Journal
BIOORGANIC & MEDICINAL CHEMISTRY
Volume 20, Issue 7, Pages 2419-2426Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2012.01.045
Keywords
Dihydrodipicolinate synthase; Inhibitor; Slow-binding; Slow-tight binding; Mass spectrometry
Funding
- Defense Threat Reduction Agency [AB07CBT004]
- Royal Society of New Zealand
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Dihydrodipicolinate synthase is a key enzyme in the lysine biosynthesis pathway that catalyzes the condensation of pyruvate and aspartate semi-aldehyde. A series of phenolic ketoacid derivatives that mimic the proposed enzymatic intermediate were designed as potential inhibitors of this enzyme and were synthesized from simple precursors. The ketoacid derivatives were shown to act as slow and slow-tight binding inhibitors. Mass spectrometric experiments provided further evidence to support the proposed model of inhibition, demonstrating either an encounter complex or a condensation product for the slow and slow-tight binding inhibitors, respectively. (C) 2012 Elsevier Ltd. All rights reserved.
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