Glycoside Hydrolase Family 15 - Revision history

Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

2021-12-18T21:15:45Z

Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

Harry Brumer: updated CAZy DB link

2011-05-09T12:42:36Z

updated CAZy DB link

Spencer Williams at 11:49, 14 June 2010

2010-06-14T11:49:03Z

Harry Brumer: /* Substrate specificities */ added EC links out

2010-01-15T08:44:02Z

Substrate specificities: added EC links out

Pedro Coutinho: /* Family Firsts */

2009-11-16T18:42:30Z

Family Firsts

Harry Brumer at 13:55, 8 November 2009

2009-11-08T13:55:24Z

Spencer Williams at 05:30, 7 November 2009

2009-11-07T05:30:39Z

Harry Brumer: /* Kinetics and Mechanism */

2009-11-06T12:15:42Z

Kinetics and Mechanism

Harry Brumer: /* Three-dimensional structures */

2009-11-06T12:15:19Z

Three-dimensional structures

Harry Brumer: /* References */

2009-11-06T08:37:10Z

References

@@ Line 1: / Line 1: @@
 {{CuratorApproved}}
-* [[Author]]: ^^^Pedro Coutinho^^^
+* [[Author]]: [[User:Pedro Coutinho|Pedro Coutinho]]
-* [[Responsible Curator]]:  ^^^Pedro Coutinho^^^
+* [[Responsible Curator]]:  [[User:Pedro Coutinho|Pedro Coutinho]]
 ----

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 |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 |-
-| colspan="2" |http://www.cazy.org/fam/GH15.html
+| colspan="2" |{{CAZyDBlink}}GH15.html
 |}
 </div>

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 == Substrate specificities ==
-[[Glycoside hydrolase]]s of this family hydrolyze the non-reducing end residues of α-glucosides. At present, the most commonly characterized activity is glucoamylase (EC [{{EClink}}3.2.1.3 3.2.1.3]), also know as amyloglucosidase, but glucodextranase (EC [{{EClink}}3.2.1.70 3.2.1.70]) and α,α-trehalase (EC [{{EClink}}3.2.1.28 3.2.1.28]) activities have been described. It has been found that fungal glucoamylases present some substrate flexibility and are able to degrade not only α-1,4-glycosidic bonds but also α-1,6-, α-1,3- and α-1,2-bonds to a lower degree <cite>Meagher1989</cite>.
+[[Glycoside hydrolase]]s of this family are [[exo]]-acting enzymes that hydrolyze the non-reducing end residues of α-glucosides. At present, the most commonly characterized activity is glucoamylase (EC [{{EClink}}3.2.1.3 3.2.1.3]), also know as amyloglucosidase, but glucodextranase (EC [{{EClink}}3.2.1.70 3.2.1.70]) and α,α-trehalase (EC [{{EClink}}3.2.1.28 3.2.1.28]) activities have been described. It has been found that fungal glucoamylases present some substrate flexibility and are able to degrade not only α-1,4-glycosidic bonds but also α-1,6-, α-1,3- and α-1,2-bonds to a lower degree <cite>Meagher1989</cite>.
 == Kinetics and Mechanism ==
@@ Line 43: / Line 43: @@
 == Family Firsts ==
 ;First sterochemistry determination:
-Inverting mechanism in ''Aspergillus niger'' glucoamylase deduced by optical rotation described by Weil ''et al.'', 1954 <cite>Weil1954</cite>.
+[[Inverting]] mechanism in ''Aspergillus niger'' glucoamylase deduced by optical rotation described by Weil ''et al.'', 1954 <cite>Weil1954</cite>.
 ;First sequence identification:

@@ Line 27: / Line 27: @@
 == Substrate specificities ==
-[[Glycoside hydrolase]]s of this family hydrolyze the non-reducing end residues of α-glucosides. At present, the most commonly characterized activity is glucoamylase (EC 3.2.1.3), also know as amyloglucosidase, but glucodextranase (EC 3.2.1.70) and α,α-trehalase (EC 3.2.1.28) activities have been described. It has been found that fungal glucoamylases present some substrate flexibility and are able to degrade not only α-1,4-glycosidic bonds but also α-1,6-, α-1,3- and α-1,2-bonds to a lower degree <cite>Meagher1989</cite>.
+[[Glycoside hydrolase]]s of this family hydrolyze the non-reducing end residues of α-glucosides. At present, the most commonly characterized activity is glucoamylase (EC [{{EClink}}3.2.1.3 3.2.1.3]), also know as amyloglucosidase, but glucodextranase (EC [{{EClink}}3.2.1.70 3.2.1.70]) and α,α-trehalase (EC [{{EClink}}3.2.1.28 3.2.1.28]) activities have been described. It has been found that fungal glucoamylases present some substrate flexibility and are able to degrade not only α-1,4-glycosidic bonds but also α-1,6-, α-1,3- and α-1,2-bonds to a lower degree <cite>Meagher1989</cite>.
 == Kinetics and Mechanism ==

@@ Line 43: / Line 43: @@
 == Family Firsts ==
 ;First sterochemistry determination:
-Inverting mechanism in glucoamylase described by Weil ''et al.'', 1954 <cite>Weil1954</cite>.
+Inverting mechanism in ''Aspergillus niger'' glucoamylase deduced by optical rotation described by Weil ''et al.'', 1954 <cite>Weil1954</cite>.
 ;First sequence identification:

← Older revision		Revision as of 13:55, 8 November 2009
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		+	{{CuratorApproved}}
	* [[Author]]: ^^^Pedro Coutinho^^^		* [[Author]]: ^^^Pedro Coutinho^^^
	* [[Responsible Curator]]: ^^^Pedro Coutinho^^^		* [[Responsible Curator]]: ^^^Pedro Coutinho^^^

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 == Substrate specificities ==
-Enzymes from this family hydrolyze the non-reducing end residues of α-glucosides by an inverting mechanism. At present, the most commonly characterized activity is glucoamylase (EC 3.2.1.3), also know as amyloglucosidase, but glucodextranase (EC 3.2.1.70) and α,α-trehalase (EC 3.2.1.28) activities have been described. It has been found that fungal glucoamylases present some substrate flexibility and are able to degrade not only α-1,4-glycosidic bonds but also α-1,6-, α-1,3- and α-1,2-bonds to a lower degree <cite>Meagher1989</cite>.
+[[Glycoside hydrolase]]s of this family hydrolyze the non-reducing end residues of α-glucosides. At present, the most commonly characterized activity is glucoamylase (EC 3.2.1.3), also know as amyloglucosidase, but glucodextranase (EC 3.2.1.70) and α,α-trehalase (EC 3.2.1.28) activities have been described. It has been found that fungal glucoamylases present some substrate flexibility and are able to degrade not only α-1,4-glycosidic bonds but also α-1,6-, α-1,3- and α-1,2-bonds to a lower degree <cite>Meagher1989</cite>.
 == Kinetics and Mechanism ==
-Family GH15 α-glycosidases are inverting enzymes, as first shown by Weil et al., 1954 <cite>Weil1954</cite> and follow a classical Koshland single-displacement mechanism. Enzymes that have been well studied kinetically include ''Aspergillus'' and ''Rhizopus'' glucoamylases.
+Family GH15 α-glycosidases are [[inverting]] enzymes, as first shown by Weil et al., 1954 <cite>Weil1954</cite> and follow a classical Koshland single-step displacement mechanism. Enzymes that have been well studied kinetically include the ''Aspergillus'' and ''Rhizopus'' glucoamylases.
 == Catalytic Residues ==
-The general acid was first identified in the ''Aspergillus awamori'' / ''Aspergillus niger ''glucoamylase as Glu179 following site-directed mutagenesis <cite>Sierks1990</cite>. The general base was defined as Glu400 following the three-dimensional structure determination <cite>Harris1993</cite> and confirmed later on by site directed mutagenesis and kinetic studies <cite>Frandsen1994</cite>. Simultaneously the general base was identified in ''Clostridium'' sp. G0005 glucoamylase by chemical modification and mutagenesis <cite>Ohnishi1994</cite>.
+The [[general acid]] was first identified in the ''Aspergillus awamori'' / ''Aspergillus niger ''glucoamylase as Glu179 following site-directed mutagenesis <cite>Sierks1990</cite>. The [[general base]] was defined as Glu400 following the three-dimensional structure determination <cite>Harris1993</cite> and confirmed later on by site directed mutagenesis and kinetic studies <cite>Frandsen1994</cite>. Simultaneously the [[general base]] was identified in ''Clostridium'' sp. G0005 glucoamylase by chemical modification and mutagenesis <cite>Ohnishi1994</cite>.
 == Three-dimensional structures ==
-Three-dimensional structures are available for a number of family GH15 enzymes, the first solved being that of ''Aspergillus  awamori'' var. X100 glucoamylase <cite>Aleshin1992</cite>. All members of this family have (α/α)<sub>6</sub> barrel fold with the two key catalytic glutamic acid residues being approximately 200 residues apart in sequence and located at the loops following barrel α-helices 5 (general acid) and 11 (general base).  Bacterial GH15 enzymes have in general an all β-strand super-β-sandwich preceding the catalytic (α/α)<sub>6</sub> barrel <cite>Aleshin2003</cite>.
+Three-dimensional structures are available for several GH15 family enzymes, the first solved being that of ''Aspergillus  awamori'' var. X100 glucoamylase <cite>Aleshin1992</cite>. All members of this family have (α/α)<sub>6</sub> barrel fold with the two key catalytic glutamic acid residues being approximately 200 residues apart in sequence and located at the loops following barrel α-helices 5 (general acid) and 11 (general base).  Bacterial GH15 enzymes have in general an all β-strand super-β-sandwich preceding the catalytic (α/α)<sub>6</sub> barrel <cite>Aleshin2003</cite>.
 == Family Firsts ==

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 #Frandsen1994 pmid=7947792
 #Aleshin2003 pmid=12614608
-#Svensson1983   Svensson S, Larsen K, Svendsen I, Boel E. The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsberg Res Commun 1983; 48(6) 529-44  DOI: 10.1007/BF02907555
+#Svensson1983   Svensson S, Larsen K, Svendsen I, Boel E. The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsberg Res Commun 1983; 48(6) 529-44  [http://dx.doi.org/10.1007/BF02907555 DOI: 10.1007/BF02907555]
 </biblio>
 [[Category:Glycoside Hydrolase Families|GH015]]