Arylmalonate decarboxylase-a highly selective bacterial biocatalyst with unknown function

Kenji Miyamoto, Robert Kourist

Research output: Contribution to journalArticleResearchpeer-review

Abstract

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)8621-31
Number of pages11
JournalApplied Microbiology and Biotechnology
Volume100
Issue number20
DOIs
Publication statusPublished - Oct 2016
Externally publishedYes

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Enzymes
Carboxy-Lyases
Carboxylic Acids
malonate decarboxylase

Keywords

  • Bordetella bronchiseptica
  • Carboxy-Lyases
  • Fatty Acids
  • Protein Conformation
  • Substrate Specificity
  • Journal Article
  • Review

Cite this

Arylmalonate decarboxylase-a highly selective bacterial biocatalyst with unknown function. / Miyamoto, Kenji; Kourist, Robert.

In: Applied Microbiology and Biotechnology, Vol. 100, No. 20, 10.2016, p. 8621-31.

Research output: Contribution to journalArticleResearchpeer-review

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