Issue 45, 2012
From the journal:

Organic & Biomolecular Chemistry

Rational substrate and enzyme engineering of transketolase for aromatics†

Panwajee Payongsri,a   David Steadman,b   John Strafford,a   Andrew MacMurray,a   Helen C. Hailesb  and  Paul A. Dalby*a  

* Corresponding authors

a Advanced Centre for Biochemical Engineering, Department of Biochemical Engineering, University College London, Torrington Place, London, UK
E-mail: p.dalby@ucl.ac.uk

b Department of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, UK

Abstract

The uses of 3-formylbenzoic acid and 4-formylbenzoic acid as molecular probes along with previous and new transketolase mutants revealed the factors governing the rate of reaction between transketolase and aromatic aldehydes. The novel α,α-dihydroxyketones were produced at 15 to 30-fold higher yields and up to 250-fold higher specific activities with D469T TK when compared to those obtained for benzaldehyde.

Graphical abstract: Rational substrate and enzyme engineering of transketolase for aromatics

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Article information

DOI
https://doi.org/10.1039/C2OB25751C
Article type
Paper
Submitted
18 Apr 2012
Accepted
08 Oct 2012
First published
09 Oct 2012

Org. Biomol. Chem., 2012,10, 9021-9029

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Rational substrate and enzyme engineering of transketolase for aromatics

P. Payongsri, D. Steadman, J. Strafford, A. MacMurray, H. C. Hailes and P. A. Dalby, Org. Biomol. Chem., 2012, 10, 9021 DOI: 10.1039/C2OB25751C

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