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Gene Review

IDP1  -  isocitrate dehydrogenase (NADP(+)) IDP1

Saccharomyces cerevisiae S288c

Synonyms: IDH, IDP, NADP(+)-specific ICDH, Oxalosuccinate decarboxylase, YDL066W
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Disease relevance of IDP1


High impact information on IDP1

  • To compare kinetic properties of homologous isozymes of NADP+-specific isocitrate dehydrogenase, histidine-tagged forms of yeast mitochondrial (IDP1) and cytosolic (IDP2) enzymes were expressed and purified [3].
  • Complementation experiments using a strain lacking IDH demonstrated that overexpression of IDP1 partially compensated for the glutamate auxotrophy associated with loss of IDH [3].
  • A substantial cellular pool of alpha-ketoglutarate is attributed to IDH function during glucose growth, and to both IDP1 and IDH function during growth on glycerol/lactate [3].
  • Using anti-Idp1p antibodies, protein localization to mitochondria and peroxisomes was observed during growth on glucose whereas cytoplasmic and peroxisomal localization was found upon acetate or fatty acid induction [4].
  • No new biosynthetic roles were identified for mitochondrial (Idp1p) or peroxisomal (Idp3p) NADP+-specific isocitrate dehydrogenase isozymes [5].

Biological context of IDP1

  • This is the first phenotype associated with altered Idp1p [6].
  • The 50-base pair DNA fragment was used as a hybridization probe to identify plasmids containing the IDP1 gene in a yeast genomic DNA library [7].
  • The complete nucleotide sequence of the IDP1 coding region was determined and translated into a 412-residue amino acid sequence for the mature protein which is preceded by a putative 16-residue mitochondrial targeting presequence [7].
  • A haploid yeast strain containing a chromosomal disruption of the IDP1 locus was constructed and found to be capable of growth with glucose but not with other carbon sources, suggesting that IDP1 provides a critical function and may be the primary source of NADPH in yeast mitochondria [7].
  • Expression of IDH RNA and protein is low with growth on glucose and is elevated with growth on non-fermentable carbon sources, a pattern of expression similar to that seen for other tricarboxylic acid cycle enzymes [8].

Associations of IDP1 with chemical compounds

  • IDH expression levels were found to be repressed in response to added glutamate during growth on glucose, while IDP1 expression levels remained unchanged [8].
  • Analysis of the IDP1 and IDH disruption mutants for glutamate auxotrophy showed that either enzyme can contribute alpha-ketoglutarate for endogenous glutamate synthesis [8].
  • For mutant strains lacking IDP1, IDP2, and/or the mitochondrial NAD+-specific isocitrate dehydrogenase (IDH), metabolite measurements indicated that major cellular flux is through the IDH-catalyzed reaction in glucose-grown cells and through the IDP2-catalyzed reaction in cells grown with a nonfermentable carbon source (glycerol and lactate) [3].
  • The cytosolic isozyme of NADP-specific isocitrate dehydrogenase (IDP2) was purified from a Saccharomyces cerevisiae mutant containing a chromosomal disruption in the gene encoding the mitochondrial isozyme (IDP1) [9].
  • In addition, a disruption mutant lacking IDH activity exhibits reduced growth rates on non-fermentable carbon sources, and mitochondria isolated from this mutant are incapable of respiration with added citrate [8].

Other interactions of IDP1

  • Loss of Idp1p (the mitochondrial NADP+-dependent enzyme) and Idp2p contributes to the loss of functional mtDNA, but only in an IDH dysfunctional background [6].

Analytical, diagnostic and therapeutic context of IDP1

  • A 20-residue amino-terminal sequence was obtained for IDP1, and degenerate oligonucleotides were used to synthesize a 50-base pair polymerase chain reaction product corresponding to the coding region for a portion of the amino terminus [7].
  • Immunoblotting using antibody raised against S. cerevisiae Idp1p detected two polypeptides consistent with these predictions [4].
  • Genomic DNA Southern-blot analysis indicates that the IDH alpha gene is not closely related to that of the other IDH isoenzymes, and IDH alpha appears to be encoded by a single gene [1].


  1. Characterization of a cDNA clone for human NAD(+)-specific isocitrate dehydrogenase alpha-subunit and structural comparison with its isoenzymes from different species. Kim, Y.O., Oh, I.U., Park, H.S., Jeng, J., Song, B.J., Huh, T.L. Biochem. J. (1995) [Pubmed]
  2. NADP(+)-isocitrate dehydrogenase from the cyanobacterium Anabaena sp. strain PCC 7120: purification and characterization of the enzyme and cloning, sequencing, and disruption of the icd gene. Muro-Pastor, M.I., Florencio, F.J. J. Bacteriol. (1994) [Pubmed]
  3. Kinetic properties and metabolic contributions of yeast mitochondrial and cytosolic NADP+-specific isocitrate dehydrogenases. Contreras-Shannon, V., Lin, A.P., McCammon, M.T., McAlister-Henn, L. J. Biol. Chem. (2005) [Pubmed]
  4. A single gene produces mitochondrial, cytoplasmic, and peroxisomal NADP-dependent isocitrate dehydrogenase in Aspergillus nidulans. Szewczyk, E., Andrianopoulos, A., Davis, M.A., Hynes, M.J. J. Biol. Chem. (2001) [Pubmed]
  5. 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]
  6. Multiple cellular consequences of isocitrate dehydrogenase isozyme dysfunction. McCammon, M.T., McAlister-Henn, L. Arch. Biochem. Biophys. (2003) [Pubmed]
  7. Isolation, nucleotide sequence, and disruption of the Saccharomyces cerevisiae gene encoding mitochondrial NADP(H)-specific isocitrate dehydrogenase. Haselbeck, R.J., McAlister-Henn, L. J. Biol. Chem. (1991) [Pubmed]
  8. Function and expression of yeast mitochondrial NAD- and NADP-specific isocitrate dehydrogenases. Haselbeck, R.J., McAlister-Henn, L. J. Biol. Chem. (1993) [Pubmed]
  9. Isolation, characterization, and disruption of the yeast gene encoding cytosolic NADP-specific isocitrate dehydrogenase. Loftus, T.M., Hall, L.V., Anderson, S.L., McAlister-Henn, L. Biochemistry (1994) [Pubmed]
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