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Issue 45, 2012
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Rational substrate and enzyme engineering of transketolase for aromatics

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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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Publication details

The article was received on 18 Apr 2012, accepted on 08 Oct 2012 and first published on 09 Oct 2012


Article type: Paper
DOI: 10.1039/C2OB25751C
Citation: 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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