FMP Publications

Our publications are recorded in a searchable database since 2010, updates will be added regularly.

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Substrate Hunting for the Myxobacterial CYP260A1 Revealed New 1alpha-Hydroxylated Products from C-19 Steroids
Khatri(*), Y., Ringle(*), M., Lisurek, M., von Kries, J. P., Zapp(*), J.; Bernhardt(*), R.
Chembiochem, 17:90-101

Tags: Screening Unit (von Kries), Structural Bioinformatics and Protein Design (Krause, G.)

Abstract: 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 1alpha-steroid hydroxylase.

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Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP)
Campus Berlin-Buch
Robert-Roessle-Str. 10
13125 Berlin, Germany
+4930 94793 - 100 
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