Isocitrate dehydrogenase (NAD+)

Isocitrate dehydrogenase (NAD+)
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

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+ \rightleftharpoons 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

  1. ↑ Hathaway, J.A. and 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.
  2. ↑ Kornberg, A. and Pricer, W.E. (1951). "Di- and triphosphopyridine nucleotide isocitric dehydrogenase in yeast". J. Biol. Chem. 189: 123–136. PMID 14832224.
  3. ↑ Plaut, G.W.E. (1963). "Isocitrate dehydrogenases". In Boyer, P.D., Lardy, H. and Myrbäck, K. The Enzymes 7 (2nd ed.). New York: Academic Press. pp. 105–126.
  4. ↑ Plaut, G.W.E. and Sung, S.-C. (1954). "Diphosphopyridine nucleotide isocitric dehydrogenase from animal tissues". J. Biol. Chem. 207: 305–314. PMID 13152105.
  5. ↑ Ramakrishnan, C.V. and Martin, S.M. (1955). "Isocitric dehydrogenase in Aspergillus niger". Arch. Biochem. Biophys. 55: 403–407.
  6. ↑ Vickery, H.B. (1962). "A suggested new nomenclature for the isomers of isocitric acid". J. Biol. Chem. 237: 1739–1741. PMID 13925783.
  7. ↑ Camacho, M.L., Brown, R.A., Bonete, M.J., Danson, M.J. and 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. PMID 8593959.
  8. ↑ Kim, Y.O., Koh, H.J., Kim, S.H., Jo, S.H., Huh, J.W., Jeong, K.S., Lee, I.J., Song, B.J. and 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. PMID 10601238.
  9. ↑ Inoue, H., Tamura, T., Ehara, N., Nishito, A., Nakayama, Y., Maekawa, M., Imada, K., Tanaka, H. and Inagaki, K. (2002). "Biochemical and molecular characterization of the NAD+-dependent isocitrate dehydrogenase from the chemolithotroph Acidithiobacillus thiooxidans". FEMS Microbiol. Lett. 214: 127–132. PMID 12204383.

External links

This article is issued from Wikipedia - version of the Monday, April 11, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.