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Issue 46, 2010
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Characterization of xenobiotic reductase A (XenA): study of active site residues, substrate spectrum and stability†‡

Yanto Yanto,a   Hua-Hsiang Yu,a   Mélanie Halla  and  Andreas S. Bommarius*ab  
Author affiliations

* Corresponding authors

a School of Chemical and Biomolecular Engineering, Parker H. Petit Institute of Bioengineering and Biosciences, Georgia Institute of Technology, 315 Ferst Drive, Atlanta, GA, USA
E-mail: andreas.bommarius@chbe.gatech.edu
Fax: (+1) 404-894-2291
Tel: (+1) 404-385-1334

b School of Chemistry and Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive, Atlanta, GA, USA

Abstract

Xenobiotic reductase A (XenA) has broad catalytic activity and reduces various α,β-unsaturated and nitro compounds with moderate to excellent stereoselectivity. Single mutants C25G and C25V are able to reduce nitrobenzene, a non-active substrate for the wild type, to produce aniline. Total turnover is dominated by chemical rather than thermal instability.

Graphical abstract: Characterization of xenobiotic reductase A (XenA): study of active site residues, substrate spectrum and stability

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Article information

https://doi.org/10.1039/C0CC02354J
Submitted
04 Jul 2010
Accepted
01 Oct 2010
First published
19 Oct 2010
Chem. Commun., 2010,46, 8809-8811
Article type
Communication
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Characterization of xenobiotic reductase A (XenA): study of active site residues, substrate spectrum and stability

Y. Yanto, H. Yu, M. Hall and A. S. Bommarius, Chem. Commun., 2010, 46, 8809
DOI: 10.1039/C0CC02354J

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