GLUD2

From Wikipedia, the free encyclopedia

Glutamate dehydrogenase 2

PDB rendering based on 1hwx.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1hwx, 1hwy, 1hwz, 1l1f, 1nqt, 1nr1, 1nr7

Identifiers

Symbols

GLUD2; GDH2; GLUDP1

External IDs

OMIM: 300144 HomoloGene: 115647 GeneCards: GLUD2 Gene

EC number

1.4.1.3

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

Orthologs

Species

Human

Mouse

n/a

n/a

n/a

RefSeq (mRNA)

NM_012084

n/a

RefSeq (protein)

NP_036216

n/a

Location (UCSC)

Chr X:
120.18 – 120.18 Mb

n/a

PubMed search

n/a

Glutamate dehydrogenase 2, mitochondrial, also known as GDH 2, is an enzyme that in humans is encoded by the GLUD2 gene.^[1]^[2]^[3]

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.^[1]

References

↑ 1.0 1.1 "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. 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. 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.. "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. "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. PMID 20194501.
Ahmed M, Forsberg J, Bergsten P. "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. 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.. "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

1.4.3: oxygen acceptor

1.4.4: disulfide acceptor

Glycine decarboxylase complex

1.4.99: other acceptors

B
enzm
1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
2.1
- 2
- 3
- 4
- 5
- 6
- 7
  - 2.7.10
  - 11-12
- 8
3.1
- - 3.1.3.48
- 2
- 3
- 4
  - 3.4.21
  - 22
  - 23
  - 24
- 5
- 6
- 7
4.1
- 2
- 3
- 4
- 5
- 6
5.1
- 2
- 3
- 4
- 99
6.1-3
- 4
- 5-6

This article is issued from Wikipedia. The text is available under the Creative Commons Attribution/Share Alike; additional terms may apply for the media files.

GLUD2

Function

References

Further reading