The Enzyme Database

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EC 3.2.1.83     
Accepted name: κ-carrageenase
Reaction: Endohydrolysis of (1→4)-β-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in κ-carrageenans
For diagram of reaction, click here
Glossary: In the field of oligosaccharides derived from agarose, carrageenans, etc., in which alternate residues are 3,6-anhydro sugars, the prefix ’neo’ designates an oligosaccharide whose non-reducing end is the anhydro sugar, and the absence of this prefix means that it is not.
For example:
ι-neocarrabiose = 3,6-anhydro-2-O-sulfo-α-D-galactopyranosyl-(1→3)-4-O-sulfo-D-galactose
ι-carrabiose = 4-O-sulfo- β-D-galactopyranosyl-(1→4)-3,6-anhydro-2-O-sulfo-D-galactose
Other name(s): κ-carrageenan 4-β-D-glycanohydrolase
Systematic name: κ-carrageenan 4-β-D-glycanohydrolase (configuration-retaining)
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: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-59-8
References:
1.  Weigl, J. and Yashe, W. The enzymic hydrolysis of carrageenan by Pseudomonas carrageenovora: purification of a κ-carrageenase. Can. J. Microbiol. 12 (1966) 939–947. [PMID: 5972647]
2.  Potin, P., Sanseau, A., Le Gall, Y., Rochas, C. and Kloareg, B. Purification and characterization of a new κ-carrageenase from a marine Cytophaga-like bacterium. Eur. J. Biochem. 201 (1991) 241–247. [PMID: 1915370]
3.  Potin, P., Richard, C., Barbeyron, T., Henrissat, B., Gey, C., Petillot, Y., Forest, E., Dideberg, O., Rochas, C. and Kloareg, B. Processing and hydrolytic mechanism of the cgkA-encoded κ-carrageenase of Alteromonas carrageenovora. Eur. J. Biochem. 228 (1995) 971–975. [PMID: 7737202]
4.  Michel, G., Barbeyron, T., Flament, D., Vernet, T., Kloareg, B. and Dideberg, O. Expression, purification, crystallization and preliminary x-ray analysis of the κ-carrageenase from Pseudoalteromonas carrageenovora. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 918–920. [PMID: 10089334]
5.  Michel, G., Chantalat, L., Duee, E., Barbeyron, T., Henrissat, B., Kloareg, B. and Dideberg, O. 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 (2001) 513–525. [PMID: 11435116]
[EC 3.2.1.83 created 1972, modified 2006]
 
 


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