GLUD2
Glutamate dehydrogenase 2, mitochondrial, also known as GDH 2, is an enzyme that in humans is encoded by the GLUD2 gene.[2][3][4] 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.[2]
References
Further reading
- Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome.". Nature. 434 (7031): 325–37. PMC 2665286 . PMID 15772651. doi:10.1038/nature03440.
- 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. PMC 2986499 . PMID 19156168. doi:10.1038/ejhg.2008.264.
- 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. PMID 16169070. doi:10.1016/j.cell.2005.08.029.
- Burki F, Kaessmann H (2004). "Birth and adaptive evolution of a hominoid gene that supports high neurotransmitter flux.". Nat. Genet. 36 (10): 1061–3. PMID 15378063. doi:10.1038/ng1431.
- 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. PMC 2987208 . PMID 19826450. doi:10.1038/ejhg.2009.179.
- 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. 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. PMID 15044002. doi:10.1016/S0014-5793(04)00183-8.
- 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. PMID 19393024. doi:10.1111/j.1471-4159.2009.05914.x.
- 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. PMID 15578726. doi:10.1002/jnr.20353.
- 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. PMID 12054821. doi:10.1016/S0022-2836(02)00161-4.
- 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. PMID 12742085. doi:10.1016/S0197-0186(03)00028-7.
- 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. PMID 19448744. doi:10.1139/o09-008.
- 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. PMC 2878061 . PMID 20194501. doi:10.1074/jbc.M109.092999.
- 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. PMID 15952740. doi:10.1021/pr050024a.
- 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. PMC 2478720 . PMID 18688271. doi:10.1371/journal.pgen.1000150.
- 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. PMC 528928 . PMID 15489334. doi:10.1101/gr.2596504.
- 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. PMID 19428807. doi:10.1016/j.neuint.2009.03.001.
- 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. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
- 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. PMID 17924438. doi:10.1002/jnr.21576.
PDB gallery |
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1hwx: CRYSTAL STRUCTURE OF BOVINE LIVER GLUTAMATE DEHYDROGENASE COMPLEXED WITH GTP, NADH, AND L-GLUTAMIC ACID
1hwy: BOVINE GLUTAMATE DEHYDROGENASE COMPLEXED WITH NAD AND 2-OXOGLUTARATE
1hwz: BOVINE GLUTAMATE DEHYDROGENASE COMPLEXED WITH NADPH, GLUTAMATE, AND GTP
1l1f: Structure of human glutamate dehydrogenase-apo form
1nqt: Crystal structure of bovine Glutamate dehydrogenase-ADP complex
1nr7: Crystal structure of apo bovine glutamate dehydrogenase
1nr1: Crystal structure of the R463A mutant of human Glutamate dehydrogenase
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