Structure-Guided Directed Evolution of Alkenyl and Arylmalonate Decarboxylases

被引：59

作者：

Okrasa, Krzysztof ^{[2
]}

Levy, Colin ^{[1
]}

Wilding, Matthew ^{[2
]}

Goodall, Mark ^{[2
]}

Baudendistel, Nina ^{[3
]}

Hauer, Bernhard ^{[3
]}

Leys, David ^{[1
]}

Micklefield, Jason ^{[2
]}

机构：

[1] Univ Manchester, Fac Life Sci, Manchester Interdisciplinary Bioctr, Manchester M1 7ND, Lancs, England

[2] Univ Manchester, Sch Chem, Manchester Interdisciplinary Bioctr, Manchester M1 7ND, Lancs, England

[3] BASF SE, GVFE, D-67056 Ludwigshafen, Germany

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2009年 / 48卷 / 41期

关键词：

decarboxylase; directed evolution; enediolates; enzyme mechanisms; inhibitors; ALCALIGENES-BRONCHISEPTICUS KU-1201; ITERATIVE SATURATION MUTAGENESIS; ASYMMETRIC DECARBOXYLATION; REACTION-MECHANISM; ACID; PURIFICATION; ENANTIOSELECTIVITY; DERIVATIVES; PROTONATION; EXPRESSION;

D O I：

10.1002/anie.200904112

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Rational enhancement: The X-ray crystal structure of an arylmalonate decarboxylase (AMDase) with a mechanism-based inhibitor bound to an active-site dioxyanion hole provides insight into the mechanism of this intriguing enzyme. The structure also guided the extension of the AMDase biocatalytic repertoire to include a wide range of α-alkenyl as well as α-arylmalonates. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：7691 / 7694

页数：4

共 32 条

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