EC 3 - Hydrolases
EC 3.2 - Glycosylases
EC 3.2.1 - Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl compounds
EC 3.2.1.83 - κ-carrageenase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 3.2.1.83
Names
Accepted name:
κ-carrageenase
Other
name:
κ-carrageenan 4-β-D-glycanohydrolase
Systematic name:
κ-carrageenan 4-β-D-glycanohydrolase (configuration-retaining)
Reaction
- Endohydrolysis of (1→4)-β-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in κ-carrageenans.
Comments:
The main products of hydrolysis are neocarrabiose-sulfate and neocarratetraose-sulfate [5]. Unlike EC 3.2.1.157 (ι-carrageenase), but similar to EC 3.2.1.81 (β-agarase), this enzyme proceeds with retention of the anomeric configuration.
Links to other databases
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
DIAGRAM
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
UniPathway
Protein domains and families:
PROSITE:PDOC00794
Gene Ontology:
GO:0033918
CAS Registry Number:
37288-59-8
UniProtKB/Swiss-Prot:
CGKA_PSEVC
References
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The enzymic hydrolysis of carrageenan by Pseudomonas carrageenovora: purification of a κ-carrageenase.Can. J. Microbiol. 12: 939-947 (1966). [PMID: 5972647]
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Purification and characterization of a new κ-carrageenase from a marine Cytophaga-like bacterium.Eur. J. Biochem. 201: 241-247 (1991). [PMID: 1915370]
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Processing and hydrolytic mechanism of the cgkA-encoded κ-carrageenase of Alteromonas carrageenovora.Eur. J. Biochem. 228: 971-975 (1995). [PMID: 7737202]
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Expression, purification, crystallization and preliminary X-ray analysis of the κ-carrageenase from Pseudoalteromonas carrageenovora.Acta Crystallogr. D Biol. Crystallogr. 55: 918-920 (1999). [PMID: 10089334]
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The κ-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases.Structure 9: 513-525 (2001). [PMID: 11435116]
[EC 3.2.1.83 created 1972, modified 2006]