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

RefSeq (mRNA)

RefSeq (protein)

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]

1 Function
2 Clinical significance
3 Interactive pathway map
4 References
5 Further reading

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

^ 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.
^ 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.
^ ^a ^b ^c "Entrez Gene: oxoglutarate (alpha-ketoglutarate) dehydrogenase (lipoamide)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4967.
^ The interactive pathway map can be edited at WikiPathways: "TCACycle_WP78". http://www.wikipathways.org/index.php/Pathway:WP78.

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.

PDB gallery

3ery: Different thermodynamic binding mechanisms and peptide fine specificities associated with a panel of structurally similar high-affinity T cell receptors

Aldehyde/oxo oxidoreductases (EC 1.2)

1.2.1: NAD or NADP	Aldehyde dehydrogenase: Acetaldehyde dehydrogenase (ALDH2) · Long-chain-aldehyde dehydrogenase Glyceraldehyde 3-phosphate dehydrogenase

1.2.2: cytochrome	Formate dehydrogenase (cytochrome)

1.2.3: oxygen	Aldehyde oxidase

1.2.4: disulfide	Oxoglutarate dehydrogenase · Pyruvate dehydrogenase · Branched-chain alpha-keto acid dehydrogenase complex (BCKDHA, BCKDHB, DBT, DLD)

1.2.7: iron-sulfur protein	Pyruvate synthase

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

Enzymes: multienzyme complexes

Photosynthesis	Photosynthetic reaction center complex proteins · Photosystem (I, II)

Dehydrogenase	Pyruvate dehydrogenase complex (E1, E2, E3) · Oxoglutarate dehydrogenase (OGDH, DLST, DLD) · Branched-chain alpha-keto acid dehydrogenase complex (BCKDHA, BCKDHB, DBT, DLD)

Other	CAD (Carbamoyl phosphate synthase II, Aspartate carbamoyltransferase, Dihydroorotase) · Cholesterol side-chain cleavage enzyme · Cytochrome b6f complex · Electron transport chain · Fatty acid synthetase complex · Glycine decarboxylase complex · Mitochondrial trifunctional protein (HADHA, HADHB) · Phosphoenolpyruvate sugar phosphotransferase system · Polyketide synthase · Sucrase-isomaltase complex · Tryptophan synthase

OGDH

Contents

Function

Clinical significance

Interactive pathway map

References

Further reading