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Structure‐Guided Directed Evolution of Alkenyl and Arylmalonate Decarboxylases
Author(s) -
Okrasa Krzysztof,
Levy Colin,
Wilding Matthew,
Goodall Mark,
Baudendistel Nina,
Hauer Bernhard,
Leys David,
Micklefield Jason
Publication year - 2009
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200904112
Subject(s) - mechanism (biology) , repertoire , active site , directed evolution , crystal structure , stereochemistry , enzyme , chemistry , crystallography , biochemistry , physics , quantum mechanics , acoustics , mutant , gene
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.