208645-70-9Relevant academic research and scientific papers
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.
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 (2007/10/03)
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.
