IDH3A

From Wikipedia, the free encyclopedia

Isocitrate dehydrogenase 3 (NAD+) alpha

Identifiers

External IDs

OMIM: 601149 MGI: 1915084 HomoloGene: 4037

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

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005530 (mRNA)
NP_005521 (protein)

NM_029573 (mRNA)
NP_083849 (protein)

Location

Chr 15: 76.23 - 76.25 Mb

Chr 9: 54.38 - 54.4 Mb

Pubmed search

[1]

[2]

Isocitrate dehydrogenase 3 (NAD+) alpha, also known as IDH3A, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: IDH3A isocitrate dehydrogenase 3 (NAD+) alpha.

[edit] Further reading

Anderson NL, Anderson NG (2003). "The human plasma proteome: history, character, and diagnostic prospects.". Mol. Cell Proteomics 1 (11): 845–67. 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. PMID 7755589.
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.
Huh TL, Kim YO, Oh IU, et al. (1997). "Assignment of the human mitochondrial NAD+ -specific isocitrate dehydrogenase alpha subunit (IDH3A) gene to 15q25.1-->q25.2by in situ hybridization.". Genomics 32 (2): 295–6. doi:10.1006/geno.1996.0120. PMID 8833160.
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.
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. 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. 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. PMID 12477932.
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. 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. PMID 15489334.
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.