Isopropylmalate dehydrogenase

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<StructureSection load='3vl2' size='350' side='right' caption='Human α-defensin 1 (PDB entry 2pm4)' scene=>

FunctionFunction

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 highlightsStructural highlights

3D structures of isopropylmalate dehydrogenase3D structures of isopropylmalate dehydrogenase

Updated on 03-April-2016

ReferencesReferences

  1. White SH, Wimley WC, Selsted ME. Structure, function, and membrane integration of defensins. Curr Opin Struct Biol. 1995 Aug;5(4):521-7. PMID:8528769

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Michal Harel, Alexander Berchansky, Joel L. Sussman