208645-73-2Relevant academic research and scientific papers
Peptide inhibitors of N-succinyl diaminopimelic acid aminotransferase (DAP-AT): A novel class of antimicrobial compounds
Cox, Russell J.,Schouten, James A.,Stentiford, Rosie A.,Wareing, Katrina J.
, p. 945 - 950 (1998)
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 hydrazinodipeptides showed potent slow binding inhibition of DAP-AT as well as antimicrobial activity.
Synthesis and in vitro enzyme activity of peptide derivatives of bacterial cell wall biosynthesis inhibitors
Cox, Russell J.,Jenkins, Helen,Schouten, James A.,Stentiford, Rosie A.,Wareing, Katrina J.
, p. 2023 - 2036 (2007/10/03)
The enzyme diaminopimelate aminotransferase (DAP-AT) is a good potential target for the design of novel antibacterial agents. We have synthesised a series of peptide hydrazines based on the structure of the natural substrate of DAP-AT. These compounds show varied inhibition properties in vitro vs. DAP-AT from E. coli as well as moderate antimicrobial activity vs. E. coli. Examination of the kinetics of inhibition reveals that hydrazine, as well as the substituted hydrazino-peptides, shows two-phase slow-binding inhibition. Possible mechanisms for inhibition are discussed. The Royal Society of Chemistry 2000.
