EC 1.1.1.42 - Isocitrate dehydrogenase (NADP+)

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IntEnz Enzyme Nomenclature
EC 1.1.1.42

Names

Accepted name:
isocitrate dehydrogenase (NADP+)
Other names:
NADP isocitric dehydrogenase
NADP-dependent isocitrate dehydrogenase
NADP-dependent isocitric dehydrogenase
NADP-linked isocitrate dehydrogenase
NADP-specific isocitrate dehydrogenase
NADP+-linked isocitrate dehydrogenase
isocitrate (NADP) dehydrogenase
isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase
isocitrate dehydrogenase (NADP)
isocitrate dehydrogenase (NADP-dependent)
oxalosuccinate decarboxylase
oxalsuccinic decarboxylase
IDH [ambiguous]
triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase
dual-cofactor-specific isocitrate dehydrogenase
NADP+-ICDH
NADP+-IDH
IDP
IDP1
IDP2
IDP3
Systematic name:
isocitrate:NADP+ oxidoreductase (decarboxylating)

Reaction

Cofactor

Comments:

Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+), oxalosuccinate can 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 [6]. The enzyme from some species can also use NAD+ but much more slowly [6,7].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00389
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004450
CAS Registry Number: 9028-48-2
UniProtKB/Swiss-Prot: (69) [show] [UniProt]

References

  1. Agosin, M.U. and Weinbach, E.C.
    Partial purification and characterization of the isocitric dehydrogenase from Trypanosoma cruzi.
    Biochim. Biophys. Acta 21: 117-126 (1956). [PMID: 13363868]
  2. Moyle, J. and Dixon, M.
    Purification of the isocitrate enzyme (triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase).
    Biochem. J. 63: 548-552 (1956). [PMID: 13355848]
  3. Plaut, G.W.E.
    Isocitrate dehydrogenases.
    In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.) The Enzymes, 2nd ed. vol. 7, Academic Press, New York, 1963, 105-126
  4. Siebert, G., Dubuc, J., Warner, R.C. and Plaut, G.W.E.
    The preparation of isocitrate dehydrogenase from mammalian heart.
    J. Biol. Chem. 226: 965-975 (1957). [PMID: 13438885]
  5. Vickery, H.B.
    A suggested new nomenclature for the isomers of isocitric acid.
    J. Biol. Chem. 237: 1739-1741 (1962). [PMID: 13925783]
  6. Camacho, M.L., Brown, R.A., Bonete, M.-J., Danson, M.J. and Hough, D.W.
    Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus solfataricus: enzyme purification, characterisation and N-terminal sequence.
    FEMS Microbiol. Lett. 134: 85-90 (1996). [PMID: 8593959]
  7. Steen, I.H., Lien, T. and Birkeland, N.-K.
    Biochemical and phylogenetic characterization of isocitrate dehydrogenase from a hyperthermophilic archaeon, Archaeoglobus fulgidus.
    Arch. Microbiol. 168: 412-420 (1998). [PMID: 9325430]
  8. Koh, H.-J., Lee, S.-M., Son, B.-G., Lee, S.-H., Ryoo, Z.Y., Chang, K.-T., Park, J.-W., Park, D.-C., Song, B.J., Veech, R.L., Song, H. and Huh, T.-L.
    Cytosolic NADP+-dependent isocitrate dehydrogenase plays a key role in lipid metabolism.
    J. Biol. Chem. 279: 39968-39974 (2004). [PMID: 15254034]
  9. Ceccarelli, C., Grodsky, N.B., Ariyaratne, N., Colman, R.F. and Bahnson, B.J.
    Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism.
    J. Biol. Chem. 277: 43454-43462 (2002). [PMID: 12207025]

[EC 1.1.1.42 created 1961, modified 2005]