title: Arylmalonate decarboxylase-a highly selective bacterial biocatalyst with unknown function.
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.
authors: Department for Biosciences and Bioinformatics, Keio University, 3-14-1 Hiyoshi, Yokohama, 223-8522, Japan.
authors: Kenji
authors: K
authors: Miyamoto
authors: Junior Research Group for Microbial Biotechnology, Ruhr-University Bochum, 44780, Bochum, Germany. Robert.Kourist@rub.de.
authors: Robert
authors: http://orcid.org/0000-0002-2853-3525
authors: R
authors: Kourist
mesh_terms: D016950:Bordetella bronchiseptica / Q000201:enzymology*; D002262:Carboxy-Lyases / Q000378:metabolism*; D005227:Fatty Acids / Q000378:metabolism; D011487:Protein Conformation; D013379:Substrate Specificity
chemical_list: D005227:Fatty Acids; D002262:Carboxy-Lyases; C071852:malonate decarboxylase
keywords: Asymmetric synthesis; Biocatalysis; Catalytic promiscuity; Cofactor-free decarboxylases; Enzyme engineering; Lyases