D2HGDH

D2HGDH
Identifiers
Aliases	D2HGDH , D2HGD, D-2-hydroxyglutarate dehydrogenase
External IDs	OMIM: 609186; MGI: 2138209; HomoloGene: 5534; GeneCards: D2HGDH; OMA:D2HGDH - orthologs
Gene location (Human) Chr. Chromosome 2 (human) [1] Band 2q37.3 Start 241,734,602 bp [1] End 241,768,816 bp [1]
Gene location (Mouse) Chr. Chromosome 1 (mouse) [2] Band 1|1 D Start 93,752,631 bp [2] End 93,780,070 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube pancreatic ductal cell tendon of biceps brachii left lobe of thyroid gland right lobe of thyroid gland anterior pituitary skin of abdomen right lobe of liver left ovary transverse colon Top expressed in left lobe of liver otolith organ utricle interventricular septum Rostral migratory stream ascending aorta hand semi-lunar valve Paneth cell ciliary body More reference expression data BioGPS n/a
Gene ontology Molecular function oxidoreductase activity catalytic activity flavin adenine dinucleotide binding oxidoreductase activity, acting on CH-OH group of donors D-lactate dehydrogenase (cytochrome) activity (R)-2-hydroxyglutarate dehydrogenase activity FAD binding Cellular component mitochondrial matrix mitochondrion extrinsic component of cytoplasmic side of plasma membrane Biological process response to calcium ion response to zinc ion response to magnesium ion response to cobalt ion response to manganese ion 2-oxoglutarate metabolic process lactate oxidation respiratory electron transport chain Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 728294 98314 Ensembl ENSG00000180902 ENSMUSG00000073609 UniProt Q8N465 Q8CIM3 RefSeq (mRNA) NM_001287249 NM_152783 NM_001352824 NM_178882 NM_001310767 RefSeq (protein) NP_001274178 NP_689996 NP_001339753 NP_001297696 NP_849213 Location (UCSC) Chr 2: 241.73 – 241.77 Mb Chr 1: 93.75 – 93.78 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

D-2-hydroxyglutarate dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the D2HGDH gene. ^{[5] [6] [7]}

This gene encodes D-2hydroxyglutarate dehydrogenase is 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. ^[7]

See also

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

References

1. GRCh38: Ensembl release 89: ENSG00000180902 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000073609 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. "Entrez Gene: D2HGDH D-2-hydroxyglutarate dehydrogenase".

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. S2CID   31099476.
• 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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• 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.
• 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. Bibcode:2005Natur.434..724H. 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. S2CID   45926378.
• 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.
• 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.