GOT2

From Wikipedia, the free encyclopedia

Glutamic-oxaloacetic transaminase 2, mitochondrial (aspartate aminotransferase 2)

Identifiers

Symbols

GOT2; KAT4; KATIV; mitAAT

External IDs

OMIM: 138150 MGI: 95792 HomoloGene: 1572 GeneCards: GOT2 Gene

EC number

2.6.1.1, 2.6.1.7

Gene Ontology
Molecular function	• L-aspartate:2-oxoglutarate aminotransferase activity • kynurenine-oxoglutarate transaminase activity • pyridoxal phosphate binding • L-phenylalanine:2-oxoglutarate aminotransferase activity
Cellular component	• mitochondrion • mitochondrial inner membrane • mitochondrial matrix • plasma membrane
Biological process	• carbohydrate metabolic process • glucose metabolic process • gluconeogenesis • 2-oxoglutarate metabolic process • oxaloacetate metabolic process • aspartate metabolic process • aspartate biosynthetic process • aspartate catabolic process • glutamate metabolic process • cellular amino acid biosynthetic process • fatty acid transport • 4-hydroxyproline catabolic process • glutamate catabolic process to aspartate • glutamate catabolic process to 2-oxoglutarate • cellular nitrogen compound metabolic process • small molecule metabolic process • response to ethanol
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 16:
58.74 – 58.77 Mb

Chr 8:
95.86 – 95.89 Mb

PubMed search

Aspartate aminotransferase, mitochondrial is an enzyme that in humans is encoded by the GOT2 gene.^[1]^[2]

Glutamic-oxaloacetic transaminase is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2, respectively. GOT plays a role in amino acid metabolism and the urea and tricarboxylic acid cycles. The two enzymes are homodimeric and show close homology.^[2]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. ^{[§ 1]}

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Glycolysis and Gluconeogenesis edit

↑ The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".

References

↑ Guidetti P, Amori L, Sapko MT, Okuno E, Schwarcz R (Jun 2007). "Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain". J Neurochem 102 (1): 103–11. doi:10.1111/j.1471-4159.2007.04556.x. PMID 17442055.
↑ 2.0 2.1 "Entrez Gene: GOT2 glutamic-oxaloacetic transaminase 2, mitochondrial (aspartate aminotransferase 2)".

Doonan S, Barra D, Bossa F (1985). "Structural and genetic relationships between cytosolic and mitochondrial isoenzymes". Int. J. Biochem. 16 (12): 1193–9. doi:10.1016/0020-711X(84)90216-7. PMID 6397370.
Furuya E, Yoshida Y, Tagawa K (1979). "Interaction of mitochondrial aspartate aminotransferase with negatively charged lecithin liposomes". J. Biochem. 85 (5): 1157–63. PMID 376500.
Craig IW, Tolley E, Bobrow M, van Heyningen V (1979). "Assignment of a gene necessary for the expression of mitochondrial glutamic-oxaloacetic transaminase in human-mouse hybrid cells". Cytogenet. Cell Genet. 22 (1–6): 190–4. doi:10.1159/000130933. PMID 752471.
Pol S, Bousquet-Lemercier B, Pavé-Preux M, et al. (1989). "Chromosomal localization of human aspartate aminotransferase genes by in situ hybridization". Hum. Genet. 83 (2): 159–64. doi:10.1007/BF00286710. PMID 2777255.
Fahien LA, Kmiotek EH, MacDonald MJ, et al. (1988). "Regulation of malate dehydrogenase activity by glutamate, citrate, alpha-ketoglutarate, and multienzyme interaction". J. Biol. Chem. 263 (22): 10687–97. PMID 2899080.
Pol S, Bousquet-Lemercier B, Pave-Preux M, et al. (1989). "Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA". Biochem. Biophys. Res. Commun. 157 (3): 1309–15. doi:10.1016/S0006-291X(88)81017-9. PMID 3207426.
Fahien LA, Kmiotek EH, Woldegiorgis G, et al. (1985). "Regulation of aminotransferase-glutamate dehydrogenase interactions by carbamyl phosphate synthase-I, Mg2+ plus leucine versus citrate and malate". J. Biol. Chem. 260 (10): 6069–79. PMID 3997814.
Martini F, Angelaccio S, Barra D, et al. (1985). "The primary structure of mitochondrial aspartate aminotransferase from human heart". Biochim. Biophys. Acta 832 (1): 46–51. doi:10.1016/0167-4838(85)90172-4. PMID 4052435.
Davidson RG, Cortner JA, Rattazzi MC, et al. (1970). "Genetic polymorphisms of human mitochondrial glutamic oxaloacetic transaminase". Science 169 (3943): 391–2. doi:10.1126/science.169.3943.391. PMID 5450376.
Ford GC, Eichele G, Jansonius JN (1980). "Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase". Proc. Natl. Acad. Sci. U.S.A. 77 (5): 2559–63. doi:10.1073/pnas.77.5.2559. PMC 349441. PMID 6930651.
Jeremiah SJ, Povey S, Burley MW, et al. (1982). "Mapping studies on human mitochondrial glutamate oxaloacetate transaminase". Ann. Hum. Genet. 46 (Pt 2): 145–52. doi:10.1111/j.1469-1809.1982.tb00705.x. PMID 7114792.
Tolley E, van Heyningen V, Brown R, et al. (1981). "Assignment to chromosome 16 of a gene necessary for the expression of human mitochondrial glutamate oxaloacetate transaminase (aspartate aminotransferase) (E.C. 2.6.1.1.)". Biochem. Genet. 18 (9–10): 947–54. doi:10.1007/BF00500127. PMID 7225087.
Lain B, Iriarte A, Mattingly JR, et al. (1995). "Structural features of the precursor to mitochondrial aspartate aminotransferase responsible for binding to hsp70". J. Biol. Chem. 270 (42): 24732–9. doi:10.1074/jbc.270.42.24732. PMID 7559589.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
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.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.

Transferase: nitrogenous groups (EC 2.6)

2.6.1: Transaminases

2.6.3: Oximinotransferases

Oximinotransferase

2.6.99: Other

Pyridoxine 5'-phosphate synthase

B
enzm
1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
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- 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

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GOT2

Interactive pathway map

References

Further reading