Isopropylmalate dehydrogenase

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<StructureSection load='3vl2' size='350' side='right' caption='Human α-defensin 1 (PDB entry [[2pm4]])' scene=''>
<StructureSection load='3vl2' size='350' side='right' caption='Human α-defensin 1 (PDB entry [[2pm4]])' scene=''>
== Function ==
== 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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'''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 ==
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**[[3vmk]] - IMDH + 3IPM + Mg – ''Shewanella bethica''
**[[3vmk]] - IMDH + 3IPM + Mg – ''Shewanella bethica''
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*2-isopropylmalate dehydrogenase
 
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**[[3fig]] - MtIMDH (mutant) + Zn
 
}}
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:44, 3 April 2016

Human α-defensin 1 (PDB entry 2pm4)

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3D structures of isopropylmalate dehydrogenase

Updated on 03-April-2016

References

  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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