Stereochemistry of the methylmalonyl-CoA decarboxylation reaction

FEBS Lett. 1987 Aug 10;220(1):121-5. doi: 10.1016/0014-5793(87)80888-8.

Abstract

The steric course of the decarboxylation of (S)-methylmalonyl-CoA to propionyl-CoA, catalyzed by the biotin-dependent sodium pump methylmalonyl-CoA decarboxylase of Veillonella alcalescens was determined. The decarboxylation of (S)-methylmalonyl-CoA in 3H2O yielded (R)-[2-3H]propionyl-CoA; and the decarboxylation of (S)-[2-3H]methylmalonyl-CoA in H2O produced (S)-[2-3H]propionyl-CoA. The results demonstrate retention of configuration during the decarboxylation reaction. The substrate stereochemistry of methylmalonyl-CoA decarboxylase is thus the same as that of all other biotin-containing enzymes investigated.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl Coenzyme A / analogs & derivatives*
  • Acyl Coenzyme A / metabolism
  • Biotin / pharmacology
  • Carboxy-Lyases / metabolism
  • Catalysis
  • Decarboxylation
  • Malonyl Coenzyme A / analogs & derivatives*
  • Malonyl Coenzyme A / metabolism
  • Methylmalonyl-CoA Decarboxylase
  • Veillonella / enzymology

Substances

  • Acyl Coenzyme A
  • methylmalonyl-coenzyme A
  • propionyl-coenzyme A
  • Malonyl Coenzyme A
  • Biotin
  • Carboxy-Lyases
  • Methylmalonyl-CoA Decarboxylase