Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 2023-2036 |
| Seitenumfang | 14 |
| Fachzeitschrift | Journal of the Chemical Society, Perkin Transactions 1 |
| Ausgabenummer | 13 |
| Publikationsstatus | Veröffentlicht - 1 Dez. 2000 |
| Extern publiziert | Ja |
Abstract
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.
ASJC Scopus Sachgebiete
- Chemie (insg.)
- Allgemeine Chemie
Zitieren
- Standard
- Harvard
- Apa
- Vancouver
- BibTex
- RIS
in: Journal of the Chemical Society, Perkin Transactions 1, Nr. 13, 01.12.2000, S. 2023-2036.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Synthesis and in vitro enzyme activity of peptide derivatives of bacterial cell wall biosynthesis inhibitors
AU - Cox, Russell J.
AU - Jenkins, Helen
AU - Schouten, James A.
AU - Stentiford, Rosie A.
AU - Wareing, Katrina J.
PY - 2000/12/1
Y1 - 2000/12/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0034617319&partnerID=8YFLogxK
U2 - 10.1039/b002701o
DO - 10.1039/b002701o
M3 - Article
AN - SCOPUS:0034617319
SP - 2023
EP - 2036
JO - Journal of the Chemical Society, Perkin Transactions 1
JF - Journal of the Chemical Society, Perkin Transactions 1
SN - 1470-4358
IS - 13
ER -