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Difference between revisions of "Glycoside Hydrolase Family 101"
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| Line 29: | Line 29: | ||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | Retaining mechanism determined by NMR with the BlGH101 enzyme. | + | Retaining mechanism determined by H<sup>1</sup>-NMR with the BlGH101 enzyme. PMID: 16141207 |
== Catalytic Residues == | == 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. | ||
Revision as of 09:34, 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
Gal-beta-1,3-GalNAc-alpha-R O-linked glycans on proteins
Kinetics and Mechanism
Retaining mechanism determined by H1-NMR with the BlGH101 enzyme. PMID: 16141207
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