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Characterization of the reversible nature of the reaction catalyzed by sphingolipid ceramide N ‐deacylase: A novel form of reverse hydrolysis reaction by Katsuhiro Kita; Toyohisa Kurita; Makoto Ito is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Sphingolipid ceramide __N__‐deacylase catalyzes a reversible reaction in which the amide linkages of the ceramides of various sphingolipids are cleaved or synthesized. Hydrolysis of sphingolipids by the enzyme proceeded efficiently at acidic pH in the presence of high concentrations of detergents, whereas the reverse reaction tended to be favored at neutral pH with a decrease in the detergent concentration. Although the catalytic efficiency (__V__~max~/__K__~m~) of the hydrolysis and reverse reactions was changed mainly by the concentration of detergents in the reaction mixture, __V__~max~ and __K__~m~ for the reverse reaction were relatively higher than those for the forward reaction, irrespective of the detergent concentration. The reverse reaction proceeded most efficiently when the molar ratio of lyso‐sphingolipids and fatty acids was fixed at 1 : 1–2, the yield of the reaction exceeding 70–80%. The reverse and exchange (transacylation) reactions did not require ATP, CoA, metal ions or addition of organic solvents. Studies using inhibitors and chemical modifiers of the enzyme protein suggested that both the hydrolysis and condensation reactions are catalyzed at the same catalyt

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Author

Katsuhiro Kita; Toyohisa Kurita; Makoto Ito

Publisher

John Wiley and Sons; Springer; Wiley (Blackwell Publishing); Springer-Verlag; Blackwell Publishing Inc.; Springer Verlag; Wiley; Springer Science and Business Media LLC (ISSN 1432-1327)

Published

2001

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)