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Irreversible inhibition of dihydrodipicolinate synthase by 4-oxo-heptenedioic acid analogues
Journal article   Peer reviewed

Irreversible inhibition of dihydrodipicolinate synthase by 4-oxo-heptenedioic acid analogues

B.A. Boughton, M.D.W. Griffin, P.A. O’Donnell, R.C.J. Dobson, M.A. Perugini, J.A. Gerrard and C.A. Hutton
Bioorganic & Medicinal Chemistry, Vol.16(23), pp.9975-9983
2008
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Abstract

We report the synthesis of (2E,5E)-4-oxoheptadienedioic acid and (2E)-4-oxoheptenedioic acid and evaluation of both diester and diacid analogues as inhibitors of bacterial dihydrodipicolinate synthase. Enzyme kinetic studies allowed the determination of second-order rate constants of inactivation; and substrate co-incubation studies have shown the inhibitors act at the active-site. Mass spectrometric analyses have further explored the enzyme–inhibitor interaction and determined the sites of enzyme alkylation.

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Collaboration types
Domestic collaboration
International collaboration
Citation topics
3 Agriculture, Environment & Ecology
3.180 Microbial Biotechnology
3.180.1184 Amino Acid Biosynthesis
Web Of Science research areas
Biochemistry & Molecular Biology
Chemistry, Medicinal
Chemistry, Organic
ESI research areas
Chemistry
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