104840-92-8Relevant articles and documents
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.
