Iota-carrageenase
| Iota-carrageenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.157 | ||||||||
| CAS no. | 50936-37-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Iota-carrageenase (EC 3.2.1.157) is an enzyme with systematic name iota-carrageenan 4-beta-D-glycanohydrolase (configuration-inverting).[1][2][3] This enzyme catalyses the following chemical reaction
- Endohydrolysis of (1->4)-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose-2-sulfate in iota-carrageenans
The main products of hydrolysis are iota-neocarratetraose sulfate and iota-neocarrahexaose sulfate.
References
- ^ Barbeyron T, Michel G, Potin P, Henrissat B, Kloareg B (November 2000). "iota-Carrageenases constitute a novel family of glycoside hydrolases, unrelated to that of kappa-carrageenases". The Journal of Biological Chemistry. 275 (45): 35499–505. doi:10.1074/jbc.m003404200. PMID 10934194.
- ^ Michel G, Chantalat L, Fanchon E, Henrissat B, Kloareg B, Dideberg O (October 2001). "The iota-carrageenase of Alteromonas fortis. A beta-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharide". The Journal of Biological Chemistry. 276 (43): 40202–9. doi:10.1074/jbc.M100670200. PMID 11493601.
- ^ Michel G, Helbert W, Kahn R, Dideberg O, Kloareg B (November 2003). "The structural bases of the processive degradation of iota-carrageenan, a main cell wall polysaccharide of red algae". Journal of Molecular Biology. 334 (3): 421–33. doi:10.1016/j.jmb.2003.09.056. PMID 14623184.
External links
- Iota-carrageenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
