Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 874-886 |
| Seitenumfang | 13 |
| Fachzeitschrift | CHEMBIOCHEM |
| Jahrgang | 3 |
| Ausgabenummer | 9 |
| Publikationsstatus | Veröffentlicht - 1 Dez. 2002 |
| Extern publiziert | Ja |
Abstract
The synthesis of methylene phosphonate, difluoromethylene phosphonate and phosphoramidate analogues of aspartyl phosphate, together with reduced analogues, is described. These compounds were shown to be effective inhibitors of aspartatesemialdehyde dehydrogenase (ASA-DH) from Escherichia coli. However, despite the structural similarity of the compounds, different patterns of inhibition were observed, indicative of two phases of recognition and binding. Correlation between measured inhibition constants with pKa values supports the theory that binding at the phosphate binding site is optimised for singly ionised phosphate analogues.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Molekularmedizin
- Biochemie, Genetik und Molekularbiologie (insg.)
- Molekularbiologie
- Chemie (insg.)
- Organische Chemie
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in: CHEMBIOCHEM, Jahrgang 3, Nr. 9, 01.12.2002, S. 874-886.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Aspartyl phosphonates and phosphoramidates
T2 - The first synthetic inhibitors of bacterial aspartate-semialdehyde dehydrogenase
AU - Cox, Russell J.
AU - Gibson, Jennifer S.
AU - Belén, María
AU - Martín, Mayo
PY - 2002/12/1
Y1 - 2002/12/1
N2 - The synthesis of methylene phosphonate, difluoromethylene phosphonate and phosphoramidate analogues of aspartyl phosphate, together with reduced analogues, is described. These compounds were shown to be effective inhibitors of aspartatesemialdehyde dehydrogenase (ASA-DH) from Escherichia coli. However, despite the structural similarity of the compounds, different patterns of inhibition were observed, indicative of two phases of recognition and binding. Correlation between measured inhibition constants with pKa values supports the theory that binding at the phosphate binding site is optimised for singly ionised phosphate analogues.
AB - The synthesis of methylene phosphonate, difluoromethylene phosphonate and phosphoramidate analogues of aspartyl phosphate, together with reduced analogues, is described. These compounds were shown to be effective inhibitors of aspartatesemialdehyde dehydrogenase (ASA-DH) from Escherichia coli. However, despite the structural similarity of the compounds, different patterns of inhibition were observed, indicative of two phases of recognition and binding. Correlation between measured inhibition constants with pKa values supports the theory that binding at the phosphate binding site is optimised for singly ionised phosphate analogues.
KW - Antibiotics
KW - Dehydrogenases
KW - Inhibitors
KW - Phosphonates
KW - Phosphoramidates
UR - http://www.scopus.com/inward/record.url?scp=0036902135&partnerID=8YFLogxK
U2 - 10.1002/1439-7633(20020902)3:9<874::AID-CBIC874>3.0.CO;2-V
DO - 10.1002/1439-7633(20020902)3:9<874::AID-CBIC874>3.0.CO;2-V
M3 - Article
C2 - 12210989
AN - SCOPUS:0036902135
VL - 3
SP - 874
EP - 886
JO - CHEMBIOCHEM
JF - CHEMBIOCHEM
SN - 1439-4227
IS - 9
ER -