GLUD2

GLUD2
Estruturas dispoñibles
PDB	Buscar ortólogos: PDBe, RCSB
Identificadores
Nomenclatura	Outros nomes GLUD2, GDH2, GLUDP1, glutamato deshidroxenase 2
Símbolo	4336
Identificadores externos	OMIM: 300144 HomoloGene: 115647 GeneCards: Xene 2747
Locus	Cr. X q24
Ontoloxía Xénica Referencias: AmiGO / QuickGO
Ortólogos
Especies	Humano Rato
Entrez	2747 n/a
Ensembl	Véxase HS n/a
UniProt	P49448 n/a
RefSeq (ARNm)	NM_012084 n/a
RefSeq (proteína) NCBI	NP_036216 n/a
Localización (UCSC)	Cr. X: 121.05 – 121.05 Mb n/a
PubMed (Busca)	2747

A glutamato deshidroxenase 2, mitocondrial, tamén chamada GDH 2, é un encima que nos humanos está codificado polo xene GLUD2 do cromosoma X sen intróns. Esta deshidroxenase é un dos encimas da familia das glutamato deshidroxenases, que están moi estendidas entre os seres vivos.

Función

A glutamato deshidroxenase 2 está localizada nas mitocondrias e actúa como un homohexámero para reciclar glutamato durante a neurotransmisión. O encima codificado cataliza a desaminación oxidativa reversible do glutamato a alfa-cetoglutarato (tamén chamado 2-oxoglutarato).

Véxase tamén

Bibliografía

• 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. 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. hdl:11858/00-001M-0000-0010-8592-0. 
• 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. Bibcode:2002PNAS...9916899M. 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. 

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Este artigo sobre bioloxía é, polo de agora, só un bosquexo. Traballa nel para axudar a contribuír a que a Galipedia mellore e medre.  Existen igualmente outros artigos relacionados con este tema nos que tamén podes contribuír.

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