This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Isopropylmalate dehydrogenase
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | {{STRUCTURE_2ayq| PDB=2ayq | SIZE=400| SCENE= |right|CAPTION=Isopropylmalate dehydrogenase dimer [[2ayq]] }} | ||
| - | < | + | <StructureSection load='3vl2' size='350' side='right' caption='Human α-defensin 1 (PDB entry [[2pm4]])' scene=''> |
| - | + | == Function == | |
| - | + | '''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>. | |
| - | + | ||
| - | + | == 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== | ||
| Line 56: | Line 54: | ||
**[[3fig]] - MtIMDH (mutant) + Zn | **[[3fig]] - MtIMDH (mutant) + Zn | ||
}} | }} | ||
| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 09:32, 3 April 2016
| |||||||||||
