Isopropylmalate dehydrogenase
From Proteopedia
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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== | ||
Revision as of 10:09, 3 April 2016
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3D structures of isopropylmalate dehydrogenase
Updated on 03-April-2016
References
- ↑ 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
- ↑ Pallo A, Olah J, Graczer E, Merli A, Zavodszky P, Weiss MS, Vas M. Structural and energetic basis of isopropylmalate dehydrogenase enzyme catalysis. FEBS J. 2014 Sep 11. doi: 10.1111/febs.13044. PMID:25211160 doi:http://dx.doi.org/10.1111/febs.13044
