CAZypedia - User contributions [en-ca]

Glycoside Hydrolase Family 116

2013-11-27T15:03:31Z

Beatrice Cobucci-Ponzano:

{{CuratorApproved}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==
This family of [[glycoside hydrolases]] was discovered characterising a β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC [{{EClink}}3.2.1.45 3.2.1.45]), β-glucosidase (EC [{{EClink}}3.2.1.21 3.2.1.21]) and β-xylosidase (EC [{{EClink}}3.2.1.37 3.2.1.37]) activities from the three domains of life. The β-glycosidase from ''S. solfataricus'' (SSO1353) is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a ''[[retaining]]'' reaction mechanism. SSO1353 is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase, involved in the catabolism of glucosylceramide, which is then converted to sphingomyelin <cite>PMID17105727</cite>. Recently, a new β-N-acetylglucosaminidase from S. solfataricus (SSO3039) from the same family <cite>PMID24060745</cite> was characterized, demonstrating that it is a bifunctional β-glucosidase/β-N-acetylglucosaminidase. The phylogenetic analysis shows that GH116 can be separated in three subfamilies <cite>PMID24060745</cite>, each of which now has an enzyme characterized in detail: subfamily 1 contains GBA2 <cite>PMID17105727</cite>, subfamily 2 includes SSO3039 <cite>PMID24060745</cite>, and subfamily 3 contains SSO1353 <cite>PMID20427274</cite>. The three subfamilies are functionally different and have evolved from a common ancestor. Common characteristics of family GH116 are the specificity for β-O-glucosides and the ''[[retaining]]'' reaction mechanism. However, subfamilies 1, 2, and 3, have also specificity for glucosylceramides, N-acetyl-glucosaminides, and xylosides, respectively, and peculiar sensitivity to competitive inhibitors. In fact, GBA2 (subfamily 1) is insensitive to CBE and is inhibited by nM amounts of NB-DNJ <cite>PMID17105727</cite>, SSO3039 (subfamily 2) is sensitive to μM and mM concentrations of NB-DNJ and CBE, respectively <cite>PMID24060745</cite>, whilst SSO1353 (subfamily 3) shows mM sensitivity to both NB-DNJ and CBE <cite>PMID20427274</cite>.

== Kinetics and Mechanism ==
The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by <sup>1</sup>H-<sup>13</sup>C NMR spectroscopy analysis of the interglycosidic linkage of disaccharides formed by the transglycosylation reaction of SSO1353 with 4NP-β-Xyl <cite>PMID20427274</cite>.

== Catalytic Residues ==
The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase SSO1353 <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==
There is currently no 3-D structure representative for GH116 (see [{{CAZyDBlink}}GH116.html GH116 at CAZy DB]).

== Family Firsts ==
;First stereochemistry determination: ''S. solfataricus'' β-glycosidase SSO1353 by NMR analysis of the interglycosidic linkage of disaccharides formed by the transglycosylation reaction with 4NP-β-Xyl <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase SSO1353 by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase SSO1353 by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure: Presently unknown (see [{{CAZyDBlink}}GH116.html GH116 at CAZy DB]).

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727

#PMID24060745 pmid=24060745
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-21T15:31:51Z

Beatrice Cobucci-Ponzano:

{{CuratorApproved}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life. The β-glycosidase from ''S. solfataricus'' (SSO1353) is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a ''[[retaining]]'' reaction mechanism. SSO1353 is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase, involved in the catabolism of glucosylceramide, which is then converted to sphingomyelin <cite>PMID17105727</cite>. SSO1353 has substrate specificity and inhibitor sensitivity slightly different from those of GBA2. In fact, the archaeal enzyme can hydrolyze both aryl β-gluco and β-xylosides
and it is inhibited by both N-butyldeoxynojirimycin (NB-DNJ) and conduritol β-epoxide (CBE) <cite>PMID20427274</cite>. Instead, GBA2 is inactive on methylumbellyferyl-β-D-xylopyranoside and is relatively insensitive to CBE <cite>PMID17105727</cite>.

== Kinetics and Mechanism ==
The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by <sup>1</sup>H-<sup>13</sup>C NMR spectroscopy analysis of the interglycosidic linkage of disaccharides formed by the transglycosylation reaction of SSO1353 with 4NP-β-Xyl <cite>PMID20427274</cite>.

== Catalytic Residues ==
The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==
There is currently no 3-D structure representative for GH116 (see [{{CAZyDBlink}}GH116.html GH116 at CAZy DB]).

== Family Firsts ==
;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR analysis of the interglycosidic linkage of disaccharides formed by the transglycosylation reaction with 4NP-β-Xyl <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure: Presently unknown (see [{{CAZyDBlink}}GH116.html GH116 at CAZy DB]).

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-07T14:47:23Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life. The β-glycosidase from ''S. solfataricus'' (SSO1353) is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a ''[[retaining]]'' reaction mechanism. SSO1353 is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase, involved in the catabolism of glucosylceramide, which is then converted to sphingomyelin <cite>PMID17105727</cite>. SSO1353 has substrate specificity and inhibitor sensitivity slightly different from those of GBA2. In fact, the archaeal enzyme can hydrolyze both aryl β-gluco and β-xylosides
and it is inhibited by both N-butyldeoxynojirimycin (NB-DNJ) and conduritol β-epoxide (CBE) <cite>PMID20427274</cite>. Instead, GBA2 is inactive on methylumbellyferyl-β-D-xylopyranoside and is relatively insensitive to CBE <cite>PMID17105727</cite>.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by <sup>1</sup>H-<sup>13</sup>C NMR spectroscopy analysis of the interglycosidic linkage of disaccharides formed by the transglycosylation reaction of SSO1353 with 4NP-β-Xyl <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR analysis of the interglycosidic linkage of disaccharides formed by the transglycosylation reaction with 4NP-β-Xyl <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-07T14:43:21Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life. The β-glycosidase from ''S. solfataricus'' (SSO1353) is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a ''[[retaining]]'' reaction mechanism. SSO1353 is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase, involved in the catabolism of glucosylceramide, which is then converted to sphingomyelin <cite>PMID17105727</cite>. SSO1353 has substrate specificity and inhibitor sensitivity slightly different from those of GBA2. In fact, the archaeal enzyme can hydrolyze both aryl β-gluco and β-xylosides
and it is inhibited by both N-butyldeoxynojirimycin (NB-DNJ) and conduritol β-epoxide (CBE) <cite>PMID20427274</cite>. Instead, GBA2 is inactive on methylumbellyferyl-β-D-xylopyranoside and is relatively insensitive to CBE <cite>PMID17105727</cite>.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by <sup>1</sup>H-<sup>13</sup>C NMR spectroscopy analysis of the interglycosidic linkage of disaccharides formed by the transglycosylation reaction of SSO1353 with 4NP-β-Xyl <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR analysis of the interglycosidic linkage of disaccharides formed by the transglycosylation reaction of SSO1353 with 4NP-β-Xyl <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-07T14:38:18Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life. The β-glycosidase from ''S. solfataricus'' (SSO1353) is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a ''[[retaining]]'' reaction mechanism. SSO1353 is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase, involved in the catabolism of glucosylceramide, which is then converted to sphingomyelin <cite>PMID17105727</cite>. SSO1353 has substrate specificity and inhibitor sensitivity slightly different from those of GBA2. In fact, the archaeal enzyme can hydrolyze both aryl β-gluco and β-xylosides
and it is inhibited by both N-butyldeoxynojirimycin (NB-DNJ) and conduritol β-epoxide (CBE) <cite>PMID20427274</cite>. Instead, GBA2 is inactive on methylumbellyferyl-β-D-xylopyranoside and is relatively insensitive to CBE <cite>PMID17105727</cite>.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by <sup>1</sup>H-<sup>13</sup>C NMR spectroscopy analysis of the interglycosidic linkage of disaccharides formed by the transglycosylation reaction of SSO1353 with 4NP-β-Xyl <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-07T14:36:57Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life. The β-glycosidase from ''S. solfataricus'' (SSO1353) is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a ''[[retaining]]'' reaction mechanism. SSO1353 is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase, involved in the catabolism of glucosylceramide, which is then converted to sphingomyelin <cite>PMID17105727</cite>. SSO1353 has substrate specificity and inhibitor sensitivity slightly different from those of GBA2. In fact, the archaeal enzyme can hydrolyze both aryl β-gluco and β-xylosides
and it is inhibited by both N-butyldeoxynojirimycin (NB-DNJ) and conduritol β-epoxide (CBE) <cite>PMID20427274</cite>. Instead, GBA2 is inactive on methylumbellyferyl-β-D-xylopyranoside and is relatively insensitive to CBE <cite>PMID17105727</cite>.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by <sup>1</sup>H-<sup>13</sup>C NMR spectroscopy analysis of the interglycosidic linkage of disaccharides formed by the transglycosylation action of SSO1353 with 4NP-β-Xyl <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-07T14:36:24Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life. The β-glycosidase from ''S. solfataricus'' (SSO1353) is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a ''[[retaining]]'' reaction mechanism. SSO1353 is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase, involved in the catabolism of glucosylceramide, which is then converted to sphingomyelin <cite>PMID17105727</cite>. SSO1353 has substrate specificity and inhibitor sensitivity slightly different from those of GBA2. In fact, the archaeal enzyme can hydrolyze both aryl β-gluco and β-xylosides
and it is inhibited by both N-butyldeoxynojirimycin (NB-DNJ) and conduritol β-epoxide (CBE) <cite>PMID20427274</cite>. Instead, GBA2 is inactive on methylumbellyferyl-β-D-xylopyranoside and is relatively insensitive to CBE <cite>PMID17105727</cite>.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by <sup>1</sup>H-<sup>13</sup>C NMR spectroscopy analysis of the interglycosidic linkage of disaccharides formed by the transglycosylation action of SSO1353 with 4NP-β-Xyl <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2-
deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-07T14:35:09Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life. The β-glycosidase from ''S. solfataricus'' (SSO1353) is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a ''[[retaining]]'' reaction mechanism. SSO1353 is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase, involved in the catabolism of glucosylceramide, which is then converted to sphingomyelin <cite>PMID17105727</cite>. SSO1353 has substrate specificity and inhibitor sensitivity slightly different from those of GBA2. In fact, the archaeal enzyme can hydrolyze both aryl β-gluco and β-xylosides
and it is inhibited by both N-butyldeoxynojirimycin (NB-DNJ) and conduritol β-epoxide (CBE) <cite>PMID20427274</cite>. Instead, GBA2 is inactive on methylumbellyferyl-β-D-xylopyranoside and is relatively insensitive to CBE <cite>PMID17105727</cite>.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by <sup>1</sup>H-<sup>13</sup>C NMR spectroscopy analysis of the interglycosidic linkage of disaccharides formed by the [[transglycosylation]] action of SSO1353 with 4NP-β-Xyl <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2-
deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-07T14:30:37Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life. The β-glycosidase from ''S. solfataricus'' (SSO1353) is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a ''[[retaining]]'' reaction mechanism. SSO1353 is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase, involved in the catabolism of glucosylceramide, which is then converted to sphingomyelin <cite>PMID17105727</cite>. SSO1353 has substrate specificity and inhibitor sensitivity slightly different from those of GBA2. In fact, the archaeal enzyme can hydrolyze both aryl β-gluco and β-xylosides
and it is inhibited by both N-butyldeoxynojirimycin (NB-DNJ) and conduritol β-epoxide (CBE) <cite>PMID20427274</cite>. Instead, GBA2 is inactive on methylumbellyferyl-β-D-glucopyranoside and is relatively insensitive to CBE <cite>PMID17105727</cite>.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by <sup>1</sup>H-<sup>13</sup>C NMR spectroscopy analysis of the interglycosidic linkage of disaccharides formed by the [[transglycosylation]] action of SSO1353 with 4NP-β-Xyl <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2-
deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-07T14:29:43Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life. The β-glycosidase from ''S. solfataricus'' (SSO1353) is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a ''[[retaining]]'' reaction mechanism. SSO1353 is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase, involved in the catabolism of glucosylceramide, which is then converted to sphingomyelin <cite>PMID17105727</cite>. SSO1353 has substrate specificity and inhibitor sensitivity slightly different from those of GBA2. In fact, the archaeal enzyme can hydrolyze both aryl β-gluco and β-xylosides
and it is inhibited by both N-butyldeoxynojirimycin (NB-DNJ) and conduritol β-epoxide (CBE) <cite>PMID20427274</cite>. Instead, GBA2 is inactive on methylumbellyferyl-β-D-glucopyranoside and is relatively insensitive to CBE <cite>PMID17105727</cite>.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by <sup>1</sup>H-<sup>13</sup>C NMR spectroscopy analysis of the interglycosidic linkage of disaccharides formed by the [index.php?title=Transglycosylation&action=edit&redlink=1 transglycosylation] action of SSO1353 on 4NP-β-Xyl <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2-
deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-01T14:26:41Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life. The β-glycosidase from ''S. solfataricus'' (SSO1353) is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a ''[[retaining]]'' reaction mechanism. SSO1353 is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase, involved in the catabolism of glucosylceramide, which is then converted to sphingomyelin <cite>PMID17105727</cite>. SSO1353 has substrate specificity and inhibitor sensitivity slightly different from those of GBA2. In fact, the archaeal enzyme can hydrolyze both aryl β-gluco and β-xylosides
and it is inhibited by both N-butyldeoxynojirimycin (NB-DNJ) and conduritol β-epoxide (CBE) <cite>PMID20427274</cite>. Instead, GBA2 is inactive on methylumbellyferyl-β-D-glucopyranoside (MU-Xyl) and is relatively insensitive to CBE <cite>PMID17105727</cite>.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2-
deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-01T14:13:25Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life. The β-glycosidase from ''S. solfataricus'' (SSO1353) is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a ''[[retaining]]'' reaction mechanism. SSO1353 is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase, involved in the catabolism of glucosylceramide, which is then converted to sphingomyelin <cite>PMID17105727</cite>. SSO1353 has substrate specificity and inhibitor sensitivity slightly different from those of GBA2. In fact, the archaeal enzyme can hydrolyze both aryl β-gluco and β-xylosides
and it is inhibited by both N-butyldeoxynojirimycin (NB-DNJ) and conduritol β-epoxide (CBE) <cite>PMID20427274</cite>. Instead, GBA2 is inactive on methylumbellyferyl-β-D-glucopyranoside (MU-Xyl) and is relatively insensitive to CBE <cite>PMID17105727</cite>.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2,4-dinitrophenyl-β-D-2-deoxy-
2-fluoro-glucopyranoside [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-01T14:11:47Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life. The β-glycosidase from ''S. solfataricus'' (SSO1353) is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a [[''retaining'']] reaction mechanism. SSO1353 is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase, involved in the catabolism of glucosylceramide, which is then converted to sphingomyelin <cite>PMID17105727</cite>. SSO1353 has substrate specificity and inhibitor sensitivity slightly different from those of GBA2. In fact, the archaeal enzyme can hydrolyze both aryl β-gluco and β-xylosides
and it is inhibited by both N-butyldeoxynojirimycin (NB-DNJ) and conduritol β-epoxide (CBE) <cite>PMID20427274</cite>. Instead, GBA2 is inactive on methylumbellyferyl-β-D-glucopyranoside (MU-Xyl) and it is relatively insensitive to CBE <cite>PMID17105727</cite>.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2,4-dinitrophenyl-β-D-2-deoxy-
2-fluoro-glucopyranoside [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-01T14:10:26Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life. The β-glycosidase from S. solfataricus (SSO1353) is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a retaining reaction mechanism. SSO1353 is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase, involved in the catabolism of glucosylceramide, which is then converted to sphingomyelin <cite>PMID17105727</cite>. SSO1353 has substrate specificity and inhibitor sensitivity slightly different from those of GBA2. In fact, the archaeal enzyme can hydrolyze both aryl β-gluco and β-xylosides
and it is inhibited by both N-butyldeoxynojirimycin (NB-DNJ) and conduritol β-epoxide (CBE) <cite>PMID20427274</cite>. Instead, GBA2 is inactive on methylumbellyferyl-β-D-glucopyranoside (MU-Xyl) and it is relatively insensitive to CBE <cite>PMID17105727</cite>.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2,4-dinitrophenyl-β-D-2-deoxy-
2-fluoro-glucopyranoside [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-01T14:05:07Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life. The β-glycosidase from S. solfataricus (SSO1353) is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a retaining reaction mechanism. SSO1353 is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase, involved in the catabolism of glucosylceramide, which is then converted to sphingomyelin <cite>PMID17105727</cite>. SSO1353 has substrate specificity and inhibitor sensitivity slightly different from those of GBA2. In fact, the archaeal enzyme can hydrolyze both aryl β-gluco and β-xylosides
and it is inhibited by both NB-DNJ and CBE <cite>PMID20427274</cite>. Instead, GBA2 is inactive on MU-Xyl and it is relatively insensitive to CBE <cite>PMID17105727</cite>.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2,4-dinitrophenyl-β-D-2-deoxy-
2-fluoro-glucopyranoside [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-01T13:59:20Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life. The β-glycosidase from S. solfataricus is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a retaining reaction mechanism. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. This enzyme, previously described
as bile acid β-glucosidase [34], is involved in the
catabolism of glucosylceramide, which is then converted to
sphingomyelin [6].

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2,4-dinitrophenyl-β-D-2-deoxy-
2-fluoro-glucopyranoside [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-01T13:56:27Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite> and contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life. The β-glycosidase from S. solfataricus is specific for the gluco- and xylosides β-bound to hydrophobic groups that are hydrolyzed by following a retaining reaction mechanism. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2,4-dinitrophenyl-β-D-2-deoxy-
2-fluoro-glucopyranoside [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-07-01T13:27:32Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 through trapping of the 2,4-dinitrophenyl-β-D-2-deoxy-
2-fluoro-glucopyranoside [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-06-28T13:36:07Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 in the sequence AIY'''<u>E</u>'''APQ through trapping of the 2-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-06-28T13:33:57Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 in the sequence AIY'''<u>E</u>'''APQ through trapping of the 2-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2,4-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-06-18T14:00:43Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 in the sequence AIY'''<u>E</u>'''APQ through trapping of the 2,4-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''S. solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''S. solfataricus'' β-glycosidase by 2,4-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''S. solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-06-18T13:41:36Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 in the sequence AIY'''<u>E</u>'''APQ through trapping of the 2,4-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==

;First stereochemistry determination: ''Sulfolobus solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''Sulfolobus solfataricus'' β-glycosidase by 2,4-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''Sulfolobus solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-06-18T13:40:08Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glycosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glycosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 in the sequence AIY'''<u>E</u>'''APQ through trapping of the 2,4-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==
;First stereochemistry determination: ''Sulfolobus solfataricus'' β-glycosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''Sulfolobus solfataricus'' β-glycosidase by 2,4-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''Sulfolobus solfataricus'' β-glycosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

User:Beatrice Cobucci-Ponzano

2010-06-18T13:38:19Z

Beatrice Cobucci-Ponzano:

[[File:Cobuccifoto.jpg|right]]

Beatrice Cobucci-Ponzano obtained her degree in Biology from the University of Naples “Federico II”, Italy, in 1997, working on the beta-glycosidase ([[GH1]]) from the archaeon ''Sulfolobus solfataricus'', under the supervision of Mosè Rossi at the [http://www.ibp.cnr.it/ Institute of Protein Biochemistry] (IBP) of the italian [http://www.cnr.it/sitocnr/Englishversion/Englishversion.html National Research Council] (CNR).

She obtained her PhD in Biochemistry and Biophysic at the University of Padua, working on the characterization of CAZymes form hyperthermophiles ([[GH1]] and [[GH31]]) under the supervision of Marco Moracci at IBP.

From 2001 she is staff scientist at IBP in the group of ^^^Marco Moracci^^^. The work focuses on the characterization and the understanding of the reaction mechanism of glycoside hydrolases, on their modification for the synthesis of glycosides (glycosynthases), and on glycosyltransferases.

She determined the reaction mechanism and the catalytic residues of alpha-L-fucosidases ([[GH29]]) <cite>PMID12569098 PMID12911294 PMID15835922</cite>, and developed a new method for the modification of this class of enzymes in efficient alpha-L-fucosynthases <cite>PMID19875083</cite>. This method could be of general applicability to all alpha-glycosidases.

Recently, she characterized a novel archaeal beta-glycosidase that allowed the creation of the CAZy family [[GH116]] <cite>PMID20427274</cite>.

'''Reference list'''

<biblio>
#PMID12569098 pmid=12569098
#PMID12911294 pmid=12911294
#PMID15835922 pmid=15835922
#PMID19875083 pmid=19875083
#PMID20427274 pmid=20427274
</biblio>

Glycoside Hydrolase Family 116

2010-06-18T13:35:02Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glucosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glucosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 in the sequence AIY'''<u>E</u>'''APQ through trapping of the 2,4-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==
;First stereochemistry determination: ''Sulfolobus solfataricus'' β-glucosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''Sulfolobus solfataricus'' β-glucosidase by 2,4-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''Sulfolobus solfataricus'' β-glucosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-06-18T13:34:13Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glucosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glucosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 in the sequence AIY'''<u>E</u>'''AP through trapping of the 2,4-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==
;First stereochemistry determination: ''Sulfolobus solfataricus'' β-glucosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''Sulfolobus solfataricus'' β-glucosidase by 2,4-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''Sulfolobus solfataricus'' β-glucosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

File:Cobuccifoto.jpg

2010-06-18T13:17:22Z

Beatrice Cobucci-Ponzano: uploaded a new version of "File:Cobuccifoto.jpg": Reverted to version as of 12:51, 18 June 2010

File:Cobuccifoto.jpg

2010-06-18T12:57:35Z

Beatrice Cobucci-Ponzano: uploaded a new version of "File:Cobuccifoto.jpg": Reverted to version as of 12:51, 18 June 2010

File:Cobuccifoto.jpg

2010-06-18T12:57:04Z

Beatrice Cobucci-Ponzano: uploaded a new version of "File:Cobuccifoto.jpg": Reverted to version as of 14:38, 14 June 2010

File:Cobuccifoto.jpg

2010-06-18T12:52:10Z

Beatrice Cobucci-Ponzano: uploaded a new version of "File:Cobuccifoto.jpg": Reverted to version as of 14:38, 14 June 2010

File:Cobuccifoto.jpg

2010-06-18T12:51:35Z

Beatrice Cobucci-Ponzano: uploaded a new version of "File:Cobuccifoto.jpg": Reverted to version as of 12:47, 18 June 2010

File:Cobuccifoto.jpg

2010-06-18T12:51:14Z

Beatrice Cobucci-Ponzano: uploaded a new version of "File:Cobuccifoto.jpg": Reverted to version as of 12:43, 18 June 2010

File:Cobuccifoto.jpg

2010-06-18T12:47:50Z

Beatrice Cobucci-Ponzano: uploaded a new version of "File:Cobuccifoto.jpg"

File:Cobuccifoto.jpg

2010-06-18T12:43:23Z

Beatrice Cobucci-Ponzano: uploaded a new version of "File:Cobuccifoto.jpg"

Glycoside Hydrolase Family 116

2010-06-18T12:37:18Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glucosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases, and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glucosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 in the sequence AIY'''<u>E</u>'''AP through trapping of the 2,4-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis of a mutant at that position, which included azide rescue experiments.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==
;First stereochemistry determination: ''Sulfolobus solfataricus'' β-glucosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''Sulfolobus solfataricus'' β-glucosidase by 2,4-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''Sulfolobus solfataricus'' β-glucosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-06-18T12:34:00Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glucosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases, and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glucosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 in the sequence AIY'''<u>E</u>'''AP through trapping of the 2,4-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis, which included azide rescue experiments, of a mutant at that position.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==
;First stereochemistry determination: ''Sulfolobus solfataricus'' β-glucosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''Sulfolobus solfataricus'' β-glucosidase by 2,4-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''Sulfolobus solfataricus'' β-glucosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-06-18T12:31:00Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glucosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) activities from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases, and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glucosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 in the sequence AIY'''E'''AP through trapping of the 2,4-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis, which included azide rescue experiments, of a mutant at that position.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==
;First stereochemistry determination: ''Sulfolobus solfataricus'' β-glucosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''Sulfolobus solfataricus'' β-glucosidase by 2,4-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: ''Sulfolobus solfataricus'' β-glucosidase by azide rescue with mutant <cite>PMID20427274</cite>.
;First 3-D structure:

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-06-18T12:26:56Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
| none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glucosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases, and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glucosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 in the sequence AIY'''E'''AP through trapping of the 2,4-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis, which included azide rescue experiments, of a mutant at that position.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==
;First stereochemistry determination: ''Sulfolobus solfataricus'' β-glucosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''Sulfolobus solfataricus'' β-glucosidase by 2,4-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-06-18T12:24:53Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glucosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases, and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glucosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 in the sequence AIY'''E'''AP through trapping of the 2,4-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis, which included azide rescue experiments, of a mutant at that position.

== Three-dimensional structures ==

Unkwown

== Family Firsts ==
;First stereochemistry determination: ''Sulfolobus solfataricus'' β-glucosidase by NMR <cite>PMID20427274</cite>.
;First catalytic nucleophile identification: ''Sulfolobus solfataricus'' β-glucosidase by 2,4-deoxy-2-fluoroglucose labeling <cite>PMID20427274</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-06-18T12:18:01Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glucosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases, and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glucosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 in the sequence AIY'''E'''AP through trapping of the 2,4-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis, which included azide rescue experiments, of a mutant at that position.

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

== Family Firsts ==
;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-06-18T12:17:05Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glucosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases, and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The catalytic residues were identified in the ''S. solfataricus'' β-glucosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 in the sequence AIY'''E'''AP through trapping of the 2,4-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis, which included azide rescue experiments, of a mutant at that position.

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

== Family Firsts ==
;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-06-18T12:16:41Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glucosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases, and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

The [[catalytic residues]] were identified in the ''S. solfataricus'' β-glucosidase <cite>PMID20427274</cite>. The [[catalytic nucleophile]] was identified as Glu335 in the sequence AIY'''E'''AP through trapping of the 2,4-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and MS/MS analysis. The [[general acid/base]] catalyst role was assigned to Asp462 through mechanistic analysis, which included azide rescue experiments, of a mutant at that position.

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

== Family Firsts ==
;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-06-18T12:14:49Z

Beatrice Cobucci-Ponzano:

{{UnderConstruction}}
* [[Author]]: ^^^Beatrice Cobucci-Ponzano^^^
* [[Responsible Curator]]: ^^^Marco Moracci^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH116'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH116.html
|}
</div>


== Substrate specificities ==

This family of [[glycoside hydrolases]] was recently discovered characterising a new β-glucosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) from the three domains of life.

== Kinetics and Mechanism ==

The enzymes of this family are ''[[retaining]]'' glycoside hydrolases, and follow the classical [[Koshland double-displacement mechanism]] <cite>Koshland</cite>. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-β-Xyl as the substrate and ''S. solfataricus ''SSO1353 as the enzyme <cite>PMID20427274</cite>.

== Catalytic Residues ==

0 false 14 18 pt 18 pt 0 0 false false false The catalytic residues were identified in the ''S. solfataricus'' β-glucosidase <cite>PMID20427274</cite>. The catalytic nucleophile was identified as Glu335 in the sequence AIY'''E'''AP through trapping of the 2,4-deoxy-2-fluoroglucosyl-enzyme intermediate and MS/MS analysis. The general acid/base catalyst role was assigned to Asp462 through mechanistic analysis, which included azide rescue experiments, of a mutant at that position.

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

== Family Firsts ==
;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.

== References ==
<biblio>
#PMID20427274 pmid=20427274
#PMID17105727 pmid=17105727
#Koshland Koshland DE Jr: Stereochemistry and the mechanism of enzyme reactions. Biol Rev 1953, 28:416-436.
</biblio>

[[Category:Glycoside Hydrolase Families|GH116]]

Glycoside Hydrolase Family 116

2010-06-18T10:50:35Z

Beatrice Cobucci-Ponzano:

Glycoside Hydrolase Family 116

2010-06-18T10:44:19Z

Beatrice Cobucci-Ponzano:

Glycoside Hydrolase Family 116

2010-06-18T10:43:35Z

Beatrice Cobucci-Ponzano:

Glycoside Hydrolase Family 116

2010-06-18T10:39:34Z

Beatrice Cobucci-Ponzano:

Glycoside Hydrolase Family 116

2010-06-18T10:38:06Z

Beatrice Cobucci-Ponzano:

Glycoside Hydrolase Family 116

2010-06-18T10:35:48Z

Beatrice Cobucci-Ponzano:

Glycoside Hydrolase Family 116

2010-06-18T10:14:19Z

Beatrice Cobucci-Ponzano: