期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 132, 期 43, 页码 15173-15175出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja107801v
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资金
- U.S. Public Health Service [R01 GM069970, P30 ES000267]
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 Paterno-Buchi-like product, without oxidation/reduction.
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