Involvement of glutamate mutase in the biosynthesis of the unique starter unit of the macrolactam polyketide antibiotic vicenistatin

J Antibiot (Tokyo). 2005 Jul;58(7):468-72. doi: 10.1038/ja.2005.62.

Abstract

The macrolactam antibiotic vicenistatin, produced in Streptomyces halstedii HC34, is biosynthesized by the polyketide pathway, using a unique 3-methylaspartate-derived molecule as starter unit. The vinI gene in the vicenistatin biosynthetic gene cluster encoding glutamate mutase, which rearranges glutamate to 3-methylaspartate, was disrupted. The vinI disruption completely abolished the production of vicenistatin, while the disruptant recovered the production of vicenistatin when 3-methylaspartate was added to the culture. These results indicate that vinI is essential for the 3-methylaspartate formation in the vicenistatin biosynthesis. Furthermore, the mutant accumulated new vicenistatin derivatives (desmethylvicenistatins), which lacked a methyl group in the starter unit. The desmethylvicenistatins were shown by feeding experiments to be derived from aspartate instead of 3-methylaspartate as the starter unit. These results indicate that the vicenistatin polyketide synthase can accept alternative starter units toward the production of novel polyketides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aminoglycosides / biosynthesis*
  • Aminoglycosides / chemistry
  • Aminoglycosides / genetics
  • Anti-Bacterial Agents / biosynthesis*
  • Anti-Bacterial Agents / chemistry
  • Intramolecular Transferases / physiology*
  • Lactams / chemistry
  • Macrolides / chemistry
  • Molecular Structure
  • Polyketide Synthases / physiology*
  • Streptomyces / enzymology*
  • Streptomyces / metabolism

Substances

  • Aminoglycosides
  • Anti-Bacterial Agents
  • Lactams
  • Macrolides
  • vicenistatin
  • Polyketide Synthases
  • Intramolecular Transferases
  • methylaspartate mutase