IDH3A

Isocitrate dehydrogenase 3 (NAD+) alpha, also known as IDH3A, is a human gene.cite web | title = Entrez Gene: IDH3A isocitrate dehydrogenase 3 (NAD+) alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3419| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: IDH3A isocitrate dehydrogenase 3 (NAD+) alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3419| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Anderson NL, Anderson NG |title=The human plasma proteome: history, character, and diagnostic prospects. |journal=Mol. Cell Proteomics |volume=1 |issue= 11 |pages= 845–67 |year= 2003 |pmid= 12488461 |doi=
*cite journal | author=Kim YO, Oh IU, Park HS, "et al." |title=Characterization of a cDNA clone for human NAD(+)-specific isocitrate dehydrogenase alpha-subunit and structural comparison with its isoenzymes from different species. |journal=Biochem. J. |volume=308 ( Pt 1) |issue= |pages= 63–8 |year= 1995 |pmid= 7755589 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Huh TL, Kim YO, Oh IU, "et al." |title=Assignment of the human mitochondrial NAD+ -specific isocitrate dehydrogenase alpha subunit (IDH3A) gene to 15q25.1-->q25.2by in situ hybridization. |journal=Genomics |volume=32 |issue= 2 |pages= 295–6 |year= 1997 |pmid= 8833160 |doi= 10.1006/geno.1996.0120
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Kim YO, Koh HJ, Kim SH, "et al." |title=Identification and functional characterization of a novel, tissue-specific NAD(+)-dependent isocitrate dehydrogenase beta subunit isoform. |journal=J. Biol. Chem. |volume=274 |issue= 52 |pages= 36866–75 |year= 2000 |pmid= 10601238 |doi=
*cite journal | author=Weiss C, Zeng Y, Huang J, "et al." |title=Bovine NAD+-dependent isocitrate dehydrogenase: alternative splicing and tissue-dependent expression of subunit 1. |journal=Biochemistry |volume=39 |issue= 7 |pages= 1807–16 |year= 2000 |pmid= 10677231 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Adkins JN, Varnum SM, Auberry KJ, "et al." |title=Toward a human blood serum proteome: analysis by multidimensional separation coupled with mass spectrometry. |journal=Mol. Cell Proteomics |volume=1 |issue= 12 |pages= 947–55 |year= 2003 |pmid= 12543931 |doi=
*cite journal | author=Soundar S, Park JH, Huh TL, Colman RF |title=Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase. |journal=J. Biol. Chem. |volume=278 |issue= 52 |pages= 52146–53 |year= 2004 |pmid= 14555658 |doi= 10.1074/jbc.M306178200
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Guo D, Han J, Adam BL, "et al." |title=Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress. |journal=Biochem. Biophys. Res. Commun. |volume=337 |issue= 4 |pages= 1308–18 |year= 2005 |pmid= 16236267 |doi= 10.1016/j.bbrc.2005.09.191
*cite journal | author=Soundar S, O'hagan M, Fomulu KS, Colman RF |title=Identification of Mn2+-binding aspartates from alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase. |journal=J. Biol. Chem. |volume=281 |issue= 30 |pages= 21073–81 |year= 2006 |pmid= 16737955 |doi= 10.1074/jbc.M602956200
*cite journal | author=Bzymek KP, Colman RF |title=Role of alpha-Asp181, beta-Asp192, and gamma-Asp190 in the distinctive subunits of human NAD-specific isocitrate dehydrogenase. |journal=Biochemistry |volume=46 |issue= 18 |pages= 5391–7 |year= 2007 |pmid= 17432878 |doi= 10.1021/bi700061t

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes