Substrate stereochemistry of 2-methyl-branched-chain acyl-CoA dehydrogenase: elimination of one hydrogen each from pro-2S)-methyl and α-methine of isobutyryl-CoA

Kay Tanaka, John J. O'Shea, Gaetano Finocchiaro, Yasuyuki Ikeda, D. John Aberhart, Pallab K. Ghoshal

Research output: Contribution to journalArticlepeer-review

Abstract

Dehydrogenation of (2S)-[3-13C]isobutyryl-CoA was carried out in vitro using 2-methyl-branched-chain acyl-CoA dehydrogenase purified from rat liver mitochondria. The product was subsequently hydrated by the addition of bovine crotonase. The resulting 3-hydroxyisobutyric acid was predominantly enriched with 13C at the β-hydroxy position as determined as a methyl ester using electron ionization-gas chromatography-mass spectroscopy. This finding indicates that isobutyryl-CoA is dehydrogenated stereospecifically at the (pro-2S)-methyl and α-methine groups to form methacrylyl-CoA, which is later hydrated with the addition of hydrogen on the same side of the molecule from which it was subtracted to produce 3-hydroxyisobutyryl-CoA.

Original languageEnglish
Pages (from-to)308-311
Number of pages4
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume873
Issue number2
DOIs
Publication statusPublished - Sep 26 1986

Keywords

  • 2-methyl-branched-chain acyl-CoA
  • Acyl-CoA dehydrogenase
  • Substrate stereochemistry

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology

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