GOT2

Glutamic-oxaloacetic transaminase 2, mitochondrial (aspartate aminotransferase 2), also known as GOT2, is a human gene.cite web | title = Entrez Gene: GOT2 glutamic-oxaloacetic transaminase 2, mitochondrial (aspartate aminotransferase 2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2806| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: GOT2 glutamic-oxaloacetic transaminase 2, mitochondrial (aspartate aminotransferase 2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2806| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Doonan S, Barra D, Bossa F |title=Structural and genetic relationships between cytosolic and mitochondrial isoenzymes. |journal=Int. J. Biochem. |volume=16 |issue= 12 |pages= 1193–9 |year= 1985 |pmid= 6397370 |doi=
*cite journal | author=Furuya E, Yoshida Y, Tagawa K |title=Interaction of mitochondrial aspartate aminotransferase with negatively charged lecithin liposomes. |journal=J. Biochem. |volume=85 |issue= 5 |pages= 1157–63 |year= 1979 |pmid= 376500 |doi=
*cite journal | author=Craig IW, Tolley E, Bobrow M, van Heyningen V |title=Assignment of a gene necessary for the expression of mitochondrial glutamic-oxaloacetic transaminase in human-mouse hybrid cells. |journal=Cytogenet. Cell Genet. |volume=22 |issue= 1-6 |pages= 190–4 |year= 1979 |pmid= 752471 |doi=
*cite journal | author=Pol S, Bousquet-Lemercier B, Pavé-Preux M, "et al." |title=Chromosomal localization of human aspartate aminotransferase genes by in situ hybridization. |journal=Hum. Genet. |volume=83 |issue= 2 |pages= 159–64 |year= 1989 |pmid= 2777255 |doi=
*cite journal | author=Fahien LA, Kmiotek EH, MacDonald MJ, "et al." |title=Regulation of malate dehydrogenase activity by glutamate, citrate, alpha-ketoglutarate, and multienzyme interaction. |journal=J. Biol. Chem. |volume=263 |issue= 22 |pages= 10687–97 |year= 1988 |pmid= 2899080 |doi=
*cite journal | author=Pol S, Bousquet-Lemercier B, Pave-Preux M, "et al." |title=Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA. |journal=Biochem. Biophys. Res. Commun. |volume=157 |issue= 3 |pages= 1309–15 |year= 1989 |pmid= 3207426 |doi=
*cite journal | author=Fahien LA, Kmiotek EH, Woldegiorgis G, "et al." |title=Regulation of aminotransferase-glutamate dehydrogenase interactions by carbamyl phosphate synthase-I, Mg2+ plus leucine versus citrate and malate. |journal=J. Biol. Chem. |volume=260 |issue= 10 |pages= 6069–79 |year= 1985 |pmid= 3997814 |doi=
*cite journal | author=Martini F, Angelaccio S, Barra D, "et al." |title=The primary structure of mitochondrial aspartate aminotransferase from human heart. |journal=Biochim. Biophys. Acta |volume=832 |issue= 1 |pages= 46–51 |year= 1985 |pmid= 4052435 |doi=
*cite journal | author=Davidson RG, Cortner JA, Rattazzi MC, "et al." |title=Genetic polymorphisms of human mitochondrial glutamic oxaloacetic transaminase. |journal=Science |volume=169 |issue= 943 |pages= 391–2 |year= 1970 |pmid= 5450376 |doi=
*cite journal | author=Ford GC, Eichele G, Jansonius JN |title=Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=77 |issue= 5 |pages= 2559–63 |year= 1980 |pmid= 6930651 |doi=
*cite journal | author=Jeremiah SJ, Povey S, Burley MW, "et al." |title=Mapping studies on human mitochondrial glutamate oxaloacetate transaminase. |journal=Ann. Hum. Genet. |volume=46 |issue= Pt 2 |pages= 145–52 |year= 1982 |pmid= 7114792 |doi=
*cite journal | author=Tolley E, van Heyningen V, Brown R, "et al." |title=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.). |journal=Biochem. Genet. |volume=18 |issue= 9-10 |pages= 947–54 |year= 1981 |pmid= 7225087 |doi=
*cite journal | author=Lain B, Iriarte A, Mattingly JR, "et al." |title=Structural features of the precursor to mitochondrial aspartate aminotransferase responsible for binding to hsp70. |journal=J. Biol. Chem. |volume=270 |issue= 42 |pages= 24732–9 |year= 1995 |pmid= 7559589 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209

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