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Gene Review

BAT1  -  branched-chain-amino-acid transaminase BAT1

Saccharomyces cerevisiae S288c

Synonyms: BCAT, Branched-chain-amino-acid aminotransferase, mitochondrial, ECA39, Protein ECA39, Protein TWT1, ...
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High impact information on BAT1

  • An overview of the layered controls of the extended leucine pathway is provided that includes a description of the newly recognized roles of Ilv5p and Bat1p in maintaining mitochondrial integrity [1].
  • Both Bat proteins show striking similarity to the mammalian protein Eca39, which is one of the few known targets of the myc oncogene [2].
  • However, the promoter region of the yeast ECA39 harbors several Gcn4 binding elements [3].
  • The tissue specific expression of human ECA39 during embryogenesis is similar to that of the mouse homolog [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 BAT1

  • The data show that, with the exception of a slow growth phenotype observed for the BAT1 deletion strain, the fermentation behaviour of the strains was unaffected by the modifications [5].

Associations of BAT1 with chemical compounds

  • We found that the LEU1, LEU2, and BAT1 genes were up-regulated in TFL20 for metabolism, and that TFL20 simultaneously produced as much i-AmOH and leucine as K30 does [6].


  1. Leucine biosynthesis in fungi: entering metabolism through the back door. Kohlhaw, G.B. Microbiol. Mol. Biol. Rev. (2003) [Pubmed]
  2. 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]
  3. ECA39 is regulated by c-Myc in human and by a Jun/Fos homolog, Gcn4, in yeast. Ben-Yosef, T., Yanuka, O., Benvenisty, N. Oncogene (1996) [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. The effect of increased branched-chain amino acid transaminase activity in yeast on the production of higher alcohols and on the flavour profiles of wine and distillates. Lilly, M., Bauer, F.F., Styger, G., Lambrechts, M.G., Pretorius, I.S. FEMS Yeast Res. (2006) [Pubmed]
  6. Properties of a trifluoroleucine-resistant mutant of Saccharomyces cerevisiae. Oba, T., Yamamoto, Y., Nomiyama, S., Suenaga, H., Muta, S., Tashiro, K., Kuhara, S. Biosci. Biotechnol. Biochem. (2006) [Pubmed]
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