Cyclization of a cellular dipentaenone by Streptomyces coelicolor cytochrome P450 154A1 without oxidation/reduction.
We report a comprehensive genetic, metabolomic, and biochemical study on the catalytic properties of Streptomyces coelicolor cytochrome P450 (P450) 154A1, known to have a unique heme orientation in its crystal structure. Deletion of the P450 154A1 gene compromised the long-term stability of the bacterial spores. A novel dipentaenone (1) with a high degree of conjugation was identified as an endogenous substrate of P450 154A1 using a metabolomics approach. The biotransformation of 1 by P450 154A1 was shown to be an unexpected intramolecular cyclization to a Paternò-Büchi-like product, without oxidation/reduction.
Cheng
Qian
Q
Department of Biochemistry and Center in Molecular Toxicology, Vanderbilt University, School of Medicine, Nashville Tennessee 37232-0146, USA.
Lamb
David C
DC
Kelly
Steven L
SL
Lei
Li
L
Guengerich
F Peter
FP
D002851:Chromatography, High Pressure Liquid; D003500:Cyclization; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D010084:Oxidation-Reduction; D010422:Pentanones / Q000737:chemistry* / Q000378:metabolism*; D048372:Streptomyces coelicolor / Q000201:enzymology*
D010422:Pentanones; D003577:Cytochrome P-450 Enzyme System