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Gene Review

IDP3  -  isocitrate dehydrogenase (NADP(+)) IDP3

Saccharomyces cerevisiae S288c

Synonyms: IDH, IDP, N2870, NADP(+)-specific ICDH, Oxalosuccinate decarboxylase, ...
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Disease relevance of IDP3

  • Both IDH subunits were expressed as recombinant proteins in Escherichia coli, and polyclonal antibodies were raised to each subunit [1].

High impact information on IDP3

  • This is based on the finding of a third NADP-dependent isocitrate dehydrogenase isoenzyme, Idp3p, next to the already known mitochondrial and cytosolic isoenzymes, which turned out to be present in the peroxisomal matrix [2].
  • Our proposal is strongly supported by the observation that peroxisomal Idp3p is essential for growth on the unsaturated fatty acids arachidonic, linoleic and petroselinic acid, which require 2, 4-dienoyl-CoA reductase activity [2].
  • Lysine produced a stronger growth stimulating effect than glutamic acid consistent with an upregulated expression of the IDP3 gene for peroxisomal synthesis of the glutamate precursor alpha-ketoglutarate [3].
  • This loss of viability is not observed following transfer of a DeltaIDP3 strain lacking peroxisomal isocitrate dehydrogenase to medium with docosahexaenoate, a nonpermissive carbon source that requires function of IDP3 for beta-oxidation [4].
  • Human PICD was identified by homology probing the data base of expressed sequence tags with the protein sequence of Saccharomyces cerevisiae Idp3p, a peroxisomal NADP(+)-dependent isocitrate dehydrogenase [5].

Biological context of IDP3

  • Three differentially compartmentalized isozymes of isocitrate dehydrogenase (mitochondrial IDP1, cytosolic IDP2, and peroxisomal IDP3) in the yeast Saccharomyces cerevisiae catalyze the NADP(+)-dependent oxidative decarboxylation of isocitrate to form alpha-ketoglutarate [6].
  • The human PICD cDNA contains a 1242-base pair open reading frame, and its deduced protein sequence is 59% identical to yeast Idp3p [5].
  • In this study, we have focused on another phenotype associated with loss of IDH, an elevated frequency of petite mutations indicating loss of functional mtDNA [7].
  • Using mutant forms of IDH with altered active site residues, a correlation was observed between the high frequency of petite mutations and the loss of catalytic activity [7].

Anatomical context of IDP3

  • The mammalian cytosolic isozyme also functionally substitutes for Idp3p allowing growth on petroselinic acid as a carbon source, suggesting partial localization to peroxisomes and provision of NADPH for beta-oxidation of that fatty acid [8].

Associations of IDP3 with chemical compounds

  • These studies revealed that the IDP isozymes are functionally interchangeable for glutamate synthesis, although mitochondrial localization has a positive impact on this function during fermentative growth [6].

Other interactions of IDP3

  • No new biosynthetic roles were identified for mitochondrial (Idp1p) or peroxisomal (Idp3p) NADP+-specific isocitrate dehydrogenase isozymes [8].

Analytical, diagnostic and therapeutic context of IDP3

  • Genomic Southern blot analysis showed distinct single-copy genes for both IDH subunits [1].


  1. NAD(+)-dependent isocitrate dehydrogenase from Arabidopsis thaliana. Characterization of two closely related subunits. Behal, R.H., Oliver, D.J. Plant Mol. Biol. (1998) [Pubmed]
  2. Peroxisomal beta-oxidation of polyunsaturated fatty acids in Saccharomyces cerevisiae: isocitrate dehydrogenase provides NADPH for reduction of double bonds at even positions. van Roermund, C.W., Hettema, E.H., Kal, A.J., van den Berg, M., Tabak, H.F., Wanders, R.J. EMBO J. (1998) [Pubmed]
  3. Distinct intracellular localization of Gpd1p and Gpd2p, the two yeast isoforms of NAD+-dependent glycerol-3-phosphate dehydrogenase, explains their different contributions to redox-driven glycerol production. Valadi, A., Granath, K., Gustafsson, L., Adler, L. J. Biol. Chem. (2004) [Pubmed]
  4. Dependence of peroxisomal beta-oxidation on cytosolic sources of NADPH. Minard, K.I., McAlister-Henn, L. J. Biol. Chem. (1999) [Pubmed]
  5. The human PICD gene encodes a cytoplasmic and peroxisomal NADP(+)-dependent isocitrate dehydrogenase. Geisbrecht, B.V., Gould, S.J. J. Biol. Chem. (1999) [Pubmed]
  6. Influence of compartmental localization on the function of yeast NADP+-specific isocitrate dehydrogenases. Contreras-Shannon, V., McAlister-Henn, L. Arch. Biochem. Biophys. (2004) [Pubmed]
  7. Multiple cellular consequences of isocitrate dehydrogenase isozyme dysfunction. McCammon, M.T., McAlister-Henn, L. Arch. Biochem. Biophys. (2003) [Pubmed]
  8. Sources of NADPH and expression of mammalian NADP+-specific isocitrate dehydrogenases in Saccharomyces cerevisiae. Minard, K.I., Jennings, G.T., Loftus, T.M., Xuan, D., McAlister-Henn, L. J. Biol. Chem. (1998) [Pubmed]
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