Issue 42, 2012
From the journal:

Chemical Communications

Bacterial CYP153A monooxygenases for the synthesis of omega-hydroxylated fatty acids†

Sumire Honda Malca,a   Daniel Scheps,a   Lisa Kühnel,a   Elena Venegas-Venegas,a   Alexander Seifert,a   Bettina M. Nestla  and  Bernhard Hauer*a  

* Corresponding authors

a Institute of Technical Biochemistry, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany
E-mail: bernhard.hauer@itb.uni-stuttgart.de
Fax: +49 711 68563196
Tel: +49 711 68563193

Abstract

CYP153A from Marinobacter aquaeolei has been identified as a fatty acid ω-hydroxylase with a broad substrate range. Two hotspots predicted to influence substrate specificity and selectivity were exchanged. Mutant G307A is 2- to 20-fold more active towards fatty acids than the wild-type. Residue L354 is determinant for the enzyme ω-regioselectivity.

Graphical abstract: Bacterial CYP153A monooxygenases for the synthesis of omega-hydroxylated fatty acids

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Article information

DOI
https://doi.org/10.1039/C2CC18103G
Article type
Communication
Submitted
27 Dec 2011
Accepted
23 Mar 2012
First published
26 Mar 2012

Chem. Commun., 2012,48, 5115-5117

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Bacterial CYP153A monooxygenases for the synthesis of omega-hydroxylated fatty acids

S. Honda Malca, D. Scheps, L. Kühnel, E. Venegas-Venegas, A. Seifert, B. M. Nestl and B. Hauer, Chem. Commun., 2012, 48, 5115 DOI: 10.1039/C2CC18103G

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