3-Isopropylmalate dehydrogenase

3-Isopropylmalate dehydrogenase (EC 1.1.1.85) is an enzyme that is a part of the isopropylmalate dehydrogenase family, which catalyzes the chemical reactions:[1][2][3][4]

(2R,3S)-3-isopropylmalate + NAD+ 4-methyl-2-oxopentanoate + CO2 + NADH
(2R,3S)-3-isopropylmalate + NAD+ (2S)-2-isopropyl-3-oxosuccinate + H+ + NADH
(2S)-2-isopropyl-3-oxosuccinate + H+ 4-methyl-2-oxopentanoate + CO2
3-Isopropylmalate dehydrogenase
Identifiers
EC no.1.1.1.85
CAS no.9030-97-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

References
  1. Burns RO, Umbarger HE, Gross SR (1963). "The biosynthesis of leucine. III. The conversion of α-hydroxy-β-carboxyisocaproate to α-ketoisocaproate". Biochemistry. 2 (5): 1053–8. doi:10.1021/bi00905a024. PMID 14087358.
  2. Calvo JM, Stevens CM, Kalyanpur MG, Umbarger HE (December 1964). "The Absolute Configuration of α-carboxyisocaproic Acid (3-Isopropylmalic Acid), an Intermediate in Leucine Biosynthesis". Biochemistry. 3 (12): 2024–7. doi:10.1021/bi00900a043. PMID 14269331.
  3. Parsons SJ, Burns RO (February 1969). "Purification and Properties of β-Isopropylmalate Dehydrogenase". J. Biol. Chem. 244 (3): 996–1003. PMID 4889950.
  4. Németh A, Svingor A, Pócsik M, Dobó J, Magyar C, Szilágyi A, Gál P, Závodszky P (February 2000). "Mirror image mutations reveal the significance of an intersubunit ion cluster in the stability of 3-isopropylmalate dehydrogenase". FEBS Lett. 468 (1): 48–52. doi:10.1016/S0014-5793(00)01190-X. PMID 10683439. S2CID 44544921.


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