Isopropylmalate dehydrogenase: Difference between revisions
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<StructureSection load='4f7i' size='350' side='right' caption='3-isopropylmalate dehydrogenase complex with 3-isopropylmalate, | <StructureSection load='4f7i' size='350' side='right' caption='3-isopropylmalate dehydrogenase complex with 3-isopropylmalate, glycerol, NAD, PMSF, Mn+2 and K- ions (PDB entry [[4f7i]])' scene=''> | ||
== Function == | == 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<ref>PMID:17979826</ref>. | '''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<ref>PMID:17979826</ref>. | ||
== Structural highlights == | == Structural highlights == | ||
IMDH active site containing the NAD cofactor is located between 2 subunits and contains the substrate and Mn+2 and K- ions<ref>PMID:25211160</ref>. | |||
</StructureSection> | </StructureSection> | ||
==3D structures of isopropylmalate dehydrogenase== | ==3D structures of isopropylmalate dehydrogenase== | ||