Abstract
A cyclopropane substrate analog 1 was designed as a mechanism-based inhibitor for 3-isopropylmalate dehydrogenase (IPMDH), the rate-determining enzyme responsible for the penultimate step in the biosynthetic pathway of the essential amino acid l-leucine. The synthesis of 1 was pursued in 5 steps from diethyl ( R)-malate. As was deduced from the time-dependent and kinetic analyses, 1 appeared to be a competitive and mechanism-based inhibitor for IPMDH ( Ki = 1.9 mM). Thus, 1 was recognized as a substrate and oxidized by IPMDH. Inhibitory mechanism is suggested to be slowering the decarboxylation step.
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