Alanine--glyoxylate aminotransferase 2, mitochondrial
Details
- Name
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Synonyms
- (R)-3-amino-2-methylpropionate--pyruvate transaminase
- 2.6.1.44
- AGT 2
- AGT2
- Beta-ALAAT II
- Beta-alanine-pyruvate aminotransferase
- D-AIBAT
- Gene Name
- AGXT2
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0000204|Alanine--glyoxylate aminotransferase 2, mitochondrial MTLIWRHLLRPLCLVTSAPRILEMHPFLSLGTSRTSVTKLSLHTKPRMPPCDFMPERYQS LGYNRVLEIHKEHLSPVVTAYFQKPLLLHQGHMEWLFDAEGSRYLDFFSGIVTVSVGHCH PKVNAVAQKQLGRLWHTSTVFFHPPMHEYAEKLAALLPEPLKVIFLVNSGSEANELAMLM ARAHSNNIDIISFRGAYHGCSPYTLGLTNVGTYKMELPGGTGCQPTMCPDVFRGPWGGSH CRDSPVQTIRKCSCAPDCCQAKDQYIEQFKDTLSTSVAKSIAGFFAEPIQGVNGVVQYPK GFLKEAFELVRARGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAA VITTPEIAKSLAKCLQHFNTFGGNPMACAIGSAVLEVIKEENLQENSQEVGTYMLLKFAK LRDEFEIVGDVRGKGLMIGIEMVQDKISCRPLPREEVNQIHEDCKHMGLLVGRGSIFSQT FRIAPSMCITKPEVDFAVEVFRSALTQHMERRAK
- Number of residues
- 514
- Molecular Weight
- 57155.905
- Theoretical pI
- 7.91
- GO Classification
- Functions(R)-3-amino-2-methylpropionate-pyruvate transaminase activity / alanine-glyoxylate transaminase activity / beta-alanine-pyruvate transaminase activity / identical protein binding / pyridoxal phosphate bindingProcessescellular nitrogen compound metabolic process / glycine biosynthetic process, by transamination of glyoxylate / glyoxylate catabolic process / glyoxylate metabolic process / L-alanine catabolic process, by transamination / nucleobase-containing small molecule metabolic process / positive regulation of nitric oxide biosynthetic process / pyrimidine nucleobase metabolic process / pyrimidine nucleoside catabolic process / small molecule metabolic processComponentsmitochondrial matrix / mitochondrion
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure.
- Pfam Domain Function
- Aminotran_3 (PF00202)
- Transmembrane Regions
- Not Available
- Cellular Location
- Mitochondrion
- Gene sequence
>lcl|BSEQ0016012|Alanine--glyoxylate aminotransferase 2, mitochondrial (AGXT2) ATGACTCTAATCTGGAGACATTTGCTGAGACCCTTGTGCCTGGTCACTTCCGCTCCCAGG ATCCTTGAGATGCATCCTTTCCTGAGCCTAGGTACTTCCCGGACATCAGTAACCAAGCTC AGTCTTCATACAAAGCCCAGAATGCCTCCATGTGACTTCATGCCTGAAAGATACCAGTCC CTTGGCTACAACCGTGTCCTGGAAATCCACAAGGAACATCTTTCTCCTGTGGTGACGGCA TATTTCCAGAAACCCCTGCTGCTCCACCAGGGGCACATGGAGTGGCTCTTTGATGCTGAA GGAAGCAGATACCTGGATTTCTTTTCCGGGATTGTTACTGTCAGTGTTGGCCATTGCCAC CCAAAGGTGAATGCAGTGGCACAAAAGCAGCTCGGCCGCCTGTGGCATACAAGCACCGTC TTCTTCCACCCTCCAATGCATGAATATGCAGAGAAGCTTGCCGCACTTCTTCCTGAGCCT CTTAAGGTCATTTTCTTGGTGAACAGTGGCTCAGAAGCCAATGAGCTGGCCATGCTGATG GCCAGGGCGCACTCAAACAACATAGACATCATTTCTTTCAGAGGAGCCTACCATGGATGC AGTCCTTACACACTTGGCTTGACAAACGTAGGGACCTACAAGATGGAACTCCCTGGTGGG ACAGGTTGCCAACCAACAATGTGTCCAGATGTTTTTCGTGGCCCTTGGGGAGGAAGCCAC TGTCGAGATTCTCCAGTGCAAACAATCAGGAAGTGCAGCTGTGCACCAGACTGCTGCCAA GCTAAAGATCAGTATATTGAGCAATTCAAAGATACGCTGAGCACATCTGTGGCCAAGTCA ATTGCTGGATTTTTCGCAGAACCTATTCAAGGTGTGAATGGAGTTGTCCAGTACCCAAAG GGGTTTCTAAAGGAAGCCTTTGAGCTGGTGCGAGCAAGGGGAGGCGTGTGCATTGCAGAT GAAGTGATTAAAGAAGAAAATCTACAGGAAAACAGTCAAGAAGTTGGGACCTACATGTTA CTAAAGTTTGCTAAGCTGCGGGATGAATTTGAAATTGTTGGAGACGTCCGAGGCAAAGGT CTCATGATAGGCATAGAAATGGTGCAGGATAAGATAAGCTGTCGGCCTCTTCCCCGTGAA GAAGTAAATCAGATCCATGAGGACTGCAAGCACATGGGACTCCTCGTTGGCAGAGGCAGC ATTTTTTCTCAGACATTTCGCATTGCGCCCTCAATGTGCATCACTAAACCAGAAGTTGAT TTTGCAGTAGAAGTATTTCGTTCTGCCTTAACCCAACACATGGAAAGAAGAGCTAAGTAA
- Chromosome Location
- 5
- Locus
- 5p13
- External Identifiers
Resource Link UniProtKB ID Q9BYV1 UniProtKB Entry Name AGT2_HUMAN GenBank Protein ID 12406973 GenBank Gene ID AJ292204 GenAtlas ID AGXT2 HGNC ID HGNC:14412 - General References
- Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [Article]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
- Rodionov RN, Murry DJ, Vaulman SF, Stevens JW, Lentz SR: Human alanine-glyoxylate aminotransferase 2 lowers asymmetric dimethylarginine and protects from inhibition of nitric oxide production. J Biol Chem. 2010 Feb 19;285(8):5385-91. doi: 10.1074/jbc.M109.091280. Epub 2009 Dec 14. [Article]
- Caplin B, Wang Z, Slaviero A, Tomlinson J, Dowsett L, Delahaye M, Salama A, Wheeler DC, Leiper J: Alanine-glyoxylate aminotransferase-2 metabolizes endogenous methylarginines, regulates NO, and controls blood pressure. Arterioscler Thromb Vasc Biol. 2012 Dec;32(12):2892-900. doi: 10.1161/ATVBAHA.112.254078. Epub 2012 Sep 27. [Article]
- Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
- Zhou JP, Bai YP, Hu XL, Kuang DB, Shi RZ, Xiong Y, Zhang W, Xia J, Chen BL, Yang TL, Chen XP: Association of the AGXT2 V140I polymorphism with risk for coronary heart disease in a Chinese population. J Atheroscler Thromb. 2014;21(10):1022-30. Epub 2014 May 16. [Article]
- Kittel A, Muller F, Konig J, Mieth M, Sticht H, Zolk O, Kralj A, Heinrich MR, Fromm MF, Maas R: Alanine-glyoxylate aminotransferase 2 (AGXT2) polymorphisms have considerable impact on methylarginine and beta-aminoisobutyrate metabolism in healthy volunteers. PLoS One. 2014 Feb 24;9(2):e88544. doi: 10.1371/journal.pone.0088544. eCollection 2014. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB00114 Pyridoxal phosphate approved, investigational, nutraceutical unknown cofactor Details DB00119 Pyruvic acid approved, investigational, nutraceutical unknown Details DB00160 Alanine nutraceutical unknown Details DB00145 Glycine approved, nutraceutical, vet_approved unknown product of Details