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. (2000). "ι-Carrageenases constitute a novel family of glycoside hydrolases, unrelated to that of κ-carrageenases". J. Biol. Chem. 275 (45): 35499–35505. doi:10.1074/jbc.m003404200. PMID 10934194.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Michel, G.; Chantalat, L.; Fanchon, E.; Henrissat, B.; Kloareg, B.; Dideberg, O. (2001). "The ι-carrageenase of Alteromonas fortis. A β-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharide". J. Biol. Chem. 276 (43): 40202–40209. doi:10.1074/jbc.M100670200. PMID 11493601.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Michel, G.; Helbert, W.; Kahn, R.; Dideberg, O.; Kloareg, B. (2003). "The structural bases of the processive degradation of ι-carrageenan, a main cell wall polysaccharide of red algae". J. Mol. Biol. 334 (3): 421–433. 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)