Glycoside Hydrolase Family 32 - Revision history

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

2021-12-18T21:18:00Z

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

Harry Brumer: added EC links

2013-07-30T16:28:45Z

added EC links

Spencer Williams: /* Kinetics and Mechanism */

2013-06-27T05:47:06Z

Kinetics and Mechanism

Spencer Williams: /* Kinetics and Mechanism */

2013-06-27T05:46:51Z

Kinetics and Mechanism

Spencer Williams: /* Kinetics and Mechanism */

2013-06-27T05:46:05Z

Kinetics and Mechanism

Spencer Williams: /* Kinetics and Mechanism */

2013-06-27T05:45:50Z

Kinetics and Mechanism

Harry Brumer: updated CAZyDBlink

2012-09-10T16:35:26Z

updated CAZyDBlink

Spencer Williams: /* Family Firsts */

2010-06-22T10:55:01Z

Family Firsts

Mirjam Czjzek at 15:32, 22 February 2010

2010-02-22T15:32:32Z

Mirjam Czjzek: /* Catalytic Residues */

2010-02-22T15:28:26Z

Catalytic Residues

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 {{CuratorApproved}}
-* [[Author]]s: ^^^Mirjam Czjzek^^^ and ^^^Wim Van den Ende^^^
+* [[Author]]s: [[User:Mirjam Czjzek|Mirjam Czjzek]] and [[User:Wim Van den Ende|Wim Van den Ende]]
-* [[Responsible Curator]]:  ^^^Mirjam Czjzek^^^
+* [[Responsible Curator]]:  [[User:Mirjam Czjzek|Mirjam Czjzek]]
 ----

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 == Substrate specificities ==
-[[Glycoside hydrolase]] family GH32 contains one of the earliest described enzyme activities, namely that of 'inverting' sucrose, from which is derived the name of 'invertase' (EC 3.2.1.26), discovered in the second half of the 19th century <cite>1</cite>. Besides the 'historical' invertases, this family also contains enzymes that hydrolyze fructose containing polysaccharides such as inulinases (EC 3.2.1.7) and exo-inulinases (EC 3.2.1.80), levanases (EC 3.2.1.65) and &beta;-2,6-fructan 6-levanbiohydrolases(EC 3.2.1.64), fructan &beta;-(2,1)-fructosidase/1-exohydrolase (EC 3.2.1.153) or fructan &beta;-(2,6)-fructosidase/6-exohydrolases (EC 3.2.1.154), as well as enzymes displaying transglycosylating activities such as sucrose:sucrose 1-fructosyltransferases (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-).
+[[Glycoside hydrolase]] family GH32 contains one of the earliest described enzyme activities, namely that of 'inverting' sucrose, from which is derived the name of 'invertase' (EC [{{EClink}}3.2.1.26 3.2.1.26]), discovered in the second half of the 19th century <cite>1</cite>. Besides the 'historical' invertases, this family also contains enzymes that hydrolyze fructose containing polysaccharides such as inulinases (EC [{{EClink}}3.2.1.7 3.2.1.7]) and exo-inulinases (EC [{{EClink}}3.2.1.80 3.2.1.80]), levanases (EC [{{EClink}}3.2.1.65 3.2.1.65]) and &beta;-2,6-fructan 6-levanbiohydrolases(EC [{{EClink}}3.2.1.64 3.2.1.64]), fructan &beta;-(2,1)-fructosidase/1-exohydrolase (EC [{{EClink}}3.2.1.153 3.2.1.153]) or fructan &beta;-(2,6)-fructosidase/6-exohydrolases (EC [{{EClink}}3.2.1.154 3.2.1.154]), as well as enzymes displaying transglycosylating activities such as sucrose:sucrose 1-fructosyltransferases (EC [{{EClink}}2.4.1.99 2.4.1.99]), fructan:fructan 1-fructosyltransferase (EC [{{EClink}}2.4.1.100 2.4.1.100]), sucrose:fructan 6-fructosyltransferase (EC [{{EClink}}2.4.1.10 2.4.1.10]), fructan:fructan 6G-fructosyltransferase (EC [{{EClink}}2.4.1.243 2.4.1.243]) and levan fructosyltransferases (EC 2.4.1.-).
 == Kinetics and Mechanism ==

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 == Kinetics and Mechanism ==
-Family GH32 enzymes are [[retaining]] enzymes, as first shown by Koshland and Stein by performing the reaction in <sup>18</sup>O-labeled water and determining the <sup>18</sup>O content of the products <cite>2</cite>. The transfructosylation activity (a type of [[transglycosylase|transglycosylases]] activity) observed for invertase in this reaction indicated that the enzyme operates with a molecular mechanism leading to overall retention of the anomeric configuration <cite>2</cite>.
+Family GH32 enzymes are [[retaining]] enzymes, as first shown by Koshland and Stein by performing the reaction in <sup>18</sup>O-labeled water and determining the <sup>18</sup>O content of the products <cite>2</cite>. The transfructosylation activity (a type of [[transglycosylases|transglycosylase]] activity) observed for invertase in this reaction indicated that the enzyme operates with a molecular mechanism leading to overall retention of the anomeric configuration <cite>2</cite>.
 == Catalytic Residues ==

@@ Line 28: / Line 28: @@
 == Kinetics and Mechanism ==
-Family GH32 enzymes are [[retaining]] enzymes, as first shown by Koshland and Stein by performing the reaction in <sup>18</sup>O-labeled water and determining the <sup>18</sup>O content of the products <cite>2</cite>. The transfructosylation activity (a type of [[transglycosidase]] activity) observed for invertase in this reaction indicated that the enzyme operates with a molecular mechanism leading to overall retention of the anomeric configuration <cite>2</cite>.
+Family GH32 enzymes are [[retaining]] enzymes, as first shown by Koshland and Stein by performing the reaction in <sup>18</sup>O-labeled water and determining the <sup>18</sup>O content of the products <cite>2</cite>. The transfructosylation activity (a type of [[transglycosylase|transglycosylases]] activity) observed for invertase in this reaction indicated that the enzyme operates with a molecular mechanism leading to overall retention of the anomeric configuration <cite>2</cite>.
 == Catalytic Residues ==

@@ Line 28: / Line 28: @@
 == Kinetics and Mechanism ==
-Family GH32 enzymes are [[retaining]] enzymes, as first shown by Koshland and Stein by performing the reaction in <sup>18</sup>O-labeled water and determining the <sup>18</sup>O content of the products <cite>2</cite>. The transfructosylation activity (a type of [[transglycosylase]] activity) observed for invertase in this reaction indicated that the enzyme operates with a molecular mechanism leading to overall retention of the anomeric configuration <cite>2</cite>.
+Family GH32 enzymes are [[retaining]] enzymes, as first shown by Koshland and Stein by performing the reaction in <sup>18</sup>O-labeled water and determining the <sup>18</sup>O content of the products <cite>2</cite>. The transfructosylation activity (a type of [[transglycosidase]] activity) observed for invertase in this reaction indicated that the enzyme operates with a molecular mechanism leading to overall retention of the anomeric configuration <cite>2</cite>.
 == Catalytic Residues ==

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 |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 |-
-| colspan="2" |http://www.cazy.org/fam/GH32.html
+| colspan="2" |{{CAZyDBlink}}GH32.html
 |}
 </div>

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 ;First [[catalytic nucleophile]] identification: ''Saccharomyces cerevisiae'' invertase <cite>3</cite>
 ;First [[general acid/base]] residue identification: ''Saccharomyces cerevisiae'' invertase <cite>4</cite>
-;First 3-D structure: bacterial &beta;-fructosidase from ''Thermotoga maritima'' by X-ray crystallography  (PDB ID [{{PDBlink}}1uyp 1uyp])  <cite>6</cite>
+;First 3-D structure: Bacterial &beta;-fructosidase from ''Thermotoga maritima'' by X-ray crystallography  (PDB ID [{{PDBlink}}1uyp 1uyp])  <cite>6</cite>
 == References ==

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 == Catalytic Residues ==
-The two residues, responsible for the catalytic reaction in family GH32 enzymes, have first been identified in yeast invertase as an aspartate located close to the N-terminus acting as the [[catalytic nucleophile]] <cite>3</cite> and a glutamate acting as the [[general acid/base]] <cite>4</cite>. An interesting feature concerns some members of GH32, such as the endo-inulinase from Aspergillus, that use a glutamate replacing the aspartate as catalytic nucleophile <cite>5</cite>.
+The two residues, responsible for the catalytic reaction in family GH32 enzymes, have first been identified in yeast invertase as an aspartate located close to the N-terminus acting as the [[catalytic nucleophile]] <cite>3</cite> and a glutamate acting as the [[general acid/base]] <cite>4</cite>. An interesting feature concerns some members of GH32, such as the endo-inulinase from ''Aspergillus  ficuum'', that use a glutamate replacing the aspartate as catalytic nucleophile <cite>5</cite>.
 == Three-dimensional structures ==