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Difference between revisions of "Glycoside Hydrolase Family 101"
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Harry Brumer (talk | contribs) |
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== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | + | Retaining mechanism determined by NMR with the BlGH101 enzyme. | |
== Catalytic Residues == | == Catalytic Residues == | ||
Revision as of 18:27, 25 June 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 NMR with the BlGH101 enzyme.
Catalytic Residues
Nucleophile SpGH101 D764 Acid/base catalyst SpGH101 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
- 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 |