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Arylmalonate decarboxylase—a highly selective bacterial biocatalyst with unknown function

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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.

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Acknowledgments

The authors thank Florian Busch (Ruhr-Universität Bochum, Germany) and Marco Bocola (RWTH Aachen, Germany) for very insightful suggestions regarding the mechanism of AMDase and Janine Maimanakos for discussions of the biological distribution of the enzyme and the phylogenetic analysis of the asp/glu racemase superfamily. The authors thank the North Rhine-Westphalian Ministry for Innovation, Science and Investigation (award number PtJ-TRI/1411ng006) and the German Academic Exchange Service (award number 57154401) for financial support.

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Authors and Affiliations

  1. Department for Biosciences and Bioinformatics, Keio University, 3-14-1 Hiyoshi, Yokohama, 223-8522, Japan

    Kenji Miyamoto

  2. Junior Research Group for Microbial Biotechnology, Ruhr-University Bochum, 44780, Bochum, Germany

    Robert Kourist

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  1. Kenji Miyamoto
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  2. Robert Kourist
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Correspondence to Robert Kourist.

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Funding

This study was funded by the North Rhine-Westphalian Ministry for Innovation, Science and Investigation (award number PtJ-TRI/1411ng006) and the German Academic Exchange Service (award number 57154401).

Conflict of interest

Robert Kourist declares that he has no conflict of interest.

Kenji Miyamoto declares that he has no conflict of interest.

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This article does not contain any studies with human participants or animals performed by any of the authors.”

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Miyamoto, K., Kourist, R. Arylmalonate decarboxylase—a highly selective bacterial biocatalyst with unknown function. Appl Microbiol Biotechnol 100, 8621–8631 (2016). https://doi.org/10.1007/s00253-016-7778-z

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  • DOI: https://doi.org/10.1007/s00253-016-7778-z

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