Journal
CHEMBIOCHEM
Volume 16, Issue 11, Pages 1670-1679Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201500125
Keywords
acetylation; biotransformations; chloramphenicol acetyltransferases; regioselectivity; steroids
Funding
- Deutscher Akademischer Austausch Dienst (DAAD) (Germany)
- Ministry of Higher Education and Scientific Research (MoHER) (Iraq)
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Chloramphenicol acetyltransferase I (CATI) detoxifies the antibiotic chloramphenicol and confers a corresponding resistance to bacteria. In this study we identified this enzyme as a steroid acetyltransferase and designed a new and efficient Escherichia-coli-based biocatalyst for the regioselective acetylation of C21 hydroxy groups in steroids of pharmaceutical interest. The cells carried a recombinant catI gene controlled by a constitutive promoter. The capacity of the whole-cell system to modify different hydroxysteroids was investigated, and NMR spectroscopy revealed that all substrates were selectively transformed into the corresponding 21-acetoxy derivatives. The biotransformation was optimized, and the reaction mechanism is discussed on the basis of a computationally modeled substrate docking into the crystal structure of CATI.
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