Cyclization of a cellular dipentaenone by Streptomyces coelicolor cytochrome P450 154A1 without oxidation/reduction.

Cheng Q, Lamb DC, Kelly SL, Lei L, Guengerich FP
J Am Chem Soc. 2010 132 (43): 15173-5

PMID: 20979426 · PMCID: PMC3118511 · DOI:10.1021/ja107801v

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.

MeSH Terms (6)

Chromatography, High Pressure Liquid Cyclization Cytochrome P-450 Enzyme System Oxidation-Reduction Pentanones Streptomyces coelicolor

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