期刊
ORGANIC & BIOMOLECULAR CHEMISTRY
卷 10, 期 17, 页码 3388-3392出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c2ob06887g
关键词
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资金
- Spanish Ministry of Science [BIO2008-01481, RyC2006-02441, BFU 2008-01711]
- Fundacion Ramon Areces
- Deutsche Bundesstiftung Umwelt (Osnabruck, Germany) [AZ13159]
A promiscuous but very enantioselective (-)-gamma-lactamase activity in the kinetic resolution of the Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) was detected in the Pseudomonas fluorescens esterase I (PFEI). The lactamase activity was increased 200-fold by the introduction of a point mutation and resulted as enantioselective as the Microbacterium sp. enzyme used industrially in this resolution. The structural and mechanistic determinants for the catalytic promiscuity and enantioselectivity were identified by molecular modeling, setting a ground stone to engineer further amidase-related activities from this esterase.
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