Isopropylmalate dehydrogenase

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Function

3-Isopropylmalate dehydrogenase (IMDH) catalyzes the oxidative decarboxylation of 3-isopropylmalate (3IPM) to 2-oxo-4-methylvalerate. This reaction is a step in the biosynthesis of leucine in bacteria and fungi. IMDH uses NAD as a cofactor. IMDH is a bifunctional enzyme that catalyzes dehydrogenation and decarboxylation in the presence of NAD and a divalent cation[1].

Structural highlights

Human α-defensin 1 (PDB entry 2pm4)

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3D structures of isopropylmalate dehydrogenase3D structures of isopropylmalate dehydrogenase

Updated on 03-April-2016

ReferencesReferences

  1. Martignon S, Rossi F, Rizzi M. Expression, purification and characterisation of Haemophilus influenzae 3-isopropylmalate dehydrogenase (LeuB). Protein Pept Lett. 2007;14(8):822-7. PMID:17979826

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Michal Harel, Alexander Berchansky, Joel L. Sussman