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- DOI: 10.1002/anie.200904112
- PMID: 19739187
- UKPMCID: 19739187
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Structure-Guided Directed Evolution of Alkenyl and Arylmalonate Decarboxylases
Okrasa, Krzysztof; Levy, Colin; Wilding, Matthew; Goodall, Mark; Baudendistel, Nina; Hauer, Bernhard; Leys, David; Micklefield, Jason
Angewandte Chemie International Edition. 2009;48(41):7691-7694.
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Full-text held externally
- DOI: 10.1002/anie.200904112
- PMID: 19739187
- UKPMCID: 19739187
Abstract
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 -alkenyl as well as -arylmalonates.