Arylmalonate decarboxylase—a highly selective bacterial biocatalyst with unknown function

Kenji Miyamoto, Robert Kourist

Research output: Contribution to journalReview articlepeer-review

11 Citations (Scopus)


Bacterial arylmalonate decarboxylase (AMDase) shows high enantioselectivity and a broad substrate spectrum in the asymmetric synthesis of optically pure arylaliphatic carboxylic acids. The determination of the structure of AMDase has greatly extended the understanding of the catalytic mechanism of this unique cofactor-free decarboxylase and allowed the generation of tailor-made enzyme variants with improved catalytic properties. Despite this increase in knowledge and applicability, the natural role of the enzyme remains unknown. This mini-review summarizes the recent findings on the molecular mechanism and the synthetic application of the enzyme.

Original languageEnglish
Pages (from-to)8621-8631
Number of pages11
JournalApplied Microbiology and Biotechnology
Issue number20
Publication statusPublished - 2016 Oct 1


  • Asymmetric synthesis
  • Biocatalysis
  • Catalytic promiscuity
  • Cofactor-free decarboxylases
  • Enzyme engineering
  • Lyases

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology


Dive into the research topics of 'Arylmalonate decarboxylase—a highly selective bacterial biocatalyst with unknown function'. Together they form a unique fingerprint.

Cite this