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Issue 11, 2013
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Sterol 3β-glucosyltransferase biocatalysts with a range of selectivities, including selectivity for testosterone

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Abstract

The main objectives of this work were to characterise a range of purified recombinant sterol 3β-glucosyltransferases and show that rational sampling of the diversity that exists within sterol 3β-glucosyltransferase sequence space can result in a range of enzyme selectivities. In our study the catalytically active domain of the Saccharomyces cerevisiae 3β-glucosyltransferase was used to mine putative sterol 3β-glucosyltransferases from the databases. Selected diverse sequences were expressed in and purified from Escherichia coli and shown to have different selectivities for the 3β-hydroxysteroids ergosterol and cholesterol. Surprisingly, three enzymes were also selective for testosterone, a 17β-hydroxysteroid. This study therefore reports for the first time sterol 3β-glucosyltransferases with selectivity for both 3β- and 17β-hydroxysteroids and is also the first report of recombinant 3β-glucosyltransferases with selectivity for steroids with a hydroxyl group at positions other than C-3. These enzymes could therefore find utility in the pharmaceutical industry for the green synthesis of a range of glycosylated compounds of medicinal interest.

Graphical abstract: Sterol 3β-glucosyltransferase biocatalysts with a range of selectivities, including selectivity for testosterone

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Article information


Submitted
23 Jul 2013
Accepted
29 Aug 2013
First published
30 Aug 2013

This article is Open Access

Mol. BioSyst., 2013,9, 2816-2822
Article type
Paper

Sterol 3β-glucosyltransferase biocatalysts with a range of selectivities, including selectivity for testosterone

V. Malik, M. Zhang, L. G. Dover, J. S. Northen, A. Flinn, J. J. Perry and G. W. Black, Mol. BioSyst., 2013, 9, 2816
DOI: 10.1039/C3MB70303G

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