GLUD2

GLUD2
Identifiers
Aliases	GLUD2 , GDH2, GLUDP1, glutamate dehydrogenase 2
External IDs	OMIM: 300144; HomoloGene: 115647; GeneCards: GLUD2; OMA:GLUD2 - orthologs
Gene location (Human) Chr. X chromosome (human) [1] Band Xq24 Start 121,047,610 bp [1] End 121,050,094 bp [1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right testis left testis testicle placenta right adrenal gland right adrenal cortex liver right lobe of liver human kidney left adrenal gland n/a More reference expression data BioGPS n/a
Gene ontology Molecular function ADP binding oxidoreductase activity GTP binding leucine binding glutamate dehydrogenase [NAD(P)+ activity] glutamate dehydrogenase (NAD+) activity oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor Cellular component cytoplasm mitochondrion Biological process cellular amino acid metabolic process glutamate metabolic process glutamate catabolic process glutamate biosynthetic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2747 n/a Ensembl ENSG00000182890 ENSG00000288118 n/a UniProt P49448 n/a RefSeq (mRNA) NM_012084 n/a RefSeq (protein) NP_036216 n/a Location (UCSC) Chr X: 121.05 – 121.05 Mb n/a PubMed search [2] n/a
Wikidata
View/Edit Human

Glutamate dehydrogenase 2, mitochondrial, also known as GDH 2, is an enzyme that in humans is encoded by the GLUD2 gene. ^{[3] [4] [5]} This dehydrogenase is one of the family of glutamate dehydrogenases that are ubiquitous in life.

Function

Glutamate dehydrogenase 2 is localized to the mitochondrion and acts as a homohexamer to recycle glutamate during neurotransmission. The encoded enzyme catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate. ^[3]

References

1. ENSG00000288118 GRCh38: Ensembl release 89: ENSG00000182890, ENSG00000288118 – Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Entrez Gene: glutamate dehydrogenase 2".
4. Shashidharan P, Michaelidis TM, Robakis NK, Kresovali A, Papamatheakis J, Plaitakis A (June 1994). "Novel human glutamate dehydrogenase expressed in neural and testicular tissues and encoded by an X-linked intronless gene". J. Biol. Chem. 269 (24): 16971–6. doi: 10.1016/S0021-9258(19)89484-X . PMID   8207021.
5. Shashidharan P, Clarke DD, Ahmed N, Moschonas N, Plaitakis A (May 1997). "Nerve tissue-specific human glutamate dehydrogenase that is thermolabile and highly regulated by ADP". J. Neurochem. 68 (5): 1804–11. doi:10.1046/j.1471-4159.1997.68051804.x. PMID   9109504. S2CID   83848260.

Further reading

• Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome". Nature. 434 (7031): 325–37. Bibcode:2005Natur.434..325R. doi:10.1038/nature03440. PMC   2665286 . PMID   15772651.
• Need AC, Keefe RS, Ge D, et al. (2009). "Pharmacogenetics of antipsychotic response in the CATIE trial: a candidate gene analysis". Eur. J. Hum. Genet. 17 (7): 946–57. doi:10.1038/ejhg.2008.264. PMC   2986499 . PMID   19156168.
• Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl: 11858/00-001M-0000-0010-8592-0 . PMID   16169070. S2CID   8235923.
• Burki F, Kaessmann H (2004). "Birth and adaptive evolution of a hominoid gene that supports high neurotransmitter flux". Nat. Genet. 36 (10): 1061–3. doi: 10.1038/ng1431 . PMID   15378063.
• Plaitakis A, Latsoudis H, Kanavouras K, et al. (2010). "Gain-of-function variant in GLUD2 glutamate dehydrogenase modifies Parkinson's disease onset". Eur. J. Hum. Genet. 18 (3): 336–41. doi:10.1038/ejhg.2009.179. PMC   2987208 . PMID   19826450.
• Yang SJ, Cho EH, Choi MM, et al. (2005). "Critical role of the cysteine 323 residue in the catalytic activity of human glutamate dehydrogenase isozymes". Mol. Cells. 19 (1): 97–103. doi: 10.1016/S1016-8478(23)13142-6 . PMID   15750346.
• Yang SJ, Huh JW, Hong HN, et al. (2004). "Important role of Ser443 in different thermal stability of human glutamate dehydrogenase isozymes". FEBS Lett. 562 (1–3): 59–64. doi: 10.1016/S0014-5793(04)00183-8 . PMID   15044002.
• Kanavouras K, Borompokas N, Latsoudis H, et al. (2009). "Mutations in human GLUD2 glutamate dehydrogenase affecting basal activity and regulation". J. Neurochem. 109 (Suppl 1): 167–73. doi: 10.1111/j.1471-4159.2009.05914.x . PMID   19393024.
• Mastorodemos V, Zaganas I, Spanaki C, et al. (2005). "Molecular basis of human glutamate dehydrogenase regulation under changing energy demands". J. Neurosci. Res. 79 (1–2): 65–73. doi:10.1002/jnr.20353. PMID   15578726. S2CID   24840962.
• Smith TJ, Schmidt T, Fang J, et al. (2002). "The structure of apo human glutamate dehydrogenase details subunit communication and allostery". J. Mol. Biol. 318 (3): 765–77. doi:10.1016/S0022-2836(02)00161-4. PMID   12054821.
• Plaitakis A, Spanaki C, Mastorodemos V, Zaganas I (2003). "Study of structure-function relationships in human glutamate dehydrogenases reveals novel molecular mechanisms for the regulation of the nerve tissue-specific (GLUD2) isoenzyme". Neurochem. Int. 43 (4–5): 401–10. doi:10.1016/S0197-0186(03)00028-7. PMID   12742085. S2CID   21332852.
• Mastorodemos V, Kotzamani D, Zaganas I, et al. (2009). "Human GLUD1 and GLUD2 glutamate dehydrogenase localize to mitochondria and endoplasmic reticulum". Biochem. Cell Biol. 87 (3): 505–16. Bibcode:2009BCB....87..008M. doi:10.1139/o09-008. PMID   19448744.
• Spanaki C, Zaganas I, Kleopa KA, Plaitakis A (2010). "Human GLUD2 glutamate dehydrogenase is expressed in neural and testicular supporting cells". J. Biol. Chem. 285 (22): 16748–56. doi: 10.1074/jbc.M109.092999 . PMC   2878061 . PMID   20194501.
• Ahmed M, Forsberg J, Bergsten P (2005). "Protein profiling of human pancreatic islets by two-dimensional gel electrophoresis and mass spectrometry". J. Proteome Res. 4 (3): 931–40. doi:10.1021/pr050024a. PMID   15952740.
• Rosso L, Marques AC, Reichert AS, Kaessmann H (2008). "Mitochondrial targeting adaptation of the hominoid-specific glutamate dehydrogenase driven by positive Darwinian selection". PLOS Genet. 4 (8) e1000150. doi: 10.1371/journal.pgen.1000150 . PMC   2478720 . PMID   18688271.
• 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.
• Zaganas I, Kanavouras K, Mastorodemos V, et al. (2009). "The human GLUD2 glutamate dehydrogenase: localization and functional aspects". Neurochem. Int. 55 (1–3): 52–63. doi:10.1016/j.neuint.2009.03.001. PMID   19428807. S2CID   40181114.
• 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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Kanavouras K, Mastorodemos V, Borompokas N, et al. (2007). "Properties and molecular evolution of human GLUD2 (neural and testicular tissue-specific) glutamate dehydrogenase". J. Neurosci. Res. 85 (15): 3398–406. doi:10.1002/jnr.21576. PMID   17924438. S2CID   30673608.