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Difference between revisions of "Glycoside Hydrolase Family 82"
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== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | + | Family 82 enzymes are inverting enzymes, as first shown by NMR [1] on the iota-carrageenase from Alteromonas fortis. | |
| − | |||
== Catalytic Residues == | == Catalytic Residues == | ||
Revision as of 07:40, 24 July 2009
| Glycoside Hydrolase Family GH82 | |
| Clan | none |
| Mechanism | inverting |
| Active site residues | not known |
| CAZy DB link | |
| http://www.cazy.org/fam/GH82.html | |
Substrate specificities
The two known members of family 82 enzymes cleave the β-1,4 galactosidic bond of the marine algal polysaccharide iota-carrageenan [1] yielding products of the neocarrabiose series.
Kinetics and Mechanism
Family 82 enzymes are inverting enzymes, as first shown by NMR [1] on the iota-carrageenase from Alteromonas fortis.
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
The first 3D structure was determined by Michel et al[2].
References
- Barbeyron T, Michel G, Potin P, Henrissat B, and Kloareg B. (2000). iota-Carrageenases constitute a novel family of glycoside hydrolases, unrelated to that of kappa-carrageenases. J Biol Chem. 2000;275(45):35499-505. DOI:10.1074/jbc.M003404200 |
- Michel G, Chantalat L, Fanchon E, Henrissat B, Kloareg B, and Dideberg O. (2001). The iota-carrageenase of Alteromonas fortis. A beta-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharide. J Biol Chem. 2001;276(43):40202-9. DOI:10.1074/jbc.M100670200 |