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

Academic Article
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Overview

authors

  • Schultz, A. W.
  • Lewis, C. A.
  • Luzung, M. R.
  • Baran, Phil
  • Moore, B. S.

publication date

  • March 2010

journal

  • Journal of Natural Products  Journal

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.

subject areas

  • Actinobacteria
  • Bioengineering
  • Dimethylallyltranstransferase
  • Marine Biology
  • Molecular Structure
  • Peptide Synthases
  • Peptides, Cyclic
  • Tryptophan
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Identity

PubMed Central ID

  • PMC2846197

International Standard Serial Number (ISSN)

  • 0163-3864

Digital Object Identifier (DOI)

  • 10.1021/np9006876

PubMed ID

  • 20055491
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Additional Document Info

start page

  • 373

end page

  • 377

volume

  • 73

issue

  • 3

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