Branched-chain-amino-acid aminotransferase, mitochondrial
Details
- Name
- Branched-chain-amino-acid aminotransferase, mitochondrial
- Synonyms
- 2.6.1.42
- BCAT(m)
- BCATM
- BCT2
- ECA40
- Placental protein 18
- PP18
- Gene Name
- BCAT2
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0001438|Branched-chain-amino-acid aminotransferase, mitochondrial MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKT FTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRP WLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSL GVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLV QQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQS LLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIP TMENGPELILRFQKELKEIQYGIRAHEWMFPV
- Number of residues
- 392
- Molecular Weight
- 44287.445
- Theoretical pI
- 8.82
- GO Classification
- Functionsbranched-chain-amino-acid transaminase activity / L-isoleucine transaminase activity / L-leucine transaminase activity / L-valine transaminase activityProcessesbranched-chain amino acid biosynthetic process / branched-chain amino acid catabolic process / cellular nitrogen compound metabolic process / isoleucine catabolic process / leucine metabolic process / regulation of hormone levels / small molecule metabolic process / valine metabolic processComponentsmitochondrial matrix / mitochondrion
- General Function
- L-valine transaminase activity
- Specific Function
- Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids.
- Pfam Domain Function
- Aminotran_4 (PF01063)
- Transmembrane Regions
- Not Available
- Cellular Location
- Mitochondrion
- Gene sequence
>lcl|BSEQ0019000|Branched-chain-amino-acid aminotransferase, mitochondrial (BCAT2) ATGGCCGCAGCCGCTCTGGGGCAGCTGTTTGAGGGCATGAAGGCGTTCAAAGGCAAAGAC CAGCAGGTGCGCCTCTTCCGCCCCTGGCTCAACATGGACCGGATGCTGCGCTCAGCCATG CGCCTGTGCCTGCCGAGTTTCGACAAGCTGGAGTTGCTGGAGTGCATCCGCCGGCTCATC GAAGTGGACAAGGACTGGGTCCCCGATGCCGCCGGCACCAGCCTCTATGTGCGGCCTGTG CTCATTGGGAACGAGCCCTCGCTGGGTGTCAGCCAGCCCACGCGCGCGCTCCTGTTCGTC ATTCTCTGCCCAGTGGGTGCCTACTTCCCTGGAGGCTCCGTGACCCCGGTCTCCCTCCTG GCCGACCCAGCCTTCATCCGGGCCTGGGTGGGCGGGGTCGGCAACTACAAGTTAGGTGGG AATTATGGGCCCACCGTGTTAGTGCAACAGGAGGCACTCAAGCGGGGCTGTGAACAGGTC CTCTGGCTGTATGGGCCCGACCACCAGCTCACCGAGGTGGGAACCATGAACATCTTTGTC TACTGGACCCACGAAGATGGGGTGCTGGAGCTGGTGACGCCCCCGCTGAATGGTGTTATC CTGCCTGGAGTGGTCAGACAGAGTCTACTGGACATGGCTCAGACCTGGGGTGAGTTCCGG GTGGTGGAGCGCACGATCACCATGAAGCAGTTGCTGCGGGCCCTGGAGGAGGGCCGCGTG CGGGAAGTCTTTGGCTCGGGCACCGCTTGCCAGGTCTGCCCAGTGCACCGAATCCTGTAC AAAGACAGGAACCTCCACATTCCCACCATGGAAAATGGGCCTGAGCTGATCCTCCGCTTC CAGAAGGAGCTGAAGGAGATCCAGTACGGAATCAGAGCCCACGAGTGGATGTTCCCGGTG TGA
- Chromosome Location
- 19
- Locus
- 19q13
- External Identifiers
Resource Link UniProtKB ID O15382 UniProtKB Entry Name BCAT2_HUMAN GenBank Protein ID 2342862 GenBank Gene ID U68418 GenAtlas ID BCAT2 HGNC ID HGNC:977 - General References
- Bledsoe RK, Dawson PA, Hutson SM: Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm). Biochim Biophys Acta. 1997 Apr 25;1339(1):9-13. [Article]
- Than NG, Sumegi B, Than GN, Bellyei S, Bohn H: Molecular cloning and characterization of placental tissue protein 18 (PP18a)/human mitochondrial branched-chain aminotransferase (BCATm) and its novel alternatively spliced PP18b variant. Placenta. 2001 Feb-Mar;22(2-3):235-43. [Article]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [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]
- Eden A, Simchen G, Benvenisty N: Two yeast homologs of ECA39, a target for c-Myc regulation, code for cytosolic and mitochondrial branched-chain amino acid aminotransferases. J Biol Chem. 1996 Aug 23;271(34):20242-5. [Article]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [Article]
- Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
- Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]
- Yennawar N, Dunbar J, Conway M, Hutson S, Farber G: The structure of human mitochondrial branched-chain aminotransferase. Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):506-15. [Article]
- Yennawar NH, Conway ME, Yennawar HP, Farber GK, Hutson SM: Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms. Biochemistry. 2002 Oct 1;41(39):11592-601. [Article]
- Goto M, Miyahara I, Hirotsu K, Conway M, Yennawar N, Islam MM, Hutson SM: Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin. J Biol Chem. 2005 Nov 4;280(44):37246-56. Epub 2005 Sep 1. [Article]
- Yennawar NH, Islam MM, Conway M, Wallin R, Hutson SM: Human mitochondrial branched chain aminotransferase isozyme: structural role of the CXXC center in catalysis. J Biol Chem. 2006 Dec 22;281(51):39660-71. Epub 2006 Oct 18. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB00167 Isoleucine investigational, nutraceutical unknown Details DB02142 Pyridoxamine-5'-Phosphate experimental unknown Details DB02635 N-[O-Phosphono-Pyridoxyl]-Isoleucine experimental unknown Details DB04074 alpha-Ketoisovalerate experimental unknown Details DB00114 Pyridoxal phosphate approved, investigational, nutraceutical unknown cofactor Details DB00142 Glutamic acid approved, nutraceutical unknown Details DB00149 Leucine investigational, nutraceutical unknown Details