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B6db families: 2.6.1.42.a

2.6.1.42 a
Activity 2.6.1.42
Description Branched-chain amino acid aminotransferase (family a)
Notes A family of fold-type IV enzymes, possibly conserved in all domains of life (although a BCAT enzyme with Fold-type I has been described in Archaea, and used to build family 2.6.1.42_b)
PDB 1I1K;1EKF;1EKV;3UZO;4DQN:;
PLP Fold Type IV
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type IV

Reference sequence ILVE_ECOLI
Domain interval 12-290
Catalytic site 160 K
 
References
 Zheng X, Cui Y, Li T, Li R, Guo L, Li D, Wu B (2019) Biochemical and structural characterization of a highly active branched-chain amino acid aminotransferase from Pseudomonas sp. for efficient biosynthesis of chiral amino acids Appl Microbiol Biotechnol 103 8051-8062.

 Chen CD, Lin CH, Chuankhayan P, Huang YC, Hsieh YC, Huang TF, Guan HH, Liu MY, Chang WC, Chen CJ (2012) Crystal structures of complexes of the branched-chain aminotransferase from Deinococcus radiodurans with α-ketoisocaproate and L-glutamate suggest the radiation resistance of this enzyme for catalysis J Bacteriol 194 6206-16.

 Ruan J, Hu J, Yin A, Wu W, Cong X, Feng X, Li S (2012) Structure of the branched-chain aminotransferase from Streptococcus mutans Acta Crystallogr D Biol Crystallogr 68 996-1002.

 Maloney GS, Kochevenko A, Tieman DM, Tohge T, Krieger U, Zamir D, Taylor MG, Fernie AR, Klee HJ (2010) Characterization of the branched-chain amino acid aminotransferase enzyme family in tomato Plant Physiol 153 925-36.

 Schuster J, Binder S. (2005) The mitochondrial branched-chain aminotransferase (AtBCAT-1) is capable to initiate degradation of leucine, isoleucine and valine in almost all tissues in Arabidopsis thaliana Plant Mol Biol 57 241-54.

 Venos ES, Knodel MH, Radford CL, Berger BJ. (2004) Branched-chain amino acid aminotransferase and methionine formation in Mycobacterium tuberculosis BMC Microbiol 4 39.

 Berger, B.J.; English, S.; Chan, G.; Knodel, M.H. (2003) Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis J Bacteriol 185 2418-31.

 Madsen, S.M.; Beck, H.C.; Ravn, P.; Vrang, A.; Hansen, A.M.; Israelsen, H. (2002) Cloning and inactivation of a branched-chain-amino-acid aminotransferase gene from Staphylococcus carnosus and characterization of the enzyme Appl Environ Microbiol 68 4007-14.

 Yvon, M.; Chambellon, E.; Bolotin, A.; Roudot-Algaron, F. (2000) Characterization and role of the branched-chain aminotransferase (BcaT) isolated from Lactococcus lactis subsp. cremoris NCDO 763 Appl Environ Microbiol 66 571-7.

 Eden, A.; Benvenisty, N. (1998) Characterization of a branched-chain amino-acid aminotransferase from Schizosaccharomyces pombe Yeast 14 189-94.

 Bledsoe, R.K.; Dawson, P.A.; Hutson, S.M. (1997) Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm) Biochim Biophys Acta 1339 9-13.

 Feild MJ, Nguyen DC, Armstrong FB. (1989 ) Amino acid sequence of Salmonella typhimurium branched-chain amino acid aminotransferase Biochemistry 28 5306-10.

 Inoue, K.; Kuramitsu, S.; Aki, K.; Watanabe, Y.; Takagi, T.; Nishigai, M.; Ikai, A.; Kagamiyama, H. (1988) Branched-chain amino acid aminotransferase of Escherichia coli: overproduction and properties J Biochem (Tokyo) 104 777-84.

Articles on 2.6.1.42.a
last changed 2019/09/12 13:20

B6db families