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BAT2  -  branched-chain-amino-acid transaminase BAT2

Saccharomyces cerevisiae S288c

Synonyms: BCAT, Branched-chain-amino-acid aminotransferase, cytosolic, ECA40, J2209, Protein TWT2, ...
 
 
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High impact information on BAT2

  • Mitochondria and cytosol isolated from bat1 and bat2 deletion mutants, respectively, contained largely reduced activities for the conversion of branched-chain 2-ketoacids to their corresponding amino acids [1].
  • ECA39 is highly expressed during log phase and is down-regulated during the stationary phase of growth, while ECA40 shows an inverse pattern of gene expression [2].
  • We suggest that BCAT is a target for c-Myc activity and discuss the evolutionary conservation of prokaryotic and eukaryotic BCATs and their possible involvement in regulation of cell proliferation [2].
  • Analysis of a null mutant of the BAT2 gene encoding cytosolic branched-chain amino acid aminotransferase, and a transformant with multi-copy plasmids containing the BAT2 gene showed that the BAT2 gene product plays an important role in the production of branched-chain alcohols and isoamyl acetate [3].
  • First of all, as propanol is synthesised from alpha-ketobutyrate, the first metabolic intermediate in the anabolic pathway of isoleucine, neither the eca39 nor eca40 mutations have any effect on the production of this higher alcohol [4].
 

Biological context of BAT2

 

Anatomical context of BAT2

  • A highly homologous protein, Bat2p, of 376 amino acid residues was found in the cytosol [1].
 

Associations of BAT2 with chemical compounds

  • Therefore we conclude that the expression of BAT2 is essential for 3-methyl-1-butanol formation on the non-fermentable carbon source, ethanol [5].
  • On the other hand, it can be concluded that the eca40 mutation has a drastic effect on the production of isobutanol [4].

References

  1. Mitochondrial and cytosolic branched-chain amino acid transaminases from yeast, homologs of the myc oncogene-regulated Eca39 protein. Kispal, G., Steiner, H., Court, D.A., Rolinski, B., Lill, R. J. Biol. Chem. (1996) [Pubmed]
  2. Two yeast homologs of ECA39, a target for c-Myc regulation, code for cytosolic and mitochondrial branched-chain amino acid aminotransferases. Eden, A., Simchen, G., Benvenisty, N. J. Biol. Chem. (1996) [Pubmed]
  3. Genetic and physiological analysis of branched-chain alcohols and isoamyl acetate production in Saccharomyces cerevisiae. Yoshimoto, H., Fukushige, T., Yonezawa, T., Sone, H. Appl. Microbiol. Biotechnol. (2002) [Pubmed]
  4. Involvement of branched-chain amino acid aminotransferases in the production of fusel alcohols during fermentation in yeast. Eden, A., Van Nedervelde, L., Drukker, M., Benvenisty, N., Debourg, A. Appl. Microbiol. Biotechnol. (2001) [Pubmed]
  5. Bat2p is essential in Saccharomyces cerevisiae for fusel alcohol production on the non-fermentable carbon source ethanol. Schoondermark-Stolk, S.A., Tabernero, M., Chapman, J., Ter Schure, E.G., Verrips, C.T., Verkleij, A.J., Boonstra, J. FEMS Yeast Res. (2005) [Pubmed]
 
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