Biology:Isocitrate dehydrogenase (NAD+)
| Isocitrate dehydrogenase (NAD+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 isocitrate dehydrogenase [NAD] heterodimer, 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+ [math]\displaystyle{ \rightleftharpoons }[/math] 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
- ↑ "The effect of adenylic acid on yeast nicotinamide adenine dinucleotide isocitrate dehydrogenase, a possible metabolic control mechanism". The Journal of Biological Chemistry 238: 2875–81. August 1963. PMID 14063317.
- ↑ "Di- and triphosphopyridine nucleotide isocitric dehydrogenases in yeast". The Journal of Biological Chemistry 189 (1): 123–36. March 1951. PMID 14832224.
- ↑ "Isocitrate dehydrogenases". The Enzymes. 7 (2nd ed.). New York: Academic Press. 1963. pp. 105–126.
- ↑ "Diphosphopyridine nucleotide isocitric dehydrogenase from animal tissues". The Journal of Biological Chemistry 207 (1): 305–14. March 1954. PMID 13152105.
- ↑ "Isocitric dehydrogenase in Aspergillus niger". Arch. Biochem. Biophys. 55: 403–407. 1955. doi:10.1016/0003-9861(55)90421-5.
- ↑ "A suggested new nomenclature for the isomers of isocitric acid". The Journal of Biological Chemistry 237: 1739–41. June 1962. PMID 13925783.
- ↑ "Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus solfataricus: enzyme purification, characterisation and N-terminal sequence". FEMS Microbiology Letters 134 (1): 85–90. December 1995. doi:10.1016/0378-1097(95)00388-l. PMID 8593959.
- ↑ "Identification and functional characterization of a novel, tissue-specific NAD(+)-dependent isocitrate dehydrogenase beta subunit isoform". The Journal of Biological Chemistry 274 (52): 36866–75. December 1999. doi:10.1074/jbc.274.52.36866. PMID 10601238.
- ↑ "Biochemical and molecular characterization of the NAD(+)-dependent isocitrate dehydrogenase from the chemolithotroph Acidithiobacillus thiooxidans". FEMS Microbiology Letters 214 (1): 127–32. August 2002. 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)
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