GOT2

From Wikipedia, the free encyclopedia

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

Identifiers

GOT2; FLJ40994

External IDs

OMIM: 138150 MGI: 95792 HomoloGene: 1572

Gene ontology
Molecular Function:	• aspartate transaminase activity
Cellular Component:	• mitochondrion
Biological Process:	• amino acid metabolic process • aspartate catabolic process • biosynthetic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_002080 (mRNA)
NP_002071 (protein)

NM_010325 (mRNA)
NP_034455 (protein)

Location

Chr 16: 57.3 - 57.33 Mb

n/a

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: GOT2 glutamic-oxaloacetic transaminase 2, mitochondrial (aspartate aminotransferase 2).

[edit] 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.