Changing the substrate specificity of P450cam towards diphenylmethane by semi-rational enzyme engineering.

doi:10.1093/protein/gzq119

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Article

Changing the substrate specificity of P450cam towards diphenylmethane by semi-rational enzyme engineering.

Protein engineering, design & selection : PEDS - 1 May 2011

Hoffmann Gregor, Bönsch Kathrin, Greiner-Stöffele Thomas, Ballschmiter Meike

Abstract excerpt

A focused library comprising nine residues of the active site of P450cam monooxygenase resulting in ∼ 300,000 protein variants was screened for activity on diphenylmethane (DPM). The assay was based on the depletion of NADH by an in vitro reconstituted P450cam system in a 96-well scale. The throughput was increased by the parallel cultivation, purification and analysis of 20 variants per well (cluster screening)....

Topics

Benzhydryl Compounds
Camphor 5-Monooxygenase
Catalytic Domain
Drug Discovery
Hydroxylation
Models, Molecular
Mutagenesis
Mutation
Protein Engineering
Pseudomonas putida
Stereoisomerism
Substrate Specificity

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Open in PubMed

Identifiers

PMID: 21273340
DOI: 10.1093/protein/gzq119

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