GLUD2

Identifiers

GLUD2, GDH2, GLUDP1, glutamate dehydrogenase 2

External IDs

Gene ontology
Molecular function	• glutamate dehydrogenase (NAD+) activity • ADP binding • oxidoreductase activity • GTP binding • leucine binding • glutamate dehydrogenase [NAD(P)+ activity]
Cellular component	• cytoplasm • mitochondrion
Biological process	• cellular amino acid metabolic process • glutamate metabolic process • glutamate catabolic process • glutamate biosynthetic process • oxidation-reduction process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


2747


n/a

Ensembl


ENSG00000182890


n/a

UniProt


P49448


n/a

RefSeq (mRNA)


NM_012084


n/a

RefSeq (protein)


NP_036216.2


n/a

Location (UCSC)

Chr X: 121.05 – 121.05 Mb

n/a

PubMed search

^[1]

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.^[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

↑ "Human PubMed Reference:".
1 2 "Entrez Gene: glutamate dehydrogenase 2".
↑ 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. PMID 8207021.
↑ 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.

Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome.". Nature. 434 (7031): 325–37. 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. PMID 16169070.
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. 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.
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.
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. 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.
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. 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.

PDB gallery

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

CH-NH₂ oxidoreductases (EC 1.4) - primarily amino acid oxidoreductases

1.4.1: NAD/NADP acceptor	Glutamate dehydrogenase GLUD1 GLUD2 Glutamate synthase (NADPH)

1.4.3: oxygen acceptor	D-amino acid oxidase Amine oxidase (Copper-containing (Lysyl Diamine Primary-amine)) (Flavin-containing (Monoamine)))

1.4.4: disulfide acceptor	Glycine cleavage system

1.4.99: other acceptors	D-amino acid dehydrogenase Amine dehydrogenase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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GLUD2

Function

References

Further reading