3-Isopropylmalate dehydrogenase
| 3-Isopropylmalate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.85 | ||||||||
| CAS no. | 9030-97-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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
References
- ^ 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.
- ^ 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.
- ^ Parsons SJ, Burns RO (February 1969). "Purification and Properties of β-Isopropylmalate Dehydrogenase". J. Biol. Chem. 244 (3): 996–1003. PMID 4889950.
- ^ 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.
