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Glycoside Hydrolase Family 38

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The text below is a template to help you create a consistent layout for GH entries. To get an idea of what to put in each field, save this edit and have a look at any of the GH families by following this link: Category:Glycoside Hydrolase Families (TIP: Right click with your mouse and open the link in a new browser window...)

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Glycoside Hydrolase Family GH38
Clan GH-x
Mechanism retaining
Active site residues known
CAZy DB link
http://www.cazy.org/fam/GH38.html

Substrate specificities

GH38 enzymes are Class II α-mannosidases. They range in breadth of specificity from the Golgi α-mannosidase (2A1), which has a dual specificity for α1,6 and α1,3-linked mannoses, to the lysosomal mannosidases, which have either broad (2B1 cleaves α1,2, α1,3 and α1,6 linkages) or narrow specificities (2B2 is specific for α1,6).

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]]