Structure‐Guided Directed Evolution of Alkenyl and Arylmalonate Decarboxylases | Zendy

Okrasa Krzysztof | Zendy; Levy Colin | Zendy; Wilding Matthew | Zendy; Goodall Mark | Zendy; Baudendistel Nina | Zendy; Hauer Bernhard | Zendy; Leys David | Zendy; Micklefield Jason | Zendy

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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.

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