Leucine aminopeptidase M inhibitors, cyanostatin A and B, isolated from cyanobacterial water blooms in Scotland

Phytochemistry. 2005 Mar;66(5):543-8. doi: 10.1016/j.phytochem.2005.01.001.

Abstract

Two leucine aminopeptidase M inhibitors, cyanostatin A and B, were isolated from cyanobacterial water blooms at Loch Rescobie in Scotland, and specifically from a Microcystis species. Both inhibitors were lipopeptides containing 3-amino-2-hydroxydecanoic acid and weak inhibitors of protein phosphatase (PP2A). Both strongly inhibited the activity of leucine aminopeptidase M with IC50 values of 40 and 12 ng/ml, respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anabaena
  • Cyanobacteria / isolation & purification*
  • Enzyme Inhibitors / isolation & purification*
  • Enzyme Inhibitors / pharmacology
  • Kinetics
  • Leucyl Aminopeptidase / antagonists & inhibitors*
  • Microcystis
  • Oligopeptides / isolation & purification
  • Oligopeptides / pharmacology*
  • Water Microbiology*

Substances

  • Enzyme Inhibitors
  • Oligopeptides
  • cyanostatin A
  • cyanostatin B
  • Leucyl Aminopeptidase