title: Peptidyl hydroxamic acids as methionine aminopeptidase inhibitors.
abstract: A new class of methionine aminopeptidase (MetAP) inhibitors, which contain an internal hydroxamate (N-acyl-N-alkylhydroxylamine) core as the metal-chelating group, has been designed, synthesized, and tested. The compounds exhibited reversible, competitive inhibition against Escherichia coli MetAP as well as human MetAP-1 and MetAP-2. The most potent inhibitor had a K(i) value of 2.5 microM and >20-fold selectivity toward E. coli MAP.
authors.affiliation: Department of Chemistry and Ohio State Biochemistry Program, The Ohio State University, 100 West 18th Avenue, Columbus, OH 43210, USA.
authors.forename: Xubo
authors.initials: X
authors.lastname: Hu
authors.forename: Jinge
authors.initials: J
authors.lastname: Zhu
authors.forename: Sumant
authors.initials: S
authors.lastname: Srivathsan
authors.forename: Dehua
authors.initials: D
authors.lastname: Pei
mesh_terms: D000626:Aminopeptidases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism; D006801:Humans; D006877:Hydroxamic Acids / Q000737:chemistry* / Q000494:pharmacology; D063208:Methionyl Aminopeptidases; D011480:Protease Inhibitors / Q000737:chemistry / Q000494:pharmacology*
chemical_list: D029968:Escherichia coli Proteins; D006877:Hydroxamic Acids; D011480:Protease Inhibitors; D000626:Aminopeptidases; D063208:Methionyl Aminopeptidases