IDH2
From Wikipedia, the free encyclopedia
Isocitrate dehydrogenase [NADP], mitochondrial is an enzyme that in humans is encoded by the IDH2 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] Somatic mosaic mutations of this gene have also been found associated to Ollier disease and Maffucci syndrome[2] .
[edit] Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles. [3]
[edit] References
- ^ a b "Entrez Gene: IDH2 isocitrate dehydrogenase 2 (NADP+), mitochondrial". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3418.
- ^ Amary, MF; Damato, S, Halai, D, Eskandarpour, M, Berisha, F, Bonar, F, McCarthy, S, Fantin, VR, Straley, KS, Lobo, S, Aston, W, Green, CL, Gale, RE, Tirabosco, R, Futreal, A, Campbell, P, Presneau, N, Flanagan, AM (2011 Nov 6). "Ollier disease and Maffucci syndrome are caused by somatic mosaic mutations of IDH1 and IDH2.". Nature genetics 43 (12): 1262–5. doi:10.1038/ng.994. PMID 22057236.
- ^ The interactive pathway map can be edited at WikiPathways: "TCA_Cycle_WP78". http://www.wikipathways.org/index.php/Pathway:WP78.
[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. doi:10.1159/000130713. 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. doi:10.1007/BF01550986. 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. doi:10.1159/000131007. 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. doi:10.1007/BF00284430. 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. doi:10.1016/0378-1119(94)90802-8. 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. doi:10.1016/S0378-1119(97)00411-3. 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- 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. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- 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.
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