Issue 27, 2012

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

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.

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

Supplementary files

Article information

Article type
Communication
Submitted
07 Dec 2011
Accepted
05 Jan 2012
First published
10 Jan 2012

Chem. Commun., 2012,48, 3288-3290

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

H. L. van Beek, G. D. Gonzalo and M. W. Fraaije, Chem. Commun., 2012, 48, 3288 DOI: 10.1039/C2CC17656D

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements