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Difference between revisions of "Glycoside Hydrolase Family 121"
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== Substrate specificities == | == Substrate specificities == | ||
| − | + | This family of glycoside hydrolases was recently established for HypBA2 from ''Bifidobacterium longum'' JCM 1217 | |
| − | |||
| − | This family of glycoside hydrolases was recently established for HypBA2 from | ||
| − | |||
| − | ''Bifidobacterium longum'' JCM 1217 | ||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
Revision as of 18:00, 26 April 2012
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
- Author: ^^^Kiyotaka Fujita^^^
- Responsible Curator: ^^^Shinya Fushinobu^^^
| Glycoside Hydrolase Family GH121 | |
| Clan | GH-x |
| Mechanism | retaining |
| Active site residues | known/not known |
| CAZy DB link | |
| https://www.cazy.org/GH121.html | |
Substrate specificities
This family of glycoside hydrolases was recently established for HypBA2 from Bifidobacterium longum JCM 1217
Kinetics and Mechanism
HypBA2 is a retaining enzyme.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First stereochemistry determination
- This was determined with HypBA2 enzyme using the 1H-NMR and 13C-NMR spectra of the transglycosylation product beta-Ara2-OMe.
References
- Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |
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Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). DOI: 10.1042/BJ20080382