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Difference between revisions of "Glycoside Hydrolase Family 38"
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== Substrate specificities == | == 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). | |
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== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
Revision as of 08:34, 20 August 2009
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...)
Make sure to delete this text and the four dashes (line) below when you are done with your page!
| 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]]