Cytochrome P450-catalyzed allylic oxidation of pentalenene to 1-deoxypentalenic acid in pentalenolactone biosynthesis
Pentalenolactone is a sesquiterpene antibiotic from Streptomyces . Its biosynthetic pathway has been elucidated, except for the oxidation of pentalen-13-al to 1-deoxypentalenic acid. In this study, we show that cytochrome P450 pentalenene oxygenase catalyzed the formation of 1-deoxypentalenic acid. Ferredoxin XNR_5179 and ferredoxin reductase XNR_4478 from S. albus are suitable redox proteins for pentalenene oxygenase. The biosynthetic pathway presented fills a gap in the biosynthetic pathway of pentalenolactone and provides an example of cytochrome P450 enzyme activity being affected by redox proteins.
Authors
- Jiao Xue (ORCID: https://orcid.org/0000-0003-1368-5654)
- Chengde Zhang (ORCID: https://orcid.org/0000-0003-2246-4976)
- Jing Li (ORCID: https://orcid.org/0000-0002-5627-4153)
- Ke Chen (ORCID: https://orcid.org/0000-0003-0433-5580)
- Zixin Deng (ORCID: https://orcid.org/0000-0003-0724-3390)
- Shiwen Wu (ORCID: https://orcid.org/0000-0003-4958-4089)
- Dongqing Zhu
Institutions
- Wuhan University (CN)
- Third Affiliated Hospital of Guangzhou Medical University (CN)
- Guangzhou Medical University (CN)
Publication Details
- Journal
- Engineering Microbiology
- Published
- 2025-04-07
- DOI
- https://doi.org/10.1016/j.engmic.2025.100206
- Primary Topic
- Plant biochemistry and biosynthesis
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Natural Science Foundation of China
- National Key Research and Development Program of China