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Glycoside Hydrolase Family 38
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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
- 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 |
[[Category:Glycoside Hydrolase Families]]