GOT2
Glutamic-oxaloacetic transaminase 2, mitochondrial (aspartate aminotransferase 2) | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||||
Symbols | GOT2 ; FLJ40994 | ||||||||||
External IDs | Template:OMIM5 Template:MGI HomoloGene: 1572 | ||||||||||
| |||||||||||
RNA expression pattern | |||||||||||
More reference expression data | |||||||||||
Orthologs | |||||||||||
Template:GNF Ortholog box | |||||||||||
Species | Human | Mouse | |||||||||
Entrez | n/a | n/a | |||||||||
Ensembl | n/a | n/a | |||||||||
UniProt | n/a | n/a | |||||||||
RefSeq (mRNA) | n/a | n/a | |||||||||
RefSeq (protein) | n/a | n/a | |||||||||
Location (UCSC) | n/a | n/a | |||||||||
PubMed search | n/a | n/a |
Glutamic-oxaloacetic transaminase 2, mitochondrial (aspartate aminotransferase 2), also known as GOT2, is a human gene.[1]
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.[1]
References
Further reading
- Doonan S, Barra D, Bossa F (1985). "Structural and genetic relationships between cytosolic and mitochondrial isoenzymes". Int. J. Biochem. 16 (12): 1193–9. 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. 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. 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. 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. PMID 4052435.
- Davidson RG, Cortner JA, Rattazzi MC; et al. (1970). "Genetic polymorphisms of human mitochondrial glutamic oxaloacetic transaminase". Science. 169 (943): 391–2. 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. 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. 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. 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. 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. 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. 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. 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. 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.
This protein-related article is a stub. You can help Wikipedia by expanding it. |