Ontology highlight
ABSTRACT:
SUBMITTER: Lowther WT
PROVIDER: S-EPMC22800 | biostudies-literature | 1998 Oct
REPOSITORIES: biostudies-literature
Lowther W T WT McMillen D A DA Orville A M AM Matthews B W BW
Proceedings of the National Academy of Sciences of the United States of America 19981001 21
Methionine aminopeptidase (MetAP) exists in two forms (type I and type II), both of which remove the N-terminal methionine from proteins. It previously has been shown that the type II enzyme is the molecular target of fumagillin and ovalicin, two epoxide-containing natural products that inhibit angiogenesis and suppress tumor growth. By using mass spectrometry, N-terminal sequence analysis, and electronic absorption spectroscopy we show that fumagillin and ovalicin covalently modify a conserved ...[more]