Delta-amino group hydroxylation of L-ornithine during coelichelin biosynthesis

Org Biomol Chem. 2008 May 21;6(10):1843-8. doi: 10.1039/b801016a. Epub 2008 Apr 4.

Abstract

The nonribosomally produced hydroxamate siderophore coelichelin from Streptomyces coelicolor contains the nonproteinogenic amino acids N(5)-hydroxyornithine and N(5)-hydroxyformylornithine that are important for iron assembly. The hydroxylation of the delta-amino group of L-ornithine is catalyzed by the flavin-dependent monooxygenase CchB. During the redox reaction nicotinamide adenine dinucleotide phosphate (NADPH) and molecular oxygen are consumed and flavin adenine dinucleotide (FAD) is needed as a cofactor. During this work the monooxygenase was biochemically characterized and it could be shown that the hydroxylation of l-ornithine is most likely the first step in the biosynthesis of the siderophore coelichelin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amination
  • Chromatography, High Pressure Liquid
  • Hydrogen Peroxide / chemistry
  • Hydrogen-Ion Concentration
  • Hydroxylation
  • Kinetics
  • Mass Spectrometry
  • Molecular Structure
  • Oligopeptides / biosynthesis*
  • Oligopeptides / chemistry*
  • Ornithine / chemistry*
  • Oxygenases / isolation & purification
  • Oxygenases / metabolism
  • Substrate Specificity

Substances

  • Oligopeptides
  • coelichelin
  • Hydrogen Peroxide
  • Ornithine
  • Oxygenases
  • dimethylaniline monooxygenase (N-oxide forming)