κ-Carrageenase

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κ-Carrageenase
Identifiers
EC no.3.2.1.83
CAS no.37288-59-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
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MetaCycmetabolic pathway
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κ-Carrageenase (EC 3.2.1.83, κ-carrageenan 4-β-D-glycanohydrolase) is an enzyme with systematic name κ-carrageenan 4-β-D-glycanohydrolase (configuration-retaining).[1][2][3][4][5] It catalyses the endohydrolysis of (1→4)-β-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in κ-carrageenans

The main products of hydrolysis are neocarrabiose-sulfate and neocarratetraose-sulfate.

References[edit]

  1. ^ Weigl J, Yaphe W (October 1966). "The enzymic hydrolysis of carrageenan by Pseudomonas carrageenovora: purification of a κ-carrageenase". Canadian Journal of Microbiology. 12 (5): 939–47. doi:10.1139/m66-127. PMID 5972647.
  2. ^ Potin P, Sanseau A, Le Gall Y, Rochas C, Kloareg B (October 1991). "Purification and characterization of a new κ-carrageenase from a marine Cytophaga-like bacterium". European Journal of Biochemistry. 201 (1): 241–7. doi:10.1111/j.1432-1033.1991.tb16280.x. PMID 1915370.
  3. ^ Potin P, Richard C, Barbeyron T, Henrissat B, Gey C, Petillot Y, Forest E, Dideberg O, Rochas C, Kloareg B (March 1995). "Processing and hydrolytic mechanism of the cgkA-encoded κ-carrageenase of Alteromonas carrageenovora". European Journal of Biochemistry. 228 (3): 971–5. doi:10.1111/j.1432-1033.1995.tb20348.x. PMID 7737202.
  4. ^ Michel G, Barbeyron T, Flament D, Vernet T, Kloareg B, Dideberg O (April 1999). "Expression, purification, crystallization and preliminary x-ray analysis of the κ-carrageenase from Pseudoalteromonas carrageenovora". Acta Crystallographica Section D. 55 (Pt 4): 918–20. doi:10.1107/s0907444998018526. PMID 10089334.
  5. ^ Michel G, Chantalat L, Duee E, Barbeyron T, Henrissat B, Kloareg B, Dideberg O (June 2001). "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 (6): 513–25. doi:10.1016/s0969-2126(01)00612-8. PMID 11435116.

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