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Functional characterization of the cyclomarin/cyclomarazine prenyltransferase CymD directs the biosynthesis of unnatural cyclic peptides.

ABSTRACT: In vitro and in vivo characterization of the cyclomarin/cyclomarazine prenyltransferase CymD revealed its ability to prenylate tryptophan prior to incorporation into both cyclic peptides by the nonribosomal peptide synthetase CymA. This knowledge was utilized to bioengineer novel derivatives of these marine bacterial natural products by providing synthetic N-alkyl tryptophans to a prenyltransferase-deficient mutant of Salinispora arenicola CNS-205.

SUBMITTER: Schultz AW

PROVIDER: S-EPMC2846197 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature

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Functional characterization of the cyclomarin/cyclomarazine prenyltransferase CymD directs the biosynthesis of unnatural cyclic peptides.

Schultz Andrew W AW Lewis Chad A CA Luzung Michael R MR Baran Phil S PS Moore Bradley S BS

Journal of natural products 20100301 3

In vitro and in vivo characterization of the cyclomarin/cyclomarazine prenyltransferase CymD revealed its ability to prenylate tryptophan prior to incorporation into both cyclic peptides by the nonribosomal peptide synthetase CymA. This knowledge was utilized to bioengineer novel derivatives of these marine bacterial natural products by providing synthetic N-alkyl tryptophans to a prenyltransferase-deficient mutant of Salinispora arenicola CNS-205. ...[more]

PMID: 20055491

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