Isocitrate dehydrogenase (NAD+)
| Isocitrate dehydrogenase (NAD+) | |||||||||
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isocitrate dehydrogenase dimer, Human | |||||||||
| Identifiers | |||||||||
| EC number | 1.1.1.41 | ||||||||
| CAS number | 9001-58-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Isocitrate dehydrogenase (NAD+) (EC 1.1.1.41, isocitric dehydrogenase, beta-ketoglutaric-isocitric carboxylase, isocitric acid dehydrogenase, NAD dependent isocitrate dehydrogenase, NAD isocitrate dehydrogenase, NAD-linked isocitrate dehydrogenase, NAD-specific isocitrate dehydrogenase, NAD isocitric dehydrogenase, isocitrate dehydrogenase (NAD), IDH (ambiguous), nicotinamide adenine dinucleotide isocitrate dehydrogenase) is an enzyme with systematic name isocitrate:NAD+ oxidoreductase (decarboxylating).[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction
- isocitrate + NAD+ 2-oxoglutarate + CO2 + NADH
Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.42, isocitrate dehydrogenase (NADP+), oxalosuccinate cannot be used as a substrate. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD+-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP+-linked enzyme that is found in both mitochondria and cytoplasm. The enzyme from some species can also use NADP+ but much more slowly.[8][9]
References
- ↑ Hathaway, J.A.; Atkinson, D.E. (1963). "The effect of adenylic acid on yeast nicotinamide adenine dinucleotide isocitrate dehydrogenase, a possible metabolic control mechanism". J. Biol. Chem. 238: 2875–2881. PMID 14063317.
- ↑ Kornberg, A.; Pricer, W.E. (1951). "Di- and triphosphopyridine nucleotide isocitric dehydrogenase in yeast". J. Biol. Chem. 189: 123–136. PMID 14832224.
- ↑ Plaut, G.W.E.; Lardy, H.; Myrbäck, K. (1963). "Isocitrate dehydrogenases". In Boyer, P.D. The Enzymes. 7 (2nd ed.). New York: Academic Press. pp. 105–126.
- ↑ Plaut, G.W.E.; Sung, S.-C. (1954). "Diphosphopyridine nucleotide isocitric dehydrogenase from animal tissues". J. Biol. Chem. 207: 305–314. PMID 13152105.
- ↑ Ramakrishnan, C.V.; Martin, S.M. (1955). "Isocitric dehydrogenase in Aspergillus niger". Arch. Biochem. Biophys. 55: 403–407. doi:10.1016/0003-9861(55)90421-5.
- ↑ Vickery, H.B. (1962). "A suggested new nomenclature for the isomers of isocitric acid". J. Biol. Chem. 237: 1739–1741. PMID 13925783.
- ↑ Camacho, M.L.; Brown, R.A.; Bonete, M.J.; Danson, M.J.; Hough, D.W. (1995). "Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus solfataricus: enzyme purification, characterisation and N-terminal sequence". FEMS Microbiol. Lett. 134: 85–90. doi:10.1016/0378-1097(95)00388-l. PMID 8593959.
- ↑ Kim, Y.O.; Koh, H.J.; Kim, S.H.; Jo, S.H.; Huh, J.W.; Jeong, K.S.; Lee, I.J.; Song, B.J.; Huh, T.L. (1999). "Identification and functional characterization of a novel, tissue-specific NAD+-dependent isocitrate dehydrogenase β subunit isoform". J. Biol. Chem. 274: 36866–36875. doi:10.1074/jbc.274.52.36866. PMID 10601238.
- ↑ Inoue, H.; Tamura, T.; Ehara, N.; Nishito, A.; Nakayama, Y.; Maekawa, M.; Imada, K.; Tanaka, H.; Inagaki, K. (2002). "Biochemical and molecular characterization of the NAD+-dependent isocitrate dehydrogenase from the chemolithotroph Acidithiobacillus thiooxidans". FEMS Microbiol. Lett. 214: 127–132. doi:10.1016/s0378-1097(02)00857-1. PMID 12204383.
External links
- Isocitrate dehydrogenase (NAD ) at the US National Library of Medicine Medical Subject Headings (MeSH)