Discovery of arylmalonate decarboxylase and conversion of the function by rational design

Kenji Miyamoto, Hiromichi Ohta

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Citation (Scopus)


Decarboxylation of malonic acid is a well-known process in the biosynthesis of long-chain fatty acids starting from acetic acid. If this kind of enzymes exhibits enantioselectivity for asubstituted malonates, it will be useful as a novel method for preparing optically active carboxylic acids. Indeed malonyl-CoA decarboxylase from uropygial gland is enantioselective to the substrate and the product. Racemate of methylmalonyl-CoA (1) was incubated with the above decarboxylase in 3H2O. (S)-Enantiomer was smoothly decarboxylated to result in 2-(3H)-propionyl-CoA (2), while (R)-isomer of the substrate remained intact (Equation 21.1). The absolute configuration of α-carbon of resulting 2 was revealed to be (R). Thus, the decarboxylase distinguishes the chirality of 1 and gives enantiomerically pure (R)-isomer by retention of configuration [1].

Original languageEnglish
Title of host publicationBiocatalysis in the Pharmaceutical and Biotechnology Industries
PublisherCRC Press
Number of pages15
ISBN (Electronic)9781420019377
ISBN (Print)9780849337321
Publication statusPublished - 2006 Jan 1

ASJC Scopus subject areas

  • General Biochemistry,Genetics and Molecular Biology
  • General Chemistry
  • General Chemical Engineering
  • General Medicine
  • Pharmacology, Toxicology and Pharmaceutics(all)


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