# Cytochrome P450-catalyzed allylic oxidation of pentalenene to 1-deoxypentalenic acid in pentalenolactone biosynthesis

## TL;DR

Scientists discovered how a specific antibiotic compound is formed using a P450 enzyme and redox proteins in a bacterial species.

## Contribution

The study identifies the P450 enzyme and redox proteins responsible for a missing step in pentalenolactone biosynthesis.

## Key findings

- Cytochrome P450 pentalenene oxygenase catalyzes the oxidation of pentalenene to 1-deoxypentalenic acid.
- Ferredoxin XNR_5179 and ferredoxin reductase XNR_4478 support the activity of pentalenene oxygenase.
- The identified pathway fills a gap in the biosynthesis of pentalenolactone.

## Abstract

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.

Image, graphical abstract