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Difference between revisions of "Glycoside Hydrolase Family 101"
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== Substrate specificities == | == Substrate specificities == | ||
| − | + | The CAZY GH101 family currently contains proteins from 12 species of bacteria, most of which are commensal human bacteria, though some may also be human pathogens. The substrates are glycoproteins which contain the dissacharride Gal-beta-1,3-GalNAc-alpha-R ''O''-linked glycans on proteins. This glycosylation is a feature of mucin containing proteins. | |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| Line 49: | Line 49: | ||
== References == | == References == | ||
<biblio> | <biblio> | ||
| − | + | PMID: 16141207 | |
</biblio> | </biblio> | ||
Revision as of 10:42, 10 July 2009
| Glycoside Hydrolase Family GH101 | |
| Clan | GH-x |
| Mechanism | retaining |
| Active site residues | known |
| CAZy DB link | |
| http://www.cazy.org/fam/GH101.html | |
Substrate specificities
The CAZY GH101 family currently contains proteins from 12 species of bacteria, most of which are commensal human bacteria, though some may also be human pathogens. The substrates are glycoproteins which contain the dissacharride Gal-beta-1,3-GalNAc-alpha-R O-linked glycans on proteins. This glycosylation is a feature of mucin containing proteins.
Kinetics and Mechanism
Retaining mechanism determined by H1-NMR with the BlGH101 enzyme.
Catalytic Residues
Using the enzyme from Streptococcus pnuemoniae the nucleophile was determined as residue D764. Willis et al in preparation The acid/base catalyst in SpGH101 was determined to be E796.
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
-
: 16141207