Cloned (Comment) | Organism |
---|---|
gene BAT1, overexpression in Saccharomyces cerevisiae taz1DELTA mutant strain | Saccharomyces cerevisiae |
gene BAT2, overexpression in Saccharomyces cerevisiae taz1DELTA mutant strain | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Saccharomyces cerevisiae | 5829 | - |
mitochondrion | - |
Saccharomyces cerevisiae | 5739 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-leucine + 2-oxoglutarate | Saccharomyces cerevisiae | - |
4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | Saccharomyces cerevisiae ATCC 204508 | - |
4-methyl-2-oxopentanoate + L-glutamate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P38891 | - |
- |
Saccharomyces cerevisiae | P47176 | - |
- |
Saccharomyces cerevisiae ATCC 204508 | P38891 | - |
- |
Saccharomyces cerevisiae ATCC 204508 | P47176 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-leucine + 2-oxoglutarate | - |
Saccharomyces cerevisiae | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | - |
Saccharomyces cerevisiae ATCC 204508 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r |
Synonyms | Comment | Organism |
---|---|---|
Bat1 | - |
Saccharomyces cerevisiae |
BAT2 | - |
Saccharomyces cerevisiae |
BcaT | - |
Saccharomyces cerevisiae |
BCAT1 | - |
Saccharomyces cerevisiae |
Bcat2 | - |
Saccharomyces cerevisiae |
branched-chain amino acid aminotransferase | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
malfunction | mutation of BCATs results in perturbed TCA-cycle intermediate levels, which in turn lead to reduced ATP levels and inhibition of TORC1 | Saccharomyces cerevisiae |
physiological function | isozyme BCAT1 is a suppressor of the taz1DELTA growth defect in yeast cells. Abolishing yeast Taz1 results in decreased total CL amounts, increased levels of MLCL, and mitochondrial dysfunction. The mitochondrial dysfunction leads to the Barth syndrome (BTHS), a metabolic and neuromuscular disorder. But elevated levels of Bat1 (BCAT1) or Bat2 (BCAT2) do not restore the reduced membrane potential, altered stability of respiratory complexes, or the defective accumulation of MLCL species in yeast taz1DELTA cells. Multi-copy suppressor screening. The growth defect rescue in both yeast and mammalian taz1-defective cells with the two different BCAT isoforms is similar. In both cell types, the mitochondrial isoform has a higher rescue capacity. Hence, although the mitochondrial and cytosolic isoforms have overlapping functions in transamination reactions, it appears that their products are required more in mitochondria and that they are not completely free to equilibrate between the matrix of mitochondria and the cytosol. Bat1 has been reported to interact with the TCA cycle enzyme aconitase | Saccharomyces cerevisiae |
physiological function | isozyme BCAT2 is a suppressor of the taz1DELTA growth defect in yeast cells. Abolishing yeast Taz1 results in decreased total CL amounts, increased levels of MLCL, and mitochondrial dysfunction. The mitochondrial dysfunction leads to the Barth syndrome (BTHS), a metabolic and neuromuscular disorder. But elevated levels of isozymes Bat1 (BCAT1) or Bat2 (BCAT2) do not restore the reduced membrane potential, altered stability of respiratory complexes, or the defective accumulation of MLCL species in yeast taz1DELTA cells. Multi-copy suppressor screening. The growth defect rescue in both yeast and mammalian taz1-defective cells with the two different BCAT isoforms is similar. In both cell types, the mitochondrial isoform has a higher rescue capacity. Hence, although the mitochondrial and cytosolic isoforms have overlapping functions in transamination reactions, it appears that their products are required more in mitochondria and that they are not completely free to equilibrate between the matrix of mitochondria and the cytosol | Saccharomyces cerevisiae |