104840-92-8Relevant 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.
N-acetylaspartylglutamic acid and its β-isomer
Piotrovskii, L. B.,Dumpis, M. A.,Poznyakova, L. N.,Aleksandrova, L. N.,Sepetov, N. F.
, p. 96 - 100 (2007/10/02)
The α-isomer is predominantly formed in the synthesis of N-acetylaspartylglutamic acid and its β-isomer upon cleavage of N-acetylaspartic acid anhydride by the diethyl ester of glutamic acid.
