IDH3B

Isocitrate dehydrogenase 3 (NAD+) beta
Identifiers
Symbols	IDH3B; FLJ11043; H-IDHB; MGC903; RP46
External IDs	OMIM: 604526 MGI: 2158650 HomoloGene: 5035 GeneCards: IDH3B Gene
EC number	1.1.1.41
Gene Ontology Molecular function • magnesium ion binding • isocitrate dehydrogenase (NAD+) activity • electron carrier 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 • 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	3420	170718
Ensembl	ENSG00000101365	ENSMUSG00000027406
UniProt	O43837	n/a
RefSeq (mRNA)	NM_006899.2	NM_130884.4
RefSeq (protein)	NP_008830.2	NP_570954.1
Location (UCSC)	Chr 20: 2.64 – 2.64 Mb	Chr 2: 130.11 – 130.11 Mb
PubMed search	[1]	[2]

Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial is an enzyme that in humans is encoded by the IDH3B gene.

Interactive pathway map

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

[[File:

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

[[

]]

|{{{bSize}}}px]]

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 beta subunit of one isozyme of NAD(+)-dependent isocitrate dehydrogenase. Three alternatively spliced transcript variants encoding different isoforms have been described for this gene.

Further reading

• 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. 
• Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052. 
• 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. 
• 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. 
• Kil IS, Park JW (2005). "Regulation of mitochondrial NADP+-dependent isocitrate dehydrogenase activity by glutathionylation.". J. Biol. Chem. 280 (11): 10846–54. doi:10.1074/jbc.M411306200. PMID 15653693. 
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
• Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration.". Cell 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. 
• 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. 

External links

• GeneReviews/NCBI/NIH/UW entry on Retinitis Pigmentosa Overview