CoA Transferase and Malonyl-CoA Decarboxylase Activity of Malonate Decarboxylase from Acinetobacter calcoaceticus

  • Byun, Hye-Sin (Department of Biochemistry, College of Science, Bioproducts Research Center, Yonsei University) ;
  • Kim, Yu-Sam (Department of Biochemistry, College of Science, Bioproducts Research Center, Yonsei University)
  • Received : 1997.04.17
  • Published : 1997.07.31

Abstract

Malonate decarboxylase from Acinetobacter calcoaceticus is shown to have malonyl-CoA: acetate CoA transferase. acetyl-CoA: malonate CoA transferase, and malonyl-CoA decarboxylase activity. These enzyme activities were elucidated by isotope exchange reactions. The enzyme modified by N-ethylmaleimide completely lost its malonate decarboxylase activity, whereas it still kept CoA transferases and malonyl-CoA decarboxylase activities. The existence of CoA transferases and malonyl-CoA decarboxylase activity is clear, but their physiological significance is obscure. The catalytic reactions for two eoA transfers and malonyl-CoA decarboxylation proceed via a cyclic mechanism, which is through two covalent intermediates, enzyme-Smalonyl and enzyme-S-acetyL proposed for malonate decarboxylation of the enzyme.

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