Arylmalonate decarboxylase-a highly selective bacterial biocatalyst with unknown function.
Appl Microbiol Biotechnol
; 100(20): 8621-31, 2016 Oct.
Article
em En
| MEDLINE
| ID: mdl-27566691
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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Base de dados:
MEDLINE
Assunto principal:
Carboxiliases
/
Bordetella bronchiseptica
Idioma:
En
Revista:
Appl Microbiol Biotechnol
Ano de publicação:
2016
Tipo de documento:
Article
País de afiliação:
Japão