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Difference between revisions of "Carbohydrate-active enzymes"

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* [[Author]]: [[User:StephenWithers|Stephen Withers]]
 
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* [[Responsible Curator]]:  [[User:SpencerWilliams|Spencer Williams]]
* [[Author]]: [[User:StephenWithers|Harry Brumer]]
 
* [[Responsible Curator]]:  [[User:SpencerWilliams|Harry Brumer]]
 
 
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Enzymatic formation and cleavage of the bond between two sugars or between a sugar and another group can occur by hydrolysis to give the free sugar (''glycosidases'' or ''glycoside hydrolases''), by transglycosylation to give a new glycoside (''transglycosidases''), by phosphorolysis to give the sugar-1-phosphate (''phosphorylases'') or by elimination to give unsaturated sugar products (''lyases''). The principal enzymes that catalyze glycoside synthesis are nucleotide phosphosugar-dependent ''glycosyltransferases''.
 
 
Enzymatic formation and cleavage of the bond between two sugars or between a sugar and another group can occur by hydrolysis to give the free sugar (glycosidases or glycoside hydrolases), by transglycosylation to give a new glycoside (transglycosidases), by phosphorolysis to give the sugar-1-phosphate (phosphorylases) or by elimination to give unsaturated sugar products (lyases). The principal enzymes that catalyze glycoside synthesis are nucleotide phosphosugar-dependent glycosyltransferases.
 
 
== Substrate specificities ==
 
== Substrate specificities ==
  

Revision as of 02:23, 9 July 2009


Glycoside Hydrolase Family GHnn
Clan GH-x
Mechanism retaining/inverting
Active site residues known/not known
CAZy DB link
http://www.cazy.org/fam/GHnn.html

Enzymatic formation and cleavage of the bond between two sugars or between a sugar and another group can occur by hydrolysis to give the free sugar (glycosidases or glycoside hydrolases), by transglycosylation to give a new glycoside (transglycosidases), by phosphorolysis to give the sugar-1-phosphate (phosphorylases) or by elimination to give unsaturated sugar products (lyases). The principal enzymes that catalyze glycoside synthesis are nucleotide phosphosugar-dependent glycosyltransferases.

Substrate specificities

Kinetics and Mechanism

Catalytic Residues

Three-dimensional structures

Family Firsts

First sterochemistry determination
Cite some reference here, with a short explanation [1].
First catalytic nucleophile identification
First general acid/base residue identification
First 3-D structure

References

  1. Comfort DA, Bobrov KS, Ivanen DR, Shabalin KA, Harris JM, Kulminskaya AA, Brumer H, and Kelly RM. (2007). Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases. Biochemistry. 2007;46(11):3319-30. DOI:10.1021/bi061521n | PubMed ID:17323919 [1]

[[Category:Glycoside Hydrolase Families]]