Isopropylmalate dehydrogenase: Difference between revisions

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{{STRUCTURE_2ayq| PDB=2ayq  | SIZE=400| SCENE= |right|CAPTION=Isopropylmalate dehydrogenase dimer [[2ayq]] }}


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<StructureSection load='3vl2' size='350' side='right' caption='Human α-defensin 1 (PDB entry [[2pm4]])' scene=''>
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== Function ==
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'''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:8528769</ref>.
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== Structural highlights ==
'''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.


==3D structures of isopropylmalate dehydrogenase==
==3D structures of isopropylmalate dehydrogenase==
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**[[3fig]] - MtIMDH (mutant) + Zn
**[[3fig]] - MtIMDH (mutant) + Zn
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== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

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Michal Harel, Alexander Berchansky, Joel L. Sussman