Details
Original language | English |
---|---|
Pages (from-to) | 1710-1711 |
Number of pages | 2 |
Journal | Chemical communications |
Volume | 1 |
Issue number | 18 |
Publication status | Published - 1 Jan 2001 |
Externally published | Yes |
Abstract
The difluoromethylene analogue of aspartyl phosphate 6 has been prepared by the fluoride catalysed coupling of diethyl trimethylsilyldifluoromethyl phosphonate with an appropriate aldehyde followed by Dess-Martin oxidation and deprotection; the deprotected compound inhibited (KI 95 μM) aspartate semi-aldehyde dehydrogenase, a key enzyme involved in bacterial amino acid and peptidoglycan biosynthesis.
ASJC Scopus subject areas
- Chemical Engineering(all)
- Catalysis
- Materials Science(all)
- Electronic, Optical and Magnetic Materials
- Materials Science(all)
- Ceramics and Composites
- Chemistry(all)
- General Chemistry
- Materials Science(all)
- Surfaces, Coatings and Films
- Materials Science(all)
- Metals and Alloys
- Materials Science(all)
- Materials Chemistry
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In: Chemical communications, Vol. 1, No. 18, 01.01.2001, p. 1710-1711.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Difluoromethylene analogues of aspartyl phosphate
T2 - The first synthetic inhibitors of aspartate semi-aldehyde dehydrogenase
AU - Cox, Russell J.
AU - Hadfield, Andrea T.
AU - Mayo-Martín, M. Belén
PY - 2001/1/1
Y1 - 2001/1/1
N2 - The difluoromethylene analogue of aspartyl phosphate 6 has been prepared by the fluoride catalysed coupling of diethyl trimethylsilyldifluoromethyl phosphonate with an appropriate aldehyde followed by Dess-Martin oxidation and deprotection; the deprotected compound inhibited (KI 95 μM) aspartate semi-aldehyde dehydrogenase, a key enzyme involved in bacterial amino acid and peptidoglycan biosynthesis.
AB - The difluoromethylene analogue of aspartyl phosphate 6 has been prepared by the fluoride catalysed coupling of diethyl trimethylsilyldifluoromethyl phosphonate with an appropriate aldehyde followed by Dess-Martin oxidation and deprotection; the deprotected compound inhibited (KI 95 μM) aspartate semi-aldehyde dehydrogenase, a key enzyme involved in bacterial amino acid and peptidoglycan biosynthesis.
UR - http://www.scopus.com/inward/record.url?scp=0035929198&partnerID=8YFLogxK
U2 - 10.1039/b103988c
DO - 10.1039/b103988c
M3 - Article
C2 - 12240277
AN - SCOPUS:0035929198
VL - 1
SP - 1710
EP - 1711
JO - Chemical communications
JF - Chemical communications
SN - 1359-7345
IS - 18
ER -