Promiscuous enantioselective (-)-γ-lactamase activity in the Pseudomonas fluorescens esterase I

Organic & Biomolecular Chemistry
Leticia L TorresAurelio Hidalgo

Abstract

A promiscuous but very enantioselective (-)-γ-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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Citations

Mar 20, 2013·The FEBS Journal·Per-Olof Syrén
Dec 17, 2014·Applied Microbiology and Biotechnology·Jianjun WangSheng Wu
Jan 1, 2012·Computational and Structural Biotechnology Journal·Kerstin Steiner, Helmut Schwab
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Oct 26, 2018·Journal of Industrial Microbiology & Biotechnology·Shaozhou Zhu, Guojun Zheng
Dec 17, 2020·Chemical Society Reviews·Sjoerd Slagman, Wolf-Dieter Fessner

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