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Glycoside Hydrolase Family 82
From CAZypedia
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| Glycoside Hydrolase Family GH82 | |
| Clan | none |
| Mechanism | inverting |
| Active site residues | not known |
| CAZy DB link | |
| http://www.cazy.org/fam/GH82.html | |
Contents |
Substrate specificities
The two known members of glycoside hydrolase 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
From structural analysis predicted to be two out of the three candidate amino acids Glu245, Asp247 or Glu310 in the A. fortis iota-carrageenase [2].
Three-dimensional structures
To date, a crystal structure has only been determined for the iota-carrageenase from A. fortis [2]. The crystal structure of a product complex has shed light on the existance of domain movement of domain A that is closed around the oligo-carrageenan in the complexed form and open in the uncomplexed enzyme [3].
Family Firsts
- First sequence identification and family creation
- iota-carrageenase sequences have been first reported for enzymes from A. fortis and Z. galactanivorans [1].
- First sterochemistry determination
- GH82 enzymes are inverting as shown by NMR [1].
- First general acid residue identification
- not determined yet.
- First general base residue identification
- not determined yet.
- First 3-D structure
iota-carrageenase from A. fortis [2]. The structure belongs to the β-helix fold (PDB 1h80 and PDB 1ktw).
References
Note: Due to an issue with PubMed data, please set your browser's character encoding to Western (ISO-8859-1) (under the 'View' menu) to properly render non-English characters in author names.- Barbeyron T, Michel G, Potin P, Henrissat B, and Kloareg B. iota-Carrageenases constitute a novel family of glycoside hydrolases, unrelated to that of kappa-carrageenases. J Biol Chem 2000 Nov 10; 275(45) 35499-505. doi:10.1074/jbc.M003404200 pmid:10934194.
- Michel G, Chantalat L, Fanchon E, Henrissat B, Kloareg B, and Dideberg O. The iota-carrageenase of Alteromonas fortis. A beta-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharide. J Biol Chem 2001 Oct 26; 276(43) 40202-9. doi:10.1074/jbc.M100670200 pmid:11493601.
- Michel G, Helbert W, Kahn R, Dideberg O, and Kloareg B. The structural bases of the processive degradation of iota-carrageenan, a main cell wall polysaccharide of red algae. J Mol Biol 2003 Nov 28; 334(3) 421-33. pmid:14623184.

