IDH3A

Isocitrate dehydrogenase 3 (NAD+) alpha
Identifiers
Symbols	IDH3A;
External IDs	OMIM: 601149 MGI: 1915084 HomoloGene: 4037 GeneCards: IDH3A Gene
EC number	1.1.1.41
Gene Ontology Molecular function • magnesium ion binding • isocitrate dehydrogenase (NAD+) activity • oxidoreductase activity • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor • NAD binding Cellular component • mitochondrion • mitochondrial matrix Biological process • carbohydrate metabolic process • tricarboxylic acid cycle • isocitrate metabolic process • 2-oxoglutarate metabolic process • NADH metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3419	67834
Ensembl	ENSG00000166411	ENSMUSG00000032279
UniProt	P50213	Q9D6R2
RefSeq (mRNA)	NM_005530	NM_029573.2
RefSeq (protein)	NP_005521	NP_083849.1
Location (UCSC)	Chr 15: 78.44 – 78.46 Mb	Chr 9: 54.43 – 54.45 Mb
PubMed search	[1]	[2]

Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial is an enzyme that in humans is encoded by the IDH3A gene.

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.

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Citric_acid_cycle edit

Isocitrate dehydrogenases 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. NAD(+)-dependent isocitrate dehydrogenases catalyze the allosterically regulated rate-limiting step of the tricarboxylic acid cycle. Each isozyme is a heterotetramer that is composed of two alpha subunits, one beta subunit, and one gamma subunit. The protein encoded by this gene is the alpha subunit of one isozyme of NAD(+)-dependent isocitrate dehydrogenase.

Further reading

• Anderson NL, Anderson NG (2003). "The human plasma proteome: history, character, and diagnostic prospects.". Mol. Cell Proteomics 1 (11): 845–67. doi:10.1074/mcp.R200007-MCP200. PMID 12488461. 
• Kim YO, Oh IU, Park HS, et al. (1995). "Characterization of a cDNA clone for human NAD(+)-specific isocitrate dehydrogenase alpha-subunit and structural comparison with its isoenzymes from different species". Biochem. J. 308 (Pt 1): 63–8. PMC 1136843. PMID 7755589. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1136843. 
• 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. 
• 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. 
• Kim YO, Koh HJ, Kim SH, et al. (2000). "Identification and functional characterization of a novel, tissue-specific NAD(+)-dependent isocitrate dehydrogenase beta subunit isoform". J. Biol. Chem. 274 (52): 36866–75. doi:10.1074/jbc.274.52.36866. PMID 10601238. 
• Weiss C, Zeng Y, Huang J, et al. (2000). "Bovine NAD+-dependent isocitrate dehydrogenase: alternative splicing and tissue-dependent expression of subunit 1". Biochemistry 39 (7): 1807–16. doi:10.1021/bi991691i. PMID 10677231. 
• 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. 
• Adkins JN, Varnum SM, Auberry KJ, et al. (2003). "Toward a human blood serum proteome: analysis by multidimensional separation coupled with mass spectrometry". Mol. Cell Proteomics 1 (12): 947–55. doi:10.1074/mcp.M200066-MCP200. PMID 12543931. 
• Soundar S, Park JH, Huh TL, Colman RF (2004). "Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase". J. Biol. Chem. 278 (52): 52146–53. doi:10.1074/jbc.M306178200. PMID 14555658. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• 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. 
• Guo D, Han J, Adam BL, et al. (2005). "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochem. Biophys. Res. Commun. 337 (4): 1308–18. doi:10.1016/j.bbrc.2005.09.191. PMID 16236267. 
• Soundar S, O'hagan M, Fomulu KS, Colman RF (2006). "Identification of Mn2+-binding aspartates from alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase". J. Biol. Chem. 281 (30): 21073–81. doi:10.1074/jbc.M602956200. PMID 16737955. 
• Bzymek KP, Colman RF (2007). "Role of alpha-Asp181, beta-Asp192, and gamma-Asp190 in the distinctive subunits of human NAD-specific isocitrate dehydrogenase". Biochemistry 46 (18): 5391–7. doi:10.1021/bi700061t. PMID 17432878.