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Chembiochem. 2016 Jan 1;17(1):90-101. doi: 10.1002/cbic.201500420. Epub 2015 Nov 20.

Substrate Hunting for the Myxobacterial CYP260A1 Revealed New 1α-Hydroxylated Products from C-19 Steroids.

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Universität des Saarlandes, Biochemie, Campus B2.2, 66123, Saarbrücken, Germany.
Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Strasse 10, 13125, Berlin, Germany.
Universität des Saarlandes, Pharmazeutische Biologie, Campus C2.2, 66123, Saarbrücken, Germany.
Universität des Saarlandes, Biochemie, Campus B2.2, 66123, Saarbrücken, Germany.


Cytochromes P450 catalyze a variety of synthetically useful reactions. However, it is difficult to determine their physiological or artificial functions when a plethora of orphan P450 systems are present in a genome. CYP260A1 from Sorangium cellulosum So ce56 is a new member among the 21 available P450s in the strain. To identify putative substrates for CYP260A1 we used high-throughput screening of a compound library (ca. 17,000 ligands). Structural analogues of the type I hits were searched for biotechnologically relevant compounds, and this led us to select C-19 steroids as potential substrates. We identified efficient surrogate redox partners for CYP260A1, and an Escherichia coli-based whole-cell biocatalyst system was developed to convert testosterone, androstenedione, and their derivatives methyltestosterone and 11-oxoandrostenedione. A detailed (1) H and (13) C NMR characterization of the product(s) from C-19 steroids revealed that CYP260A1 is the very first 1α-steroid hydroxylase.


Sorangium cellulosum; cytochromes P450; high-throughput screening; hydroxylation; steroids

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