D2HGDH

D-2-hydroxyglutarate dehydrogenase
Identifiers
Symbols	D2HGDH; D2HGD; FLJ42195; MGC25181
External IDs	OMIM: 609186 HomoloGene: 5534 GeneCards: D2HGDH Gene
EC number	1.1.99.-
Gene Ontology Molecular function • protein binding • oxidoreductase activity • flavin adenine dinucleotide binding • (R)-2-hydroxyglutarate dehydrogenase activity • (R)-2-hydroxyglutarate dehydrogenase activity Cellular component • mitochondrion • mitochondrial matrix Biological process • 2-oxoglutarate metabolic process • response to manganese ion • response to zinc ion • response to cobalt ion • response to magnesium ion • cellular protein metabolic process • response to calcium ion Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	728294	98314
Ensembl	ENSG00000180902	ENSMUSG00000073609
UniProt	Q8N465	n/a
RefSeq (mRNA)	XM_001130341	NM_178882.3
RefSeq (protein)	XP_001130341	NP_849213.2
Location (UCSC)	Chr 2: 242.67 – 242.71 Mb	Chr 1: 95.72 – 95.75 Mb
PubMed search	[1]	[2]

D-2-hydroxyglutarate dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the D2HGDH gene.^[1][2][3]

This gene encodes D-2hydroxyglutarate dehydrogenase, a mitochondrial enzyme belonging to the FAD-binding oxidoreductase/transferase type 4 family. This enzyme, which is most active in liver and kidney but also active in heart and brain, converts D-2-hydroxyglutarate to 2-ketoglutarate. Mutations in this gene are present in D-2-hydroxyglutaric aciduria, a rare recessive neurometabolic disorder causing developmental delay, epilepsy, hypotonia, and dysmorphic features.^[3]

See also

• L2HGDH
• 2-hydroxyglutarate synthase
• 2-hydroxyglutarate dehydrogenase
• Hydroxyacid-oxoacid transhydrogenase

References

1. ^ Achouri Y, Noel G, Vertommen D, Rider MH, Veiga-Da-Cunha M, Van Schaftingen E (Jun 2004). "Identification of a dehydrogenase acting on D-2-hydroxyglutarate". Biochem J 381 (Pt 1): 35–42. doi:10.1042/BJ20031933. PMC 1133759. PMID 15070399. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1133759. 
2. ^ Struys EA, Salomons GS, Achouri Y, Van Schaftingen E, Grosso S, Craigen WJ, Verhoeven NM, Jakobs C (Jan 2005). "Mutations in the D-2-hydroxyglutarate dehydrogenase gene cause D-2-hydroxyglutaric aciduria". Am J Hum Genet 76 (2): 358–60. doi:10.1086/427890. PMC 1196381. PMID 15609246. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1196381. 
3. ^ ^{a b} "Entrez Gene: D2HGDH D-2-hydroxyglutarate dehydrogenase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=728294. 

Further reading

• Gibson KM, Craigen W, Herman GE, Jakobs C (1995). "D-2-hydroxyglutaric aciduria in a newborn with neurological abnormalities: a new neurometabolic disorder?". J. Inherit. Metab. Dis. 16 (3): 497–500. doi:10.1007/BF00711664. PMID 7609436. 
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548. 
• 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. 
• Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4.". Nature 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621. 
• Struys EA, Korman SH, Salomons GS, et al. (2005). "Mutations in phenotypically mild D-2-hydroxyglutaric aciduria.". Ann. Neurol. 58 (4): 626–30. doi:10.1002/ana.20559. PMID 16037974. 
• Misra VK, Struys EA, O'brien W, et al. (2006). "Phenotypic heterogeneity in the presentation of D-2-hydroxyglutaric aciduria in monozygotic twins.". Mol. Genet. Metab. 86 (1-2): 200–5. doi:10.1016/j.ymgme.2005.06.005. PMID 16081310. 
• 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. 
• Struys EA, Verhoeven NM, Salomons GS, et al. (2006). "D-2-hydroxyglutaric aciduria in three patients with proven SSADH deficiency: genetic coincidence or a related biochemical epiphenomenon?". Mol. Genet. Metab. 88 (1): 53–7. doi:10.1016/j.ymgme.2005.12.002. PMID 16442322. 
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.