抄録
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.
本文言語 | English |
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ページ(範囲) | 8621-8631 |
ページ数 | 11 |
ジャーナル | Applied Microbiology and Biotechnology |
巻 | 100 |
号 | 20 |
DOI | |
出版ステータス | Published - 2016 10月 1 |
ASJC Scopus subject areas
- バイオテクノロジー
- 応用微生物学とバイオテクノロジー