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Nat Chem Biol. 2017 Nov;13(11):1155-1157. doi: 10.1038/nchembio.2471. Epub 2017 Sep 11.

Oxidative cyclization of prodigiosin by an alkylglycerol monooxygenase-like enzyme.

Author information

1
Department of Chemistry, University of California, Berkeley, California, USA.
2
Department of Chemical and Biomolecular Engineering, University of California, Berkeley, California, USA.
3
DOE Joint BioEnergy Institute, Emeryville, California, USA.
4
Biological Systems and Engineering Division, Lawrence Berkeley National Lab, Berkeley, California, USA.
5
DOE Joint Genome Institute, Walnut Creek, California, USA.
6
Department of Bioengineering and California Institute for Quantitative Biosciences, University of California, Berkeley, California, USA.
7
Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Hørsholm, Denmark.

Abstract

Prodiginines, which are tripyrrole alkaloids displaying a wide array of bioactivities, occur as linear and cyclic congeners. Identification of an unclustered biosynthetic gene led to the discovery of the enzyme responsible for catalyzing the regiospecific C-H activation and cyclization of prodigiosin to cycloprodigiosin in Pseudoalteromonas rubra. This enzyme is related to alkylglycerol monooxygenase and unrelated to RedG, the Rieske oxygenase that produces cyclized prodiginines in Streptomyces, implying convergent evolution.

PMID:
28892091
PMCID:
PMC5677514
DOI:
10.1038/nchembio.2471
[Indexed for MEDLINE]
Free PMC Article

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