Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 1029-1035 |
| Seitenumfang | 7 |
| Fachzeitschrift | Journal of the Chemical Society. Perkin Transactions 1 |
| Jahrgang | 8 |
| Publikationsstatus | Veröffentlicht - 1 Jan. 2002 |
| Extern publiziert | Ja |
Abstract
The synthesis of a novel epoxide inhibitor 6 of meso-DAP epimerase was achieved. A new and convenient assay for meso-DAP epimerase was devised which is a considerable improvement on previously reported assay methods. This assay was used to determine the inhibitory properties of 6. The epoxide 6 shows limited competitive inhibition vs. meso-DAP epimerase, but clear time dependent inhibition indicative of the expected covalent attachment at the active site. Epoxide 6, although an effective inhibitor of meso-DAP epimerase, was unstable at pH 7.3 in aqueous buffer, being hydrolysed to the corresponding diol.
ASJC Scopus Sachgebiete
- Chemie (insg.)
- Allgemeine Chemie
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in: Journal of the Chemical Society. Perkin Transactions 1, Jahrgang 8, 01.01.2002, S. 1029-1035.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Synthesis and in vitro enzyme activity of an oxa analogue of azi-DAP
AU - Cox, Russell J.
AU - Durston, Jeremy
AU - Roper, David I.
PY - 2002/1/1
Y1 - 2002/1/1
N2 - The synthesis of a novel epoxide inhibitor 6 of meso-DAP epimerase was achieved. A new and convenient assay for meso-DAP epimerase was devised which is a considerable improvement on previously reported assay methods. This assay was used to determine the inhibitory properties of 6. The epoxide 6 shows limited competitive inhibition vs. meso-DAP epimerase, but clear time dependent inhibition indicative of the expected covalent attachment at the active site. Epoxide 6, although an effective inhibitor of meso-DAP epimerase, was unstable at pH 7.3 in aqueous buffer, being hydrolysed to the corresponding diol.
AB - The synthesis of a novel epoxide inhibitor 6 of meso-DAP epimerase was achieved. A new and convenient assay for meso-DAP epimerase was devised which is a considerable improvement on previously reported assay methods. This assay was used to determine the inhibitory properties of 6. The epoxide 6 shows limited competitive inhibition vs. meso-DAP epimerase, but clear time dependent inhibition indicative of the expected covalent attachment at the active site. Epoxide 6, although an effective inhibitor of meso-DAP epimerase, was unstable at pH 7.3 in aqueous buffer, being hydrolysed to the corresponding diol.
UR - http://www.scopus.com/inward/record.url?scp=0036009994&partnerID=8YFLogxK
U2 - 10.1039/b201727j
DO - 10.1039/b201727j
M3 - Article
AN - SCOPUS:0036009994
VL - 8
SP - 1029
EP - 1035
JO - Journal of the Chemical Society. Perkin Transactions 1
JF - Journal of the Chemical Society. Perkin Transactions 1
SN - 1472-7781
ER -