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Difference between revisions of "Glycoside Hydrolase Family 130"

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[[GH130]]  contains phosphorylases catalyzing the phosphorolysis of β1-4mannosidic linkage at the non-reducing end of substrates. 4-O-β-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), β-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-β-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family.
 
[[GH130]]  contains phosphorylases catalyzing the phosphorolysis of β1-4mannosidic linkage at the non-reducing end of substrates. 4-O-β-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), β-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-β-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family.
 
== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
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GH130 phosphorylases phosphorolyze β1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. 
  
 
== Catalytic Residues ==
 
== Catalytic Residues ==

Revision as of 16:29, 16 November 2014

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Glycoside Hydrolase Family GH130
Clan GH-x
Mechanism retaining/inverting
Active site residues known/not known
CAZy DB link
https://www.cazy.org/GH130.html


Substrate specificities

GH130 contains phosphorylases catalyzing the phosphorolysis of β1-4mannosidic linkage at the non-reducing end of substrates. 4-O-β-D-Mannosyl-D-glucose phosphorylase (EC 2.4.1.281), β-1,4-mannooligosaccharide phosphorylase(EC 2.4.1.319), and 1,4-β-mannosyl-N-acetylglucosamine phosphorylase (EC 2.4.1.320) are members of this family.

Kinetics and Mechanism

GH130 phosphorylases phosphorolyze β1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al.

Catalytic Residues

Content is to be added here.

Three-dimensional structures

Content is to be added here.

Family Firsts

First stereochemistry determination
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First catalytic nucleophile identification
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First general acid/base residue identification
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First 3-D structure
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References

  1. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 | PubMed ID:18838391 [Cantarel2009]
  2. Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). DOI: 10.1042/BJ20080382

    [DaviesSinnott2008]