Blending Baeyer-Villiger monooxygenases: using a robust BVMO as a scaffold for creating chimeric enzymes with novel catalytic properties

Hugo L van Beek; Gonzalo de Gonzalo; Marco W Fraaije

doi:10.1039/c2cc17656d

Blending Baeyer-Villiger monooxygenases: using a robust BVMO as a scaffold for creating chimeric enzymes with novel catalytic properties

Chem Commun (Camb). 2012 Apr 4;48(27):3288-90. doi: 10.1039/c2cc17656d. Epub 2012 Jan 27.

Authors

Hugo L van Beek¹, Gonzalo de Gonzalo, Marco W Fraaije

Affiliation

¹ Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.

PMID: 22286124
DOI: 10.1039/c2cc17656d

Abstract

The thermostable Baeyer-Villiger monooxygenase (BVMO) phenylacetone monooxygenase (PAMO) is used as a scaffold to introduce novel selectivities from other BVMOs or the metagenome by structure-inspired subdomain exchanges. This yields biocatalysts with new preferences in the oxidation of sulfides and the Baeyer-Villiger oxidation of ketones, all while maintaining most of the original thermostability.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Acetone / analogs & derivatives
Acetone / metabolism
Biocatalysis
Kinetics
Metagenome
Mixed Function Oxygenases / chemistry*
Mixed Function Oxygenases / genetics
Models, Molecular
NADH, NADPH Oxidoreductases / chemistry
NADH, NADPH Oxidoreductases / genetics
Oxidation-Reduction
Oxygenases / chemistry
Oxygenases / genetics
Protein Engineering
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Fusion Proteins / chemistry*
Recombinant Fusion Proteins / genetics
Stereoisomerism
Substrate Specificity

Substances

Recombinant Fusion Proteins
Acetone
Mixed Function Oxygenases
Oxygenases
cyclohexanone oxygenase
NADH, NADPH Oxidoreductases
NAD phosphite oxidoreductase
1-phenyl-2-propanone