OGDH

Oxoglutarate (alpha-ketoglutarate) dehydrogenase (lipoamide)
PDB rendering based on 3ery.
Available structures PDB 3ery
Identifiers
Symbols	OGDH; AKGDH; E1k; OGDC
External IDs	OMIM: 613022 MGI: 1098267 HomoloGene: 55662 GeneCards: OGDH Gene
EC number	1.2.4.2
Gene Ontology Molecular function • oxoglutarate dehydrogenase (succinyl-transferring) activity • oxidoreductase activity • thiamine pyrophosphate binding • oxoglutarate dehydrogenase (NAD+) activity Cellular component • mitochondrion • mitochondrial matrix • mitochondrial membrane Biological process • generation of precursor metabolites and energy • glycolysis • tricarboxylic acid cycle • lysine catabolic process • cerebellar cortex development • striatum development • hippocampus development • thalamus development • pyramidal neuron development • tangential migration from the subventricular zone to the olfactory bulb • cellular nitrogen compound metabolic process • olfactory bulb mitral cell layer development Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	4967	18293
Ensembl	ENSG00000105953	ENSMUSG00000020456
UniProt	Q02218	Q60597
RefSeq (mRNA)	NM_001003941.2	NM_010956.3
RefSeq (protein)	NP_001003941.1	NP_035086.2
Location (UCSC)	Chr 7: 44.65 – 44.75 Mb	Chr 11: 6.19 – 6.26 Mb
PubMed search	[1]	[2]

Alpha-ketoglutarate dehydrogenase also known as 2-oxoglutarate dehydrogenase E1 component, mitochondrial is an enzyme that in humans is encoded by the OGDH gene.^[1][2][3]

Function

This gene encodes one subunit of the 2-oxoglutarate dehydrogenase complex. This complex catalyzes the overall conversion of 2-oxoglutarate (alpha-ketoglutarate) to succinyl-CoA and CO₂ during the citric acid cycle. The protein is located in the mitochondrial matrix and uses thiamine pyrophosphate as a cofactor.^[3]

Clinical significance

A congenital deficiency in 2-oxoglutarate dehydrogenase activity is believed to lead to hypotonia, metabolic acidosis, and hyperlactatemia.^[3]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.^[4]

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Citric_acid_cycle edit

References

1. ^ Koike K, Urata Y, Goto S (March 1992). "Cloning and nucleotide sequence of the cDNA encoding human 2-oxoglutarate dehydrogenase (lipoamide)". Proc. Natl. Acad. Sci. U.S.A. 89 (5): 1963–7. doi:10.1073/pnas.89.5.1963. PMC 48574. PMID 1542694. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=48574. 
2. ^ Szabo P, Cai X, Ali G, Blass JP (March 1994). "Localization of the gene (OGDH) coding for the E1k component of the alpha-ketoglutarate dehydrogenase complex to chromosome 7p13-p11.2". Genomics 20 (2): 324–6. doi:10.1006/geno.1994.1178. PMID 8020988. 
3. ^ ^{a b c} "Entrez Gene: oxoglutarate (alpha-ketoglutarate) dehydrogenase (lipoamide)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4967. 
4. ^ The interactive pathway map can be edited at WikiPathways: "TCACycle_WP78". http://www.wikipathways.org/index.php/Pathway:WP78. 

Further reading

• Shi Q, Chen HL, Xu H, Gibson GE (2005). "Reduction in the E2k subunit of the alpha-ketoglutarate dehydrogenase complex has effects independent of complex activity.". J. Biol. Chem. 280 (12): 10888–96. doi:10.1074/jbc.M409064200. PMID 15649899. 
• 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. 
• Reed LJ, Hackert ML (1990). "Structure-function relationships in dihydrolipoamide acyltransferases.". J. Biol. Chem. 265 (16): 8971–4. PMID 2188967. 
• "Toward a complete human genome sequence.". Genome Res. 8 (11): 1097–108. 1998. doi:10.1101/gr.8.11.1097. PMID 9847074. 
• Bonaldo MF, Lennon G, Soares MB (1996). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548. 
• Koike K (1995). "The gene encoding human 2-oxoglutarate dehydrogenase: structural organization and mapping to chromosome 7p13-p14.". Gene 159 (2): 261–6. doi:10.1016/0378-1119(95)00086-L. PMID 7622061. 
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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. 
• McCartney RG, Rice JE, Sanderson SJ, et al. (1998). "Subunit interactions in the mammalian alpha-ketoglutarate dehydrogenase complex. Evidence for direct association of the alpha-ketoglutarate dehydrogenase and dihydrolipoamide dehydrogenase components.". J. Biol. Chem. 273 (37): 24158–64. doi:10.1074/jbc.273.37.24158. PMID 9727038. 
• van Bever Y, Balemans W, Duval EL, et al. (2007). "Exclusion of OGDH and BMP4 as candidate genes in two siblings with autosomal recessive DOOR syndrome.". Am. J. Med. Genet. A 143 (7): 763–7. doi:10.1002/ajmg.a.31641. PMID 17343268. 
• Habelhah H, Laine A, Erdjument-Bromage H, et al. (2004). "Regulation of 2-oxoglutarate (alpha-ketoglutarate) dehydrogenase stability by the RING finger ubiquitin ligase Siah.". J. Biol. Chem. 279 (51): 53782–8. doi:10.1074/jbc.M410315200. PMID 15466852. 

This article incorporates text from the United States National Library of Medicine, which is in the public domain.