Structural basis of steroid binding and oxidation by the cytochrome P450 CYP109E1 from Bacillus megaterium

Cytochrome P450 monooxygenases (P450s) are attractive enzymes for the pharmaceutical industry, in particular, for applications in steroidal drug synthesis. Here, we report a comprehensive functional and structural characterization of CYP109E1, a novel steroid‐converting cytochrome P450 enzyme identi...

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Bibliographic Details
Published in:	The FEBS journal Vol. 283; no. 22; pp. 4128 - 4148
Main Authors:	Jóźwik, Ilona K., Kiss, Flora M., Gricman, Łukasz, Abdulmughni, Ammar, Brill, Elisa, Zapp, Josef, Pleiss, Juergen, Bernhardt, Rita, Thunnissen, Andy‐Mark W. H.
Format:	Journal Article
Language:	English
Published:	England Blackwell Publishing Ltd 01-11-2016 John Wiley and Sons Inc
Subjects:	Amino Acid Sequence Bacillus megaterium Bacillus megaterium - enzymology Bacillus megaterium - genetics Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology Binding Sites - genetics Catalytic Domain Corticosterone - chemistry Corticosterone - metabolism crystallography Crystallography, X-Ray Cytochrome P-450 Enzyme System - chemistry Cytochrome P-450 Enzyme System - classification Cytochrome P-450 Enzyme System - metabolism cytochrome P450 Enzymes Heme - chemistry Heme - metabolism Molecular Dynamics Simulation Molecular Structure Original Oxidation Oxidation-Reduction Pharmacology Protein Binding Protein Domains Sequence Homology, Amino Acid steroid Steroids Steroids - chemistry Steroids - metabolism structure‐function Substrate Specificity testosterone Testosterone - chemistry Testosterone - metabolism structure-function crystallography cytochrome P450 testosterone steroid
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