Mutational biosynthesis of novel rapamycins by a strain of Streptomyces hygroscopicus NRRL 5491 disrupted in rapL, encoding a putative lysine cyclodeaminase

J Bacteriol. 1998 Feb;180(4):809-14. doi: 10.1128/JB.180.4.809-814.1998.

Abstract

The gene rapL lies within the region of the Streptomyces hygroscopicus chromosome which contains the biosynthetic gene cluster for the immunosuppressant rapamycin. Introduction of a frameshift mutation into rapL by phiC31 phage-mediated gene replacement gave rise to a mutant which did not produce significant amounts of rapamycin. Growth of this rapL mutant on media containing added L-pipecolate restored wild-type levels of rapamycin production, consistent with a proposal that rapL encodes a specific L-lysine cyclodeaminase important for the production of the L-pipecolate precursor. In the presence of added proline derivatives, rapL mutants synthesized novel rapamycin analogs, indicating a relaxed substrate specificity for the enzyme catalyzing pipecolate incorporation into the macrocycle.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ammonia-Lyases / genetics*
  • Cell Cycle / drug effects
  • Frameshift Mutation*
  • Gas Chromatography-Mass Spectrometry
  • Genes, Bacterial
  • Hydroxyproline / analogs & derivatives
  • Immunosuppressive Agents / chemistry
  • Immunosuppressive Agents / metabolism*
  • Immunosuppressive Agents / pharmacology
  • Magnetic Resonance Spectroscopy
  • Multigene Family
  • Pipecolic Acids / metabolism
  • Polyenes / chemistry
  • Polyenes / metabolism*
  • Polyenes / pharmacology
  • Sirolimus
  • Streptomyces / enzymology
  • Streptomyces / genetics*

Substances

  • Immunosuppressive Agents
  • Pipecolic Acids
  • Polyenes
  • Ammonia-Lyases
  • lysine cyclodeaminase
  • Hydroxyproline
  • Sirolimus