contains cellulases, xylanases and other enzymes.
In GH8b enzymes, the Asp residue is replaced by Asn, and the general base is a Glu residue located in a long loop inserted between α7 and α8 helices. GH8b contains chitosanases, licheninases, cellulases and other enzymes.
The position of the general base in GH8c is unknown.

== Three-dimensional structures ==
Several three-dimensional structures of GH8 members from bacterial origin have been solved. The first solved 3-D structure was endoglucanase CelA from ''Clostridium thermocellum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) in 1996 <cite>REF2</cite>. As members of Clan GH-M they have a (α/α)<sub>6</sub> fold similar to [[Glycoside Hydrolase Family 48]]. The general acid residue is located at the N-terminal end of α4 helix. Position of the general base differ among [[#Subfamilies]]. Atomic (0.94 Å) resolution structure of CelA in complex with substrate ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1KWF PDB 1kwf]) has been determined <cite>REF3</cite>.

== Glycosynthase ==
Reducing-end-xylose releasing exo-oligoxylanase from ''Bacillus halodurans'' C-125 is the first inverting GH that was converted to glycosynthase by mutating the general base residue <cite>REF4</cite>.

== Family Firsts ==
;First gene cloning: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF6</cite>
;First sterochemistry determination: Cite some reference here, with a ''short'' explanation .
;First general acid residue identification:
;First general base residue identification of GH8a:
;First general base residue identification of GH8b: Chitosanase from ''Bacillus'' sp. K17 by crystal structure and a mutant <cite>REF1</cite>.
;First 3-D structure: Endoglucanase CelA from ''Clostridium thermocellum'' by X-ray crystallography ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=15465062
#REF2 pmid=8805535
#REF3 pmid=11884144
#REF4 pmid=16301312
#REF5 pmid=8223599
#REF6 pmid=3980433
</biblio>

[[Category:Glycoside Hydrolase Families|GH008]]

Glycoside Hydrolase Family 8

2009-08-06T01:45:14Z

Motomitsu Kitaoka: /* Catalytic Residues */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]] and [[User:ShinyaFushinobu|Shinya Fushinobu]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 8'''
|-
|'''Clan'''
|GH-M
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH8.html
|}
</div>

== Substrate specificities ==
GH8 enzymes cleave β-1,4 linkages of β-1,4 glucans, xylans (or xylooligosaccharides), chitosans, and lichenans (1,3-1,4-β-D-glucan). All of GH8 members have been found from Bacteria, and there is no members from Eukaryotic or Archaeal origin. The majority of the enzymes are endo-acting enzymes, but one member has an exo-activity that releases β-D-xylose residues from the reducing end of xylooligosaccharides. The substrate specificities found in GH8 are: chitosanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.132 3.2.1.132]), cellulase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.4 3.2.1.4]), licheninase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.73 3.2.1.73]), endo-1,4-β-xylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.8 3.2.1.8]) and reducing-end-xylose releasing exo-oligoxylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.156 3.2.1.156]).

== Kinetics and Mechanism ==
GH8 enzymes are inverting enzymes, as first shown by Fiebrobe ''et al.'' on endoglucanase C from ''Clostridium cellulolyticum'' (CelCCC) <CITE>REF5</CITE>.

== Catalytic Residues ==
The general acid (proton donor to the leaving group) was first identified in CelA from ''C. thermocellum'' as Glu95 <cite>REF#2</cite>.
The general base (proton acceptor from the nucleophilic water) of GH8a subfamily was first identified in CelA from ''C. thermocellum'' as Asp278 <cite>REF#2</cite>.
The general base of GH8b subfamily was first identified in chitosanase from ''Bacillus'' sp. K17 as Glu309 based on its crystal structure and by making E309Q mutant <cite>REF1</cite>.

== Subfamilies ==
GH8 enzymes are divided into at least three subfamilies, depending on the position of the general base <cite>REF1</cite>.
GH8a has the general base (Asp) at the N-terminal end of α8 helix. GH8a contains cellulases, xylanases and other enzymes.
In GH8b enzymes, the Asp residue is replaced by Asn, and the general base is a Glu residue located in a long loop inserted between α7 and α8 helices. GH8b contains chitosanases, licheninases, cellulases and other enzymes.
The position of the general base in GH8c is unknown.

== Three-dimensional structures ==
Several three-dimensional structures of GH8 members from bacterial origin have been solved. The first solved 3-D structure was endoglucanase CelA from ''Clostridium thermocellum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) in 1996 <cite>REF2</cite>. As members of Clan GH-M they have a (α/α)<sub>6</sub> fold similar to [[Glycoside Hydrolase Family 48]]. The general acid residue is located at the N-terminal end of α4 helix. Position of the general base differ among [[#Subfamilies]]. Atomic (0.94 Å) resolution structure of CelA in complex with substrate ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1KWF PDB 1kwf]) has been determined <cite>REF3</cite>.

== Glycosynthase ==
Reducing-end-xylose releasing exo-oligoxylanase from ''Bacillus halodurans'' C-125 is the first inverting GH that was converted to glycosynthase by mutating the general base residue <cite>REF4</cite>.

== Family Firsts ==
;First gene cloning: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF6</cite>
;First sterochemistry determination: Cite some reference here, with a ''short'' explanation .
;First general acid residue identification:
;First general base residue identification of GH8a:
;First general base residue identification of GH8b: Chitosanase from ''Bacillus'' sp. K17 by crystal structure and a mutant <cite>REF1</cite>.
;First 3-D structure: Endoglucanase CelA from ''Clostridium thermocellum'' by X-ray crystallography ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=15465062
#REF2 pmid=8805535
#REF3 pmid=11884144
#REF4 pmid=16301312
#REF5 pmid=8223599
#REF6 pmid=3980433
</biblio>

[[Category:Glycoside Hydrolase Families|GH008]]

Glycoside Hydrolase Family 8

2009-08-06T01:43:41Z

Motomitsu Kitaoka: /* Catalytic Residues */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]] and [[User:ShinyaFushinobu|Shinya Fushinobu]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 8'''
|-
|'''Clan'''
|GH-M
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH8.html
|}
</div>

== Substrate specificities ==
GH8 enzymes cleave β-1,4 linkages of β-1,4 glucans, xylans (or xylooligosaccharides), chitosans, and lichenans (1,3-1,4-β-D-glucan). All of GH8 members have been found from Bacteria, and there is no members from Eukaryotic or Archaeal origin. The majority of the enzymes are endo-acting enzymes, but one member has an exo-activity that releases β-D-xylose residues from the reducing end of xylooligosaccharides. The substrate specificities found in GH8 are: chitosanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.132 3.2.1.132]), cellulase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.4 3.2.1.4]), licheninase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.73 3.2.1.73]), endo-1,4-β-xylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.8 3.2.1.8]) and reducing-end-xylose releasing exo-oligoxylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.156 3.2.1.156]).

== Kinetics and Mechanism ==
GH8 enzymes are inverting enzymes, as first shown by Fiebrobe ''et al.'' on endoglucanase C from ''Clostridium cellulolyticum'' (CelCCC) <CITE>REF5</CITE>.

== Catalytic Residues ==
The general acid (proton donor to the leaving group) was first identified in CelA from ''C. thermocellum'' as Glu95 <CITE>REF#4</CITE>.
The general base (proton acceptor from the nucleophilic water) of GH8a subfamily was first identified in CelA from ''C. thermocellum'' as Asp278 <CITE>REF#4</CITE>.
The general base of GH8b subfamily was first identified in chitosanase from ''Bacillus'' sp. K17 as Glu309 based on its crystal structure and by making E309Q mutant <cite>REF1</cite>.

== Subfamilies ==
GH8 enzymes are divided into at least three subfamilies, depending on the position of the general base <cite>REF1</cite>.
GH8a has the general base (Asp) at the N-terminal end of α8 helix. GH8a contains cellulases, xylanases and other enzymes.
In GH8b enzymes, the Asp residue is replaced by Asn, and the general base is a Glu residue located in a long loop inserted between α7 and α8 helices. GH8b contains chitosanases, licheninases, cellulases and other enzymes.
The position of the general base in GH8c is unknown.

== Three-dimensional structures ==
Several three-dimensional structures of GH8 members from bacterial origin have been solved. The first solved 3-D structure was endoglucanase CelA from ''Clostridium thermocellum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) in 1996 <cite>REF2</cite>. As members of Clan GH-M they have a (α/α)<sub>6</sub> fold similar to [[Glycoside Hydrolase Family 48]]. The general acid residue is located at the N-terminal end of α4 helix. Position of the general base differ among [[#Subfamilies]]. Atomic (0.94 Å) resolution structure of CelA in complex with substrate ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1KWF PDB 1kwf]) has been determined <cite>REF3</cite>.

== Glycosynthase ==
Reducing-end-xylose releasing exo-oligoxylanase from ''Bacillus halodurans'' C-125 is the first inverting GH that was converted to glycosynthase by mutating the general base residue <cite>REF4</cite>.

== Family Firsts ==
;First gene cloning: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF6</cite>
;First sterochemistry determination: Cite some reference here, with a ''short'' explanation .
;First general acid residue identification:
;First general base residue identification of GH8a:
;First general base residue identification of GH8b: Chitosanase from ''Bacillus'' sp. K17 by crystal structure and a mutant <cite>REF1</cite>.
;First 3-D structure: Endoglucanase CelA from ''Clostridium thermocellum'' by X-ray crystallography ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=15465062
#REF2 pmid=8805535
#REF3 pmid=11884144
#REF4 pmid=16301312
#REF5 pmid=8223599
#REF6 pmid=3980433
</biblio>

[[Category:Glycoside Hydrolase Families|GH008]]

Glycoside Hydrolase Family 8

2009-08-06T01:33:53Z

Motomitsu Kitaoka: /* References */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]] and [[User:ShinyaFushinobu|Shinya Fushinobu]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 8'''
|-
|'''Clan'''
|GH-M
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH8.html
|}
</div>

== Substrate specificities ==
GH8 enzymes cleave β-1,4 linkages of β-1,4 glucans, xylans (or xylooligosaccharides), chitosans, and lichenans (1,3-1,4-β-D-glucan). All of GH8 members have been found from Bacteria, and there is no members from Eukaryotic or Archaeal origin. The majority of the enzymes are endo-acting enzymes, but one member has an exo-activity that releases β-D-xylose residues from the reducing end of xylooligosaccharides. The substrate specificities found in GH8 are: chitosanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.132 3.2.1.132]), cellulase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.4 3.2.1.4]), licheninase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.73 3.2.1.73]), endo-1,4-β-xylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.8 3.2.1.8]) and reducing-end-xylose releasing exo-oligoxylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.156 3.2.1.156]).

== Kinetics and Mechanism ==
GH8 enzymes are inverting enzymes, as first shown by Fiebrobe ''et al.'' on endoglucanase C from ''Clostridium cellulolyticum'' (CelCCC) <CITE>REF5</CITE>.

== Catalytic Residues ==
The general acid (proton donor to the leaving group) was first suggested/identified in ... as Glu...
The general base (proton acceptor from the nucleophilic water) of GH8a subfamily was first suggested/identified in ... as Asp...
The general base of GH8b subfamily was first identified in chitosanase from ''Bacillus'' sp. K17 as Glu309 based on its crystal structure and by making E309Q mutant <cite>REF1</cite>.

== Subfamilies ==
GH8 enzymes are divided into at least three subfamilies, depending on the position of the general base <cite>REF1</cite>.
GH8a has the general base (Asp) at the N-terminal end of α8 helix. GH8a contains cellulases, xylanases and other enzymes.
In GH8b enzymes, the Asp residue is replaced by Asn, and the general base is a Glu residue located in a long loop inserted between α7 and α8 helices. GH8b contains chitosanases, licheninases, cellulases and other enzymes.
The position of the general base in GH8c is unknown.

== Three-dimensional structures ==
Several three-dimensional structures of GH8 members from bacterial origin have been solved. The first solved 3-D structure was endoglucanase CelA from ''Clostridium thermocellum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) in 1996 <cite>REF2</cite>. As members of Clan GH-M they have a (α/α)<sub>6</sub> fold similar to [[Glycoside Hydrolase Family 48]]. The general acid residue is located at the N-terminal end of α4 helix. Position of the general base differ among [[#Subfamilies]]. Atomic (0.94 Å) resolution structure of CelA in complex with substrate ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1KWF PDB 1kwf]) has been determined <cite>REF3</cite>.

== Glycosynthase ==
Reducing-end-xylose releasing exo-oligoxylanase from ''Bacillus halodurans'' C-125 is the first inverting GH that was converted to glycosynthase by mutating the general base residue <cite>REF4</cite>.

== Family Firsts ==
;First gene cloning: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF6</cite>
;First sterochemistry determination: Cite some reference here, with a ''short'' explanation .
;First general acid residue identification:
;First general base residue identification of GH8a:
;First general base residue identification of GH8b: Chitosanase from ''Bacillus'' sp. K17 by crystal structure and a mutant <cite>REF1</cite>.
;First 3-D structure: Endoglucanase CelA from ''Clostridium thermocellum'' by X-ray crystallography ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=15465062
#REF2 pmid=8805535
#REF3 pmid=11884144
#REF4 pmid=16301312
#REF5 pmid=8223599
#REF6 pmid=3980433
</biblio>

[[Category:Glycoside Hydrolase Families|GH008]]

Glycoside Hydrolase Family 8

2009-08-06T01:28:44Z

Motomitsu Kitaoka: /* Kinetics and Mechanism */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]] and [[User:ShinyaFushinobu|Shinya Fushinobu]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 8'''
|-
|'''Clan'''
|GH-M
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH8.html
|}
</div>

== Substrate specificities ==
GH8 enzymes cleave β-1,4 linkages of β-1,4 glucans, xylans (or xylooligosaccharides), chitosans, and lichenans (1,3-1,4-β-D-glucan). All of GH8 members have been found from Bacteria, and there is no members from Eukaryotic or Archaeal origin. The majority of the enzymes are endo-acting enzymes, but one member has an exo-activity that releases β-D-xylose residues from the reducing end of xylooligosaccharides. The substrate specificities found in GH8 are: chitosanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.132 3.2.1.132]), cellulase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.4 3.2.1.4]), licheninase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.73 3.2.1.73]), endo-1,4-β-xylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.8 3.2.1.8]) and reducing-end-xylose releasing exo-oligoxylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.156 3.2.1.156]).

== Kinetics and Mechanism ==
GH8 enzymes are inverting enzymes, as first shown by Fiebrobe ''et al.'' on endoglucanase C from ''Clostridium cellulolyticum'' (CelCCC) <CITE>REF5</CITE>.

== Catalytic Residues ==
The general acid (proton donor to the leaving group) was first suggested/identified in ... as Glu...
The general base (proton acceptor from the nucleophilic water) of GH8a subfamily was first suggested/identified in ... as Asp...
The general base of GH8b subfamily was first identified in chitosanase from ''Bacillus'' sp. K17 as Glu309 based on its crystal structure and by making E309Q mutant <cite>REF1</cite>.

== Subfamilies ==
GH8 enzymes are divided into at least three subfamilies, depending on the position of the general base <cite>REF1</cite>.
GH8a has the general base (Asp) at the N-terminal end of α8 helix. GH8a contains cellulases, xylanases and other enzymes.
In GH8b enzymes, the Asp residue is replaced by Asn, and the general base is a Glu residue located in a long loop inserted between α7 and α8 helices. GH8b contains chitosanases, licheninases, cellulases and other enzymes.
The position of the general base in GH8c is unknown.

== Three-dimensional structures ==
Several three-dimensional structures of GH8 members from bacterial origin have been solved. The first solved 3-D structure was endoglucanase CelA from ''Clostridium thermocellum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) in 1996 <cite>REF2</cite>. As members of Clan GH-M they have a (α/α)<sub>6</sub> fold similar to [[Glycoside Hydrolase Family 48]]. The general acid residue is located at the N-terminal end of α4 helix. Position of the general base differ among [[#Subfamilies]]. Atomic (0.94 Å) resolution structure of CelA in complex with substrate ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1KWF PDB 1kwf]) has been determined <cite>REF3</cite>.

== Glycosynthase ==
Reducing-end-xylose releasing exo-oligoxylanase from ''Bacillus halodurans'' C-125 is the first inverting GH that was converted to glycosynthase by mutating the general base residue <cite>REF4</cite>.

== Family Firsts ==
;First gene cloning: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF6</cite>
;First sterochemistry determination: Cite some reference here, with a ''short'' explanation .
;First general acid residue identification:
;First general base residue identification of GH8a:
;First general base residue identification of GH8b: Chitosanase from ''Bacillus'' sp. K17 by crystal structure and a mutant <cite>REF1</cite>.
;First 3-D structure: Endoglucanase CelA from ''Clostridium thermocellum'' by X-ray crystallography ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=15465062
#REF2 pmid=8805535
#REF3 pmid=11884144
#REF4 pmid=16301312
#REF6 pmid=3980433
</biblio>

[[Category:Glycoside Hydrolase Families|GH008]]

Glycoside Hydrolase Family 8

2009-08-05T09:04:03Z

Motomitsu Kitaoka: /* Kinetics and Mechanism */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]] and [[User:ShinyaFushinobu|Shinya Fushinobu]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 8'''
|-
|'''Clan'''
|GH-M
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH8.html
|}
</div>

== Substrate specificities ==
GH8 enzymes cleave β-1,4 linkages of β-1,4 glucans, xylans (or xylooligosaccharides), chitosans, and lichenans (1,3-1,4-β-D-glucan). All of GH8 members have been found from Bacteria, and there is no members from Eukaryotic or Archaeal origin. The majority of the enzymes are endo-acting enzymes, but one member has an exo-activity that releases β-D-xylose residues from the reducing end of xylooligosaccharides. The substrate specificities found in GH8 are: chitosanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.132 3.2.1.132]), cellulase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.4 3.2.1.4]), licheninase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.73 3.2.1.73]), endo-1,4-β-xylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.8 3.2.1.8]) and reducing-end-xylose releasing exo-oligoxylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.156 3.2.1.156]).

== Kinetics and Mechanism ==
GH8 enzymes are inverting enzymes, as first shown by .... on .

== Catalytic Residues ==
The general acid (proton donor to the leaving group) was first suggested/identified in ... as Glu...
The general base (proton acceptor from the nucleophilic water) of GH8a subfamily was first suggested/identified in ... as Asp...
The general base of GH8b subfamily was first identified in chitosanase from ''Bacillus'' sp. K17 as Glu309 based on its crystal structure and by making E309Q mutant <cite>REF1</cite>.

== Subfamilies ==
GH8 enzymes are divided into at least three subfamilies, depending on the position of the general base <cite>REF1</cite>.
GH8a has the general base (Asp) at the N-terminal end of α8 helix. GH8a contains cellulases, xylanases and other enzymes.
In GH8b enzymes, the Asp residue is replaced by Asn, and the general base is a Glu residue located in a long loop inserted between α7 and α8 helices. GH8b contains chitosanases, licheninases, cellulases and other enzymes.
The position of the general base in GH8c is unknown.

== Three-dimensional structures ==
Several three-dimensional structures of GH8 members from bacterial origin have been solved. The first solved 3-D structure was endoglucanase CelA from ''Clostridium thermocellum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) in 1996 <cite>REF2</cite>. As members of Clan GH-M they have a (α/α)<sub>6</sub> fold similar to [[Glycoside Hydrolase Family 48]]. The general acid residue is located at the N-terminal end of α4 helix. Position of the general base differ among [[#Subfamilies]]. Atomic (0.94 Å) resolution structure of CelA in complex with substrate ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1KWF PDB 1kwf]) has been determined <cite>REF3</cite>.

== Glycosynthase ==
Reducing-end-xylose releasing exo-oligoxylanase from ''Bacillus halodurans'' C-125 is the first inverting GH that was converted to glycosynthase by mutating the general base residue <cite>REF4</cite>.

== Family Firsts ==
;First gene cloning: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF6</cite>
;First sterochemistry determination: Cite some reference here, with a ''short'' explanation .
;First general acid residue identification:
;First general base residue identification of GH8a:
;First general base residue identification of GH8b: Chitosanase from ''Bacillus'' sp. K17 by crystal structure and a mutant <cite>REF1</cite>.
;First 3-D structure: Endoglucanase CelA from ''Clostridium thermocellum'' by X-ray crystallography ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=15465062
#REF2 pmid=8805535
#REF3 pmid=11884144
#REF4 pmid=16301312
#REF6 pmid=3980433
</biblio>

[[Category:Glycoside Hydrolase Families|GH008]]

Glycoside Hydrolase Family 8

2009-08-05T08:22:52Z

Motomitsu Kitaoka: /* Kinetics and Mechanism */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]] and [[User:ShinyaFushinobu|Shinya Fushinobu]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 8'''
|-
|'''Clan'''
|GH-M
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH8.html
|}
</div>

== Substrate specificities ==
GH8 enzymes cleave β-1,4 linkages of β-1,4 glucans, xylans (or xylooligosaccharides), chitosans, and lichenans (1,3-1,4-β-D-glucan). All of GH8 members have been found from Bacteria, and there is no members from Eukaryotic or Archaeal origin. The majority of the enzymes are endo-acting enzymes, but one member has an exo-activity that releases β-D-xylose residues from the reducing end of xylooligosaccharides. The substrate specificities found in GH8 are: chitosanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.132 3.2.1.132]), cellulase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.4 3.2.1.4]), licheninase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.73 3.2.1.73]), endo-1,4-β-xylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.8 3.2.1.8]) and reducing-end-xylose releasing exo-oligoxylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.156 3.2.1.156]).

== Kinetics and Mechanism ==
GH8 enzymes are inverting enzymes, as first shown by Cornet ''et al.'' <cite>ref5</cite> on celA from ''Clostridium thermocellum''.

== Catalytic Residues ==
The general acid (proton donor to the leaving group) was first suggested/identified in ... as Glu...
The general base (proton acceptor from the nucleophilic water) of GH8a subfamily was first suggested/identified in ... as Asp...
The general base of GH8b subfamily was first identified in chitosanase from ''Bacillus'' sp. K17 as Glu309 based on its crystal structure and by making E309Q mutant <cite>REF1</cite>.

== Subfamilies ==
GH8 enzymes are divided into at least three subfamilies, depending on the position of the general base <cite>REF1</cite>.
GH8a has the general base (Asp) at the N-terminal end of α8 helix. GH8a contains cellulases, xylanases and other enzymes.
In GH8b enzymes, the Asp residue is replaced by Asn, and the general base is a Glu residue located in a long loop inserted between α7 and α8 helices. GH8b contains chitosanases, licheninases, cellulases and other enzymes.
The position of the general base in GH8c is unknown.

== Three-dimensional structures ==
Several three-dimensional structures of GH8 members from bacterial origin have been solved. The first solved 3-D structure was endoglucanase CelA from ''Clostridium thermocellum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) in 1996 <cite>REF2</cite>. As members of Clan GH-M they have a (α/α)<sub>6</sub> fold similar to [[Glycoside Hydrolase Family 48]]. The general acid residue is located at the N-terminal end of α4 helix. Position of the general base differ among [[#Subfamilies]]. Atomic (0.94 Å) resolution structure of CelA in complex with substrate ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1KWF PDB 1kwf]) has been determined <cite>REF3</cite>.

== Glycosynthase ==
Reducing-end-xylose releasing exo-oligoxylanase from ''Bacillus halodurans'' C-125 is the first inverting GH that was converted to glycosynthase by mutating the general base residue <cite>REF4</cite>.

== Family Firsts ==
;First gene cloning: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF6</cite>
;First sterochemistry determination: Cite some reference here, with a ''short'' explanation .
;First general acid residue identification:
;First general base residue identification of GH8a:
;First general base residue identification of GH8b: Chitosanase from ''Bacillus'' sp. K17 by crystal structure and a mutant <cite>REF1</cite>.
;First 3-D structure: Endoglucanase CelA from ''Clostridium thermocellum'' by X-ray crystallography ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=15465062
#REF2 pmid=8805535
#REF3 pmid=11884144
#REF4 pmid=16301312
#REF6 pmid=3980433
</biblio>

[[Category:Glycoside Hydrolase Families|GH008]]

Glycoside Hydrolase Family 8

2009-08-05T08:21:38Z

Motomitsu Kitaoka: /* Kinetics and Mechanism */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]] and [[User:ShinyaFushinobu|Shinya Fushinobu]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 8'''
|-
|'''Clan'''
|GH-M
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH8.html
|}
</div>

== Substrate specificities ==
GH8 enzymes cleave β-1,4 linkages of β-1,4 glucans, xylans (or xylooligosaccharides), chitosans, and lichenans (1,3-1,4-β-D-glucan). All of GH8 members have been found from Bacteria, and there is no members from Eukaryotic or Archaeal origin. The majority of the enzymes are endo-acting enzymes, but one member has an exo-activity that releases β-D-xylose residues from the reducing end of xylooligosaccharides. The substrate specificities found in GH8 are: chitosanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.132 3.2.1.132]), cellulase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.4 3.2.1.4]), licheninase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.73 3.2.1.73]), endo-1,4-β-xylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.8 3.2.1.8]) and reducing-end-xylose releasing exo-oligoxylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.156 3.2.1.156]).

== Kinetics and Mechanism ==
GH8 enzymes are inverting enzymes, as first shown by Cornet ''et al.'' <cite ref5> on celA from ''Clostridium thermocellum''.

== Catalytic Residues ==
The general acid (proton donor to the leaving group) was first suggested/identified in ... as Glu...
The general base (proton acceptor from the nucleophilic water) of GH8a subfamily was first suggested/identified in ... as Asp...
The general base of GH8b subfamily was first identified in chitosanase from ''Bacillus'' sp. K17 as Glu309 based on its crystal structure and by making E309Q mutant <cite>REF1</cite>.

== Subfamilies ==
GH8 enzymes are divided into at least three subfamilies, depending on the position of the general base <cite>REF1</cite>.
GH8a has the general base (Asp) at the N-terminal end of α8 helix. GH8a contains cellulases, xylanases and other enzymes.
In GH8b enzymes, the Asp residue is replaced by Asn, and the general base is a Glu residue located in a long loop inserted between α7 and α8 helices. GH8b contains chitosanases, licheninases, cellulases and other enzymes.
The position of the general base in GH8c is unknown.

== Three-dimensional structures ==
Several three-dimensional structures of GH8 members from bacterial origin have been solved. The first solved 3-D structure was endoglucanase CelA from ''Clostridium thermocellum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) in 1996 <cite>REF2</cite>. As members of Clan GH-M they have a (α/α)<sub>6</sub> fold similar to [[Glycoside Hydrolase Family 48]]. The general acid residue is located at the N-terminal end of α4 helix. Position of the general base differ among [[#Subfamilies]]. Atomic (0.94 Å) resolution structure of CelA in complex with substrate ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1KWF PDB 1kwf]) has been determined <cite>REF3</cite>.

== Glycosynthase ==
Reducing-end-xylose releasing exo-oligoxylanase from ''Bacillus halodurans'' C-125 is the first inverting GH that was converted to glycosynthase by mutating the general base residue <cite>REF4</cite>.

== Family Firsts ==
;First gene cloning: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF6</cite>
;First sterochemistry determination: Cite some reference here, with a ''short'' explanation .
;First general acid residue identification:
;First general base residue identification of GH8a:
;First general base residue identification of GH8b: Chitosanase from ''Bacillus'' sp. K17 by crystal structure and a mutant <cite>REF1</cite>.
;First 3-D structure: Endoglucanase CelA from ''Clostridium thermocellum'' by X-ray crystallography ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=15465062
#REF2 pmid=8805535
#REF3 pmid=11884144
#REF4 pmid=16301312
#REF6 pmid=3980433
</biblio>

[[Category:Glycoside Hydrolase Families|GH008]]

Glycoside Hydrolase Family 8

2009-08-05T08:17:27Z

Motomitsu Kitaoka: /* References */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]] and [[User:ShinyaFushinobu|Shinya Fushinobu]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 8'''
|-
|'''Clan'''
|GH-M
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH8.html
|}
</div>

== Substrate specificities ==
GH8 enzymes cleave β-1,4 linkages of β-1,4 glucans, xylans (or xylooligosaccharides), chitosans, and lichenans (1,3-1,4-β-D-glucan). All of GH8 members have been found from Bacteria, and there is no members from Eukaryotic or Archaeal origin. The majority of the enzymes are endo-acting enzymes, but one member has an exo-activity that releases β-D-xylose residues from the reducing end of xylooligosaccharides. The substrate specificities found in GH8 are: chitosanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.132 3.2.1.132]), cellulase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.4 3.2.1.4]), licheninase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.73 3.2.1.73]), endo-1,4-β-xylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.8 3.2.1.8]) and reducing-end-xylose releasing exo-oligoxylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.156 3.2.1.156]).

== Kinetics and Mechanism ==
GH8 enzymes are inverting enzymes, as first shown by ... (ref) on ... from ....

== Catalytic Residues ==
The general acid (proton donor to the leaving group) was first suggested/identified in ... as Glu...
The general base (proton acceptor from the nucleophilic water) of GH8a subfamily was first suggested/identified in ... as Asp...
The general base of GH8b subfamily was first identified in chitosanase from ''Bacillus'' sp. K17 as Glu309 based on its crystal structure and by making E309Q mutant <cite>REF1</cite>.

== Subfamilies ==
GH8 enzymes are divided into at least three subfamilies, depending on the position of the general base <cite>REF1</cite>.
GH8a has the general base (Asp) at the N-terminal end of α8 helix. GH8a contains cellulases, xylanases and other enzymes.
In GH8b enzymes, the Asp residue is replaced by Asn, and the general base is a Glu residue located in a long loop inserted between α7 and α8 helices. GH8b contains chitosanases, licheninases, cellulases and other enzymes.
The position of the general base in GH8c is unknown.

== Three-dimensional structures ==
Several three-dimensional structures of GH8 members from bacterial origin have been solved. The first solved 3-D structure was endoglucanase CelA from ''Clostridium thermocellum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) in 1996 <cite>REF2</cite>. As members of Clan GH-M they have a (α/α)<sub>6</sub> fold similar to [[Glycoside Hydrolase Family 48]]. The general acid residue is located at the N-terminal end of α4 helix. Position of the general base differ among [[#Subfamilies]]. Atomic (0.94 Å) resolution structure of CelA in complex with substrate ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1KWF PDB 1kwf]) has been determined <cite>REF3</cite>.

== Glycosynthase ==
Reducing-end-xylose releasing exo-oligoxylanase from ''Bacillus halodurans'' C-125 is the first inverting GH that was converted to glycosynthase by mutating the general base residue <cite>REF4</cite>.

== Family Firsts ==
;First gene cloning: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF6</cite>
;First sterochemistry determination: Cite some reference here, with a ''short'' explanation .
;First general acid residue identification:
;First general base residue identification of GH8a:
;First general base residue identification of GH8b: Chitosanase from ''Bacillus'' sp. K17 by crystal structure and a mutant <cite>REF1</cite>.
;First 3-D structure: Endoglucanase CelA from ''Clostridium thermocellum'' by X-ray crystallography ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=15465062
#REF2 pmid=8805535
#REF3 pmid=11884144
#REF4 pmid=16301312
#REF6 pmid=3980433
</biblio>

[[Category:Glycoside Hydrolase Families|GH008]]

Glycoside Hydrolase Family 8

2009-08-05T08:14:24Z

Motomitsu Kitaoka: /* Family Firsts */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]] and [[User:ShinyaFushinobu|Shinya Fushinobu]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 8'''
|-
|'''Clan'''
|GH-M
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH8.html
|}
</div>

== Substrate specificities ==
GH8 enzymes cleave β-1,4 linkages of β-1,4 glucans, xylans (or xylooligosaccharides), chitosans, and lichenans (1,3-1,4-β-D-glucan). All of GH8 members have been found from Bacteria, and there is no members from Eukaryotic or Archaeal origin. The majority of the enzymes are endo-acting enzymes, but one member has an exo-activity that releases β-D-xylose residues from the reducing end of xylooligosaccharides. The substrate specificities found in GH8 are: chitosanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.132 3.2.1.132]), cellulase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.4 3.2.1.4]), licheninase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.73 3.2.1.73]), endo-1,4-β-xylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.8 3.2.1.8]) and reducing-end-xylose releasing exo-oligoxylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.156 3.2.1.156]).

== Kinetics and Mechanism ==
GH8 enzymes are inverting enzymes, as first shown by ... (ref) on ... from ....

== Catalytic Residues ==
The general acid (proton donor to the leaving group) was first suggested/identified in ... as Glu...
The general base (proton acceptor from the nucleophilic water) of GH8a subfamily was first suggested/identified in ... as Asp...
The general base of GH8b subfamily was first identified in chitosanase from ''Bacillus'' sp. K17 as Glu309 based on its crystal structure and by making E309Q mutant <cite>REF1</cite>.

== Subfamilies ==
GH8 enzymes are divided into at least three subfamilies, depending on the position of the general base <cite>REF1</cite>.
GH8a has the general base (Asp) at the N-terminal end of α8 helix. GH8a contains cellulases, xylanases and other enzymes.
In GH8b enzymes, the Asp residue is replaced by Asn, and the general base is a Glu residue located in a long loop inserted between α7 and α8 helices. GH8b contains chitosanases, licheninases, cellulases and other enzymes.
The position of the general base in GH8c is unknown.

== Three-dimensional structures ==
Several three-dimensional structures of GH8 members from bacterial origin have been solved. The first solved 3-D structure was endoglucanase CelA from ''Clostridium thermocellum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) in 1996 <cite>REF2</cite>. As members of Clan GH-M they have a (α/α)<sub>6</sub> fold similar to [[Glycoside Hydrolase Family 48]]. The general acid residue is located at the N-terminal end of α4 helix. Position of the general base differ among [[#Subfamilies]]. Atomic (0.94 Å) resolution structure of CelA in complex with substrate ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1KWF PDB 1kwf]) has been determined <cite>REF3</cite>.

== Glycosynthase ==
Reducing-end-xylose releasing exo-oligoxylanase from ''Bacillus halodurans'' C-125 is the first inverting GH that was converted to glycosynthase by mutating the general base residue <cite>REF4</cite>.

== Family Firsts ==
;First gene cloning: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF6</cite>
;First sterochemistry determination: Cite some reference here, with a ''short'' explanation .
;First general acid residue identification:
;First general base residue identification of GH8a:
;First general base residue identification of GH8b: Chitosanase from ''Bacillus'' sp. K17 by crystal structure and a mutant <cite>REF1</cite>.
;First 3-D structure: Endoglucanase CelA from ''Clostridium thermocellum'' by X-ray crystallography ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=15465062
#REF2 pmid=8805535
#REF3 pmid=11884144
#REF4 pmid=16301312
</biblio>

[[Category:Glycoside Hydrolase Families|GH008]]

Glycoside Hydrolase Family 8

2009-08-05T08:13:57Z

Motomitsu Kitaoka: /* Family Firsts */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]] and [[User:ShinyaFushinobu|Shinya Fushinobu]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 8'''
|-
|'''Clan'''
|GH-M
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH8.html
|}
</div>

== Substrate specificities ==
GH8 enzymes cleave β-1,4 linkages of β-1,4 glucans, xylans (or xylooligosaccharides), chitosans, and lichenans (1,3-1,4-β-D-glucan). All of GH8 members have been found from Bacteria, and there is no members from Eukaryotic or Archaeal origin. The majority of the enzymes are endo-acting enzymes, but one member has an exo-activity that releases β-D-xylose residues from the reducing end of xylooligosaccharides. The substrate specificities found in GH8 are: chitosanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.132 3.2.1.132]), cellulase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.4 3.2.1.4]), licheninase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.73 3.2.1.73]), endo-1,4-β-xylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.8 3.2.1.8]) and reducing-end-xylose releasing exo-oligoxylanase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.156 3.2.1.156]).

== Kinetics and Mechanism ==
GH8 enzymes are inverting enzymes, as first shown by ... (ref) on ... from ....

== Catalytic Residues ==
The general acid (proton donor to the leaving group) was first suggested/identified in ... as Glu...
The general base (proton acceptor from the nucleophilic water) of GH8a subfamily was first suggested/identified in ... as Asp...
The general base of GH8b subfamily was first identified in chitosanase from ''Bacillus'' sp. K17 as Glu309 based on its crystal structure and by making E309Q mutant <cite>REF1</cite>.

== Subfamilies ==
GH8 enzymes are divided into at least three subfamilies, depending on the position of the general base <cite>REF1</cite>.
GH8a has the general base (Asp) at the N-terminal end of α8 helix. GH8a contains cellulases, xylanases and other enzymes.
In GH8b enzymes, the Asp residue is replaced by Asn, and the general base is a Glu residue located in a long loop inserted between α7 and α8 helices. GH8b contains chitosanases, licheninases, cellulases and other enzymes.
The position of the general base in GH8c is unknown.

== Three-dimensional structures ==
Several three-dimensional structures of GH8 members from bacterial origin have been solved. The first solved 3-D structure was endoglucanase CelA from ''Clostridium thermocellum'' ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) in 1996 <cite>REF2</cite>. As members of Clan GH-M they have a (α/α)<sub>6</sub> fold similar to [[Glycoside Hydrolase Family 48]]. The general acid residue is located at the N-terminal end of α4 helix. Position of the general base differ among [[#Subfamilies]]. Atomic (0.94 Å) resolution structure of CelA in complex with substrate ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1KWF PDB 1kwf]) has been determined <cite>REF3</cite>.

== Glycosynthase ==
Reducing-end-xylose releasing exo-oligoxylanase from ''Bacillus halodurans'' C-125 is the first inverting GH that was converted to glycosynthase by mutating the general base residue <cite>REF4</cite>.

== Family Firsts ==
;First gene cloning: Cellulase (''celA'') from ''Clostridium thermocellum'' <cite>REF10</cite>
;First sterochemistry determination: Cite some reference here, with a ''short'' explanation .
;First general acid residue identification:
;First general base residue identification of GH8a:
;First general base residue identification of GH8b: Chitosanase from ''Bacillus'' sp. K17 by crystal structure and a mutant <cite>REF1</cite>.
;First 3-D structure: Endoglucanase CelA from ''Clostridium thermocellum'' by X-ray crystallography ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1CEM PDB 1cem]) <cite>REF2</cite>.

== References ==
<biblio>
#REF1 pmid=15465062
#REF2 pmid=8805535
#REF3 pmid=11884144
#REF4 pmid=16301312
</biblio>

[[Category:Glycoside Hydrolase Families|GH008]]

User:Motomitsu Kitaoka

2009-07-28T03:22:37Z

Motomitsu Kitaoka:

[[Image:KitaokaH21.jpg|right]]

'''Motomitsu Kitaoka''' is Leader of Enzyme Laboratory, National Food Research Institute, National Agriculture and Food Research Organization, Japan. He obtained Ph. D. from The University of Tokyo in 1993. He has been working on phosphorolytic enzymes for more than 20 years, especially working on developing new procedure to produce oligosaccharides practically such as a kg-scale preparation of Gal-β1,3-GlcNAc <cite>REF1</cite>. He also converted an inverting GH into glycosynthase <cite>REF2</cite>. Out of research on carbohydrate, he developed a simple (he believes it the simplest) protocol to introduce random mutations in DNA <cite>REF3</cite>.

<biblio>
#REF1 pmid=17690443
#REF2 pmid=16301312
#REF3 pmid=17406496
</biblio>

[[Category:Contributors|Kitaoka, Motomitsu]]

User:Motomitsu Kitaoka

2009-07-28T03:21:22Z

Motomitsu Kitaoka:

[[Image:KitaokaH21.jpg|right]]

'''Motomitsu Kitaoka''' is Leader of Enzyme Laboratory, National Food Research Institute, National Agriculture and Food Research Organization, Japan. He obtained Ph. D. from The University of Tokyo in 1993. He has been working on phosphorolytic enzymes for more than 20 years, especially working on developing new procedure to produce oligosaccharides practically such as a kg-scale preparation of Gal-β1,3-GlcNAc <cite>REF1</cite>. He also converted an inverting GH into glycosynthase <cite>REF2</cite>. Out of research on carbohydrate, he developed a simple (he believes it the simplest) protocol to generate random mutagenesis in DNA <cite>REF3</cite>.

<biblio>
#REF1 pmid=17690443
#REF2 pmid=16301312
#REF3 pmid=17406496
</biblio>

[[Category:Contributors|Kitaoka, Motomitsu]]

User:Motomitsu Kitaoka

2009-07-28T03:20:23Z

Motomitsu Kitaoka:

[[Image:KitaokaH21.jpg|right]]

'''Motomitsu Kitaoka''' is Leader of Enzyme Laboratory, National Food Research Institute, National Agriculture and Food Research Organization, Japan. He obtained Ph. D. from The University of Tokyo in 1993. He has been working on phosphorolytic enzymes for more than 20 years, especially working on developing new procedure to produce oligosaccharides practically such as a kg-scale preparation of Gal-β1,3-GlcNAc <cite>REF1</cite>. He also converted an inverting GH into glycosynthase <cite>REF2</cite>. Out of research on carbohydrate, he developed a simple (he believes it the simplest) protocol to generate random mutagenesis in DNA <cite>REF3</cite>.

<biblio>
#REF1 pmid=17690443
#REF2 pmid=16301312
#REF3 pmid=17406496
</biblio>

[[Category:Contributors|Kitaoka, Motomitsu]]

User:Motomitsu Kitaoka

2009-07-28T03:16:13Z

Motomitsu Kitaoka:

[[Image:KitaokaH21.jpg|right]]

'''Motomitsu Kitaoka''' is Leader of Enzyme Laboratory, National Food Research Institute, National Agriculture and Food Research Organization, Japan. He obtained Ph. D. from The University of Tokyo in 1993. He has been working on phosphorolytic enzymes for more than 20 years, especially working on developing new procedure to produce oligosaccharides practically such as a kg-scale preparation of Gal-β1,3-GlcNAc <cite>REF1</cite>. He also converted an inverting GH into glycosynthase <cite>REF2</cite>. Out of research on carbohydrate, he developed a simple (he believes it the simplest) protocol to generate random mutagenesis in DNA <cite>REF3</cite>.

[[Category:Contributors|Kitaoka, Motomitsu]]

User:Motomitsu Kitaoka

2009-07-28T03:13:02Z

Motomitsu Kitaoka:

[[Image:KitaokaH21.jpg|right]]

'''Motomitsu Kitaoka''' is Leader of Enzyme Laboratory, National Food Research Institute, National Agriculture and Food Research Organization, Japan. He obtained Ph. D. from The University of Tokyo in 1993. He has been working on phosphorolytic enzymes for more than 20 years, especially working on developing new procedure to produce oligosaccharides practically such as a kg-scale preparation of Gal-β1,3-GlcNAc. Out of research on carbohydrate, he developed a simple (he believes it the simplest) protocol to generate random mutagenesis in DNA.

[[Category:Contributors|Kitaoka, Motomitsu]]

User:Motomitsu Kitaoka

2009-07-28T03:11:05Z

Motomitsu Kitaoka:

[[Image:KitaokaH21.jpg|right]]

'''Motomitsu Kitaoka''' is Leader of Enzyme Laboratory, National Food Research Institute, National Agriculture and Food Research Organization, Japan. He obtained Ph. D. from The University of Tokyo in 1993. He has been working on phosphorolytic enzymes for more than 20 years, especially working on developing new procedure to produce oligosaccharides practically such as a kg-scale preparation of Galb1,3GlcNAc. Out of research on carbohydrate, he developed a simple (he believes it the simplest) protocol to generate random mutagenesis in DNA.

[[Category:Contributors|Kitaoka, Motomitsu]]

File:KitaokaH21.jpg

2009-07-28T03:00:10Z

Motomitsu Kitaoka:

User:Motomitsu Kitaoka

2009-07-28T02:59:43Z

Motomitsu Kitaoka:

[[Image:KitaokaH21.jpg|right]]

'''Motomitsu Kitaoka''' is Leader of Enzyme Laboratory, National Food Research Institute, National Agriculture and Food Research Organization, Japan. He has long time been working on phosphorolytic enzymes, especially working on developing new procedure to produce oligosaccharides practically. Out of research on carbohydrate, he developed a simple (he believes it the simplest) protocol to generate random mutagenesis in DNA.
[[Category:Contributors|Kitaoka, Motomitsu]]

User:Motomitsu Kitaoka

2009-07-28T02:55:15Z

Motomitsu Kitaoka:

'''Motomitsu Kitaoka''' is Leader of Enzyme Laboratory, National Food Research Institute, National Agriculture and Food Research Organization, Japan. He has long time been working on phosphorolytic enzymes, especially working on developing new procedure to produce oligosaccharides practically. Out of research on carbohydrate, he developed a simple (he believes it the simplest) protocol to generate random mutagenesis in DNA.
[[Category:Contributors|Kitaoka, Motomitsu]]

Glycoside Hydrolase Family 112

2009-07-15T02:27:51Z

Motomitsu Kitaoka: /* Three-dimensional structures */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?2.4.1.211 2.4.1.211]) <cite>REF1</cite> and β-1,4-D-galactosyl-L-rhamnose phosphorylase (EC 2.4.1.-) <cite>REF2</cite>. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) <cite>REF3</cite>, lacto-''N''-biose I phosphorylase (LNBP) <cite>REF4</cite>, and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) <cite>REF1,REF4,REF5</cite> based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) <cite>REF4</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. <cite>REF1</cite> on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of [[Glycoside Hydrolase Family 42]], supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' <cite>REF1</cite>.
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF5</cite>.
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>.
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>.

== References ==
<biblio>
#REF1 pmid=9889079
#REF2 pmid=19491100
#REF3 pmid=18183385
#REF4 pmid=18723650
#REF5 pmid=15933016
#REF6 pmid=17587697
#REF7 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-15T00:02:16Z

Motomitsu Kitaoka: /* Substrate specificities */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?2.4.1.211 2.4.1.211]) <cite>REF1</cite> and β-1,4-D-galactosyl-L-rhamnose phosphorylase (EC 2.4.1.-) <cite>REF2</cite>. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) <cite>REF3</cite>, lacto-''N''-biose I phosphorylase (LNBP) <cite>REF4</cite>, and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) <cite>REF1,REF4,REF5</cite> based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) <cite>REF4</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. <cite>REF1</cite> on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' <cite>REF1</cite>.
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF5</cite>.
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>.
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>.

== References ==
<biblio>
#REF1 pmid=9889079
#REF2 pmid=19491100
#REF3 pmid=18183385
#REF4 pmid=18723650
#REF5 pmid=15933016
#REF6 pmid=17587697
#REF7 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-15T00:01:44Z

Motomitsu Kitaoka: /* Substrate specificities */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?2.4.1.211 2.4.1.211]) <cite>REF1</cite> and β-1,4-D-galactosyl-L-rhamnose phosphorylase (EC 2.4.1.-)<cite>REF2</cite>. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) <cite>REF3</cite>, lacto-''N''-biose I phosphorylase (LNBP) <cite>REF4</cite>, and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) <cite>REF1,REF4,REF5</cite> based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) <cite>REF4</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. <cite>REF1</cite> on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' <cite>REF1</cite>.
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF5</cite>.
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>.
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>.

== References ==
<biblio>
#REF1 pmid=9889079
#REF2 pmid=19491100
#REF3 pmid=18183385
#REF4 pmid=18723650
#REF5 pmid=15933016
#REF6 pmid=17587697
#REF7 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-15T00:00:25Z

Motomitsu Kitaoka: /* Substrate specificities */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase <cite>REF1</cite> and β-1,4-D-galactosyl-L-rhamnose phosphorylase (EC [http://us.expasy.org/cgi-bin/nicezyme.pl?2.4.1.211 2.4.1.211]) <cite>REF2</cite>. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) <cite>REF3</cite>, lacto-''N''-biose I phosphorylase (LNBP) <cite>REF4</cite>, and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) <cite>REF1,REF4,REF5</cite> based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) <cite>REF4</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. <cite>REF1</cite> on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' <cite>REF1</cite>.
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF5</cite>.
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>.
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>.

== References ==
<biblio>
#REF1 pmid=9889079
#REF2 pmid=19491100
#REF3 pmid=18183385
#REF4 pmid=18723650
#REF5 pmid=15933016
#REF6 pmid=17587697
#REF7 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T23:55:59Z

Motomitsu Kitaoka: /* Family Firsts */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase <cite>REF1</cite> and β-1,4-D-galactosyl-L-rhamnose phosphorylase <cite>REF2</cite>. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) <cite>REF3</cite>, lacto-''N''-biose I phosphorylase (LNBP) <cite>REF4</cite>, and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) <cite>REF1,REF4,REF5</cite> based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) <cite>REF4</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. <cite>REF1</cite> on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' <cite>REF1</cite>.
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF5</cite>.
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>.
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>.

== References ==
<biblio>
#REF1 pmid=9889079
#REF2 pmid=19491100
#REF3 pmid=18183385
#REF4 pmid=18723650
#REF5 pmid=15933016
#REF6 pmid=17587697
#REF7 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T23:54:49Z

Motomitsu Kitaoka: /* Three-dimensional structures */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase <cite>REF1</cite> and β-1,4-D-galactosyl-L-rhamnose phosphorylase <cite>REF2</cite>. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) <cite>REF3</cite>, lacto-''N''-biose I phosphorylase (LNBP) <cite>REF4</cite>, and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) <cite>REF1,REF4,REF5</cite> based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) <cite>REF4</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. <cite>REF1</cite> on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' [1].
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [5].
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6].
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7].

== References ==
<biblio>
#REF1 pmid=9889079
#REF2 pmid=19491100
#REF3 pmid=18183385
#REF4 pmid=18723650
#REF5 pmid=15933016
#REF6 pmid=17587697
#REF7 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T23:54:09Z

Motomitsu Kitaoka: /* Kinetics and Mechanism */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase <cite>REF1</cite> and β-1,4-D-galactosyl-L-rhamnose phosphorylase <cite>REF2</cite>. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) <cite>REF3</cite>, lacto-''N''-biose I phosphorylase (LNBP) <cite>REF4</cite>, and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) <cite>REF1,REF4,REF5</cite> based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) <cite>REF4</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. <cite>REF1</cite> on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7]. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' [1].
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [5].
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6].
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7].

== References ==
<biblio>
#REF1 pmid=9889079
#REF2 pmid=19491100
#REF3 pmid=18183385
#REF4 pmid=18723650
#REF5 pmid=15933016
#REF6 pmid=17587697
#REF7 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T23:53:15Z

Motomitsu Kitaoka: /* Catalytic Residues */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase <cite>REF1</cite> and β-1,4-D-galactosyl-L-rhamnose phosphorylase <cite>REF2</cite>. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) <cite>REF3</cite>, lacto-''N''-biose I phosphorylase (LNBP) <cite>REF4</cite>, and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) <cite>REF1,REF4,REF5</cite> based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) <cite>REF4</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. [1] on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7]. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' [1].
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [5].
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6].
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7].

== References ==
<biblio>
#REF1 pmid=9889079
#REF2 pmid=19491100
#REF3 pmid=18183385
#REF4 pmid=18723650
#REF5 pmid=15933016
#REF6 pmid=17587697
#REF7 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T23:52:34Z

Motomitsu Kitaoka: /* Substrate specificities */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase <cite>REF1</cite> and β-1,4-D-galactosyl-L-rhamnose phosphorylase <cite>REF2</cite>. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) <cite>REF3</cite>, lacto-''N''-biose I phosphorylase (LNBP) <cite>REF4</cite>, and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) <cite>REF1,REF4,REF5</cite> based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) <cite>REF4</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. [1] on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6]. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7]. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' [1].
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [5].
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6].
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7].

== References ==
<biblio>
#REF1 pmid=9889079
#REF2 pmid=19491100
#REF3 pmid=18183385
#REF4 pmid=18723650
#REF5 pmid=15933016
#REF6 pmid=17587697
#REF7 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T23:49:04Z

Motomitsu Kitaoka: /* Substrate specificities */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase <cite>REF1</cite> and β-1,4-D-galactosyl-L-rhamnose phosphorylase <cite>REF2</cite>. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) <cite>REF3</cite>, lacto-''N''-biose I phosphorylase (LNBP) <cite>REF4</cite>, and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) <cite>REF1,4,5</cite> based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) <cite>REF4</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. [1] on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6]. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7]. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' [1].
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [5].
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6].
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7].

== References ==
<biblio>
#REF1 pmid=9889079
#REF2 pmid=19491100
#REF3 pmid=18183385
#REF4 pmid=18723650
#REF5 pmid=15933016
#REF6 pmid=17587697
#REF7 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

User:Motomitsu Kitaoka

2009-07-14T23:45:46Z

Motomitsu Kitaoka:

Glycoside Hydrolase Family 112

2009-07-14T08:53:49Z

Motomitsu Kitaoka: /* References */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase [1] and β-1,4-D-gaactosyl-L-rhamnose phosphorylase [2]. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) [3], lacto-''N''-biose I phosphorylase (LNBP) [4], and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) [1,4,5] based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) [4].

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. [1] on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6]. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7]. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' [1].
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [5].
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6].
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7].

== References ==
<biblio>
#REF1 pmid=9889079
#REF2 pmid=19491100
#REF3 pmid=18183385
#REF4 pmid=18723650
#REF5 pmid=15933016
#REF6 pmid=17587697
#REF7 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T08:48:18Z

Motomitsu Kitaoka: /* References */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase [1] and β-1,4-D-gaactosyl-L-rhamnose phosphorylase [2]. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) [3], lacto-''N''-biose I phosphorylase (LNBP) [4], and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) [1,4,5] based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) [4].

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. [1] on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6]. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7]. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' [1].
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [5].
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6].
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7].

== References ==
<biblio>
#REF7 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T08:45:55Z

Motomitsu Kitaoka: /* Family Firsts */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase [1] and β-1,4-D-gaactosyl-L-rhamnose phosphorylase [2]. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) [3], lacto-''N''-biose I phosphorylase (LNBP) [4], and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) [1,4,5] based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) [4].

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. [1] on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6]. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7]. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' [1].
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [5].
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6].
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7].

== References ==
<biblio>
#REF1 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T08:44:38Z

Motomitsu Kitaoka: /* Substrate specificities */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase [1] and β-1,4-D-gaactosyl-L-rhamnose phosphorylase [2]. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) [3], lacto-''N''-biose I phosphorylase (LNBP) [4], and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) [1,4,5] based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) [4].

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. [1] on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6]. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7]. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' <cite>REF1</cite>.
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF5</cite>.
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>.
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>.

== References ==
<biblio>
#REF1 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T08:40:12Z

Motomitsu Kitaoka: /* Substrate specificities */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase <cite>REF1</cite> and β-1,4-D-gaactosyl-L-rhamnose phosphorylase <cite>REF2</cite>. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) <cite>REF3</cite>, lacto-''N''-biose I phosphorylase (LNBP) <cite>REF4</cite>, and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) <cite>REF1 4 5</cite> based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) <cite>REF4</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. [1] on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6]. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7]. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' <cite>REF1</cite>.
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF5</cite>.
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>.
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>.

== References ==
<biblio>
#REF1 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T08:39:39Z

Motomitsu Kitaoka: /* Substrate specificities */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase <cite>REF1</cite> and β-1,4-D-gaactosyl-L-rhamnose phosphorylase <cite>REF2</cite>. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) <cite>REF3</cite>, lacto-''N''-biose I phosphorylase (LNBP) <cite>REF4</cite>, and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) <cite>REF1,4,5</cite> based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) <cite>REF4</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. [1] on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6]. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7]. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' <cite>REF1</cite>.
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF5</cite>.
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>.
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>.

== References ==
<biblio>
#REF1 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T08:38:05Z

Motomitsu Kitaoka: /* Substrate specificities */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase <cite>REF1</cite> and β-1,4-D-gaactosyl-L-rhamnose phosphorylase <cite>REF2</cite>. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) <cite>REF3</cite>, lacto-''N''-biose I phosphorylase (LNBP) <cite>REF4</cite>, and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) <cite>REF1</cite><cite>REF4</cite><cite>REF5</cite> based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) <cite>REF4</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. [1] on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6]. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7]. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' <cite>REF1</cite>.
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF5</cite>.
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>.
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>.

== References ==
<biblio>
#REF1 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T08:35:13Z

Motomitsu Kitaoka: /* Substrate specificities */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase <cite>REF1</cite> and β-1,4-D-gaactosyl-L-rhamnose phosphorylase <cite>REF2</cite>. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) <cite>REF3</cite>, lacto-''N''-biose I phosphorylase (LNBP) <cite>REF4</cite>, and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) <cite>REF1,4,5</cite> based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) <cite>REF4</cite>.

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. [1] on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6]. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7]. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' <cite>REF1</cite>.
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF5</cite>.
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>.
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>.

== References ==
<biblio>
#REF1 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T08:32:06Z

Motomitsu Kitaoka: /* Family Firsts */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase [1] and β-1,4-D-gaactosyl-L-rhamnose phosphorylase [2]. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) [3], lacto-''N''-biose I phosphorylase (LNBP) [4], and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) [1,4,5] based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) [4].

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. [1] on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6]. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7]. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'' <cite>REF1</cite>.
;First cloned: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF5</cite>.
;First catalytic nucleophile identification: phosphate
;First general acid/base residue identification: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF6</cite>.
;First 3-D structure: β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' <cite>REF7</cite>.

== References ==
<biblio>
#REF1 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T08:26:52Z

Motomitsu Kitaoka: /* Family Firsts */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase [1] and β-1,4-D-gaactosyl-L-rhamnose phosphorylase [2]. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) [3], lacto-''N''-biose I phosphorylase (LNBP) [4], and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) [1,4,5] based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) [4].

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. [1] on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6]. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7]. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination:
Normal 0 0 2 MicrosoftInternetExplorer4

beta-1,3-D-galactosyl-D-hexososamine phosphorylase from Bifidobacterium bifidum [5].

Normal 0 0 2 MicrosoftInternetExplorer4

First cloned

beta-1,3-D-galactosyl-D-hexososamine phosphorylase from Bifidobacterium longum
;First catalytic nucleophile identification:
phosphate
;First general acid/base residue identification:
Normal 0 0 2 MicrosoftInternetExplorer4

beta-1,3-D-galactosyl-D-hexososamine phosphorylase from Bifidobacterium longum [1].
;First 3-D structure: Cite some reference here, with a ''short'' explanation <cite>REF1</cite>.
Normal 0 0 2 MicrosoftInternetExplorer4

beta-1,3-D-galactosyl-D-hexososamine phosphorylase from Bifidobacterium longum

== References ==
<biblio>
#REF1 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T08:23:55Z

Motomitsu Kitaoka: /* Three-dimensional structures */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase [1] and β-1,4-D-gaactosyl-L-rhamnose phosphorylase [2]. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) [3], lacto-''N''-biose I phosphorylase (LNBP) [4], and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) [1,4,5] based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) [4].

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. [1] on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6]. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
The first solved 3-D structure was β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [7]. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a β-galactosidase of GH42, supporting the classification of these phosphorolytic enzymes as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination:
;First catalytic nucleophile identification:
;First general acid/base residue identification:
;First 3-D structure: Cite some reference here, with a ''short'' explanation <cite>REF1</cite>.

== References ==
<biblio>
#REF1 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]

Glycoside Hydrolase Family 112

2009-07-14T08:22:18Z

Motomitsu Kitaoka: /* Three-dimensional structures */

* [[Author]]: [[User:MotomitsuKitaoka|Motomitsu Kitaoka]]
* [[Responsible Curator]]: [[User:ShinyaFushinobu|Shinya Fushinobu]]
----

<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family 112'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH112.html
|}
</div>

== Substrate specificities ==
This family contains beta-galactoside phosphorolyzing enzymes, β-1,3-D-galactosyl-D-hexososamine phosphorylase [1] and β-1,4-D-gaactosyl-L-rhamnose phosphorylase [2]. The former enzymes are subcategorized into galacto-''N''-biose phosphorylase, (GNBP) [3], lacto-''N''-biose I phosphorylase (LNBP) [4], and galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) [1,4,5] based on the substrate preference on galacto-''N''-biose (GNB, Gal-β1,3-GalNAc) and lacto-''N''-biose I (LNB, Gal-β1,3-GlcNAc) [4].

== Kinetics and Mechanism ==
Phosphorolysis by GH112 enzymes proceeds with inversion of anomeric configuration, as first shown by Derensy-Dron et al. [1] on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium bifidum'', i.e. LNB + Pi ↔ α-galactose 1-phosphate + GlcNAc. Considering the topology of the active site structure, the reaction mechanism for inverting phosphorylase is proposed to be similar to that for inverting GH. With the aid of general acid residue, the enzymatic phosphorolysis begins with direct nucleophilic attack by phosphate on the anomeric C-1 carbon, instead of the water molecule activated by a general base residue in inverting GH reaction.

== Catalytic Residues ==
The catalytic proton donar residue was firstly estimated by mutational analysis on β-1,3-D-galactosyl-D-hexososamine phosphorylase from ''Bifidobacterium longum'' [6]. Catalytic nucleophile is phosphate.

== Three-dimensional structures ==
Normal 0 0 2 MicrosoftInternetExplorer4 The first solved 3-D structure was beta-1,3-D-galactosyl-D-hexososamine phosphorylase from Bifidobacterium longum [7]. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a beta-galactosidase of GH42, supporting the classification of GLNBP homologues as one of the GH families. A large conformational change in TIM barrel scaffold was observerd with substrate-binding.

== Family Firsts ==
;First sterochemistry determination:
;First catalytic nucleophile identification:
;First general acid/base residue identification:
;First 3-D structure: Cite some reference here, with a ''short'' explanation <cite>REF1</cite>.

== References ==
<biblio>
#REF1 pmid=19124470

</biblio>

[[Category:Glycoside Hydrolase Families]]