IDH2

From Wikipedia, the free encyclopedia

Isocitrate dehydrogenase 2 (NADP+), mitochondrial

PDB rendering based on 1lwd.

Available structures: 1lwd

Identifiers

Symbol(s)

IDH2; IDH; IDP; ICD-M; IDHM; mNADP-IDH

External IDs

OMIM: 147650 MGI: 96414 HomoloGene: 37590

Gene ontology
Molecular Function:	• isocitrate dehydrogenase (NADP+) activity • oxidoreductase activity • oxidoreductase activity, acting on NADH or NADPH, NAD or NADP as acceptor
Cellular Component:	• mitochondrion • mitochondrial inner membrane
Biological Process:	• carbohydrate metabolic process • glyoxylate cycle • tricarboxylic acid cycle • metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002168 (mRNA)
NP_002159 (protein)

NM_173011 (mRNA)
NP_766599 (protein)

Location

Chr 15: 88.43 - 88.45 Mb

Chr 7: 79.97 - 79.99 Mb

Pubmed search

[1]

[2]

Isocitrate dehydrogenase 2 (NADP+), mitochondrial, also known as IDH2, is a human gene.^[1]

Isocitrate dehydrogenases are enzymes that catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. Each NADP(+)-dependent isozyme is a homodimer. The protein encoded by the IDH2 gene is the NADP(+)-dependent isocitrate dehydrogenase found in the mitochondria. It plays a role in intermediary metabolism and energy production. This protein may tightly associate or interact with the pyruvate dehydrogenase complex.^[1]

[edit] References

^ ^a ^b Entrez Gene: IDH2 isocitrate dehydrogenase 2 (NADP+), mitochondrial.

[edit] Further reading

Bruns GA, Eisenman RE, Gerald PS (1977). "Human mitochondrial NADP-dependent isocitrate dehydrogenase in man-mouse somatic cell hybrids.". Cytogenet. Cell Genet. 17 (4): 200–11. PMID 11969.
Shimizu N, Giles RE, Kucherlapati RS, et al. (1978). "Somatic cell genetic assignment of the human gene for mitochondrial NADP-linked isocitrate dehydrogenase to the long arm of chromosome 15.". Somatic Cell Genet. 3 (1): 47–60. PMID 564083.
Champion MJ, Brown JA, Shows TB (1979). "Assignment of cytoplasmic alpha-mannosidase (MANA) and confirmation of mitochondrial isocitrate dehydrogenase (IDHM) to the q11 leads to qter region of chromosome 15 in man.". Cytogenet. Cell Genet. 22 (1-6): 498–502. PMID 752528.
Grzeschik KH (1976). "Assignment of a gene for human mitochondrial isocitrate dehydrogenase (ICD-M, EC 1.1.1.41) to chromosome 15.". Hum. Genet. 34 (1): 23–8. PMID 965003.
Klimek J, Boguslawski W, Tialowska B, Zelewski L (1976). "Regulation of progesterone biosynthesis in human placental mitochondria by Krebs cycle metabolites.". Acta Biochim. Pol. 23 (2-3): 185–92. PMID 970033.
Chamberlain KG, Penington DG (1988). "Monoamine oxidase and other mitochondrial enzymes in density subpopulations of human platelets.". Thromb. Haemost. 59 (1): 29–33. PMID 3363531.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Luo H, Shan X, Wu J (1996). "Expression of human mitochondrial NADP-dependent isocitrate dehydrogenase during lymphocyte activation". J. Cell. Biochem. 60 (4): 495–507. doi:10.1002/(SICI)1097-4644(19960315)60:4<495::AID-JCB6>3.0.CO;2-N. PMID 8707889.
Oh IU, Inazawa J, Kim YO, et al. (1997). "Assignment of the human mitochondrial NADP(+)-specific isocitrate dehydrogenase (IDH2) gene to 15q26.1 by in situ hybridization.". Genomics 38 (1): 104–6. doi:10.1006/geno.1996.0602. PMID 8954790.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Foster LJ, Rudich A, Talior I, et al. (2006). "Insulin-dependent interactions of proteins with GLUT4 revealed through stable isotope labeling by amino acids in cell culture (SILAC).". J. Proteome Res. 5 (1): 64–75. doi:10.1021/pr0502626. PMID 16396496.
Kil IS, Kim SY, Lee SJ, Park JW (2007). "Small interfering RNA-mediated silencing of mitochondrial NADP+-dependent isocitrate dehydrogenase enhances the sensitivity of HeLa cells toward tumor necrosis factor-alpha and anticancer drugs.". Free Radic. Biol. Med. 43 (8): 1197–207. doi:10.1016/j.freeradbiomed.2007.07.009. PMID 17854715.