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.
Tomoharu Sano  1 ,  Hiroo Takagi ,  Louise F Morrison ,  James S Metcalf ,  Geoffrey A Codd ,  Kunimitsu Kaya
Affiliations
  • 1. National Institute for Environmental Studies, 16-2 Onogawa, Tsukuba, Ibaraki 305-8506, Japan. [email protected]
PMID: 15721946 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.

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