Author(s): Sara Martignon, Franca Rossi and Menico Rizzi
Page: [822 - 827] Pages: 6
* (Excluding Mailing and Handling)
3-isopropylmalate dehydrogenase (3IPMDH) is the third enzyme in leucine biosynthesis and a promising target for the development of broad-spectrum antibacterial agents. We report here the expression, purification and biochemical characterisation of Haemophilus influenzae 3-isopropylmalate dehydrogenase. The observed enzyme inhibition by the reaction product NADH could represent a regulatory mechanism for 3IPMDH.
Keywords: Haemophilus influenzae, 3-isopropylmalate dehydrogenase, recombinant enzyme, leucine biosynthesis, antibacterial target, product inhibition
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