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