title: Peptide inhibitors of N-succinyl diaminopimelic acid aminotransferase (DAP-AT): a novel class of antimicrobial compounds.
abstract: Dipeptide substrates of N-Succinyl Diaminopimelic Acid Aminotransferase (DAP-AT) were converted to hydrazines by treatment with hydrazine and cyanoborohydride. These compounds were tested in vitro as inhibitors of DAP-AT from E. coli and in vivo as antibiotics. The hydrazino-dipeptides showed potent slow binding slow binding inhibition of DAP-AT as well as antimicrobial activity.
authors.affiliation: University of Bristol, School of Chemistry, UK. r.j.cox@bris.ac.uk
authors.forename: R J
authors.initials: RJ
authors.lastname: Cox
authors.forename: J A
authors.initials: JA
authors.lastname: Schouten
authors.forename: R A
authors.initials: RA
authors.lastname: Stentiford
authors.forename: K J
authors.initials: KJ
authors.lastname: Wareing
mesh_terms: D000900:Anti-Bacterial Agents / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D004151:Dipeptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D005969:Glutamate Dehydrogenase / Q000037:antagonists & inhibitors; D006834:Hydrazines / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D007202:Indicators and Reagents; D007700:Kinetics; D015394:Molecular Structure; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D051277:Succinyldiaminopimelate Transaminase; D000637:Transaminases / Q000037:antagonists & inhibitors*
chemical_list: D000900:Anti-Bacterial Agents; D004151:Dipeptides; D004791:Enzyme Inhibitors; D006834:Hydrazines; D007202:Indicators and Reagents; D005969:Glutamate Dehydrogenase; D000637:Transaminases; D051277:Succinyldiaminopimelate Transaminase