Protein Variants | Comment | Organism |
---|---|---|
K202A | site-directed mutagenesis, inactive mutant | Saccharomyces cerevisiae |
K219A | site-directed mutagenesis, inactive mutant | Saccharomyces cerevisiae |
additional information | construction of two artificial genes encoding the mitochondrial-targeting signal (MTS)-deleted Bat1 (Bat1-MTS) and the MTS of Bat1-fused Bat2 (Bat2+MTS) from originating Bat1 and Bat2 genes. Bat2+MTS is relocalized into the mitochondria, because Bat2 localization is changed from cytosol to the mitochondria by addition of MTS, and can partially restore the valine content and growth in DELTAbat1DELTAbat2 cells. Bat1-MTS and Bat2+MTS function properly in DELTAbat1DELTAbat2 cells. Mutant DELTAbat1DELTAbat2 cells harboring Bat1-MTS grow similarly to DELTAbat1 cells | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Saccharomyces cerevisiae | 5829 | - |
mitochondrion | - |
Saccharomyces cerevisiae | 5739 | - |
additional information | subcellular localization of wild-type and mutant enzymes, overview | Saccharomyces cerevisiae | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-isoleucine + 2-oxoglutarate | Saccharomyces cerevisiae | - |
3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | Saccharomyces cerevisiae | - |
4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | Saccharomyces cerevisiae | - |
3-methyl-2-oxobutanoate + L-glutamate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P38891 | - |
- |
Saccharomyces cerevisiae | P47176 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-isoleucine + 2-oxoglutarate | - |
Saccharomyces cerevisiae | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | - |
Saccharomyces cerevisiae | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Saccharomyces cerevisiae | 3-methyl-2-oxobutanoate + L-glutamate | - |
r |
Subunits | Comment | Organism |
---|---|---|
homodimer | - |
Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
Bat1 | - |
Saccharomyces cerevisiae |
BAT2 | - |
Saccharomyces cerevisiae |
BcaT | - |
Saccharomyces cerevisiae |
branched-chain amino acid aminotransferase | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | PLP | Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
malfunction | yeast strains with a single gene disruption of BAT1 or BAT2 are constructed and only DELTAbat1 cells show the slow-growth phenotype. There is no mitochondrial localization in mutant Bat1-MTS, whereas mutant Bat2+MTS is relocalized into the mitochondria. Bat1 and Bat2 isozymes deletion mutants phenotype analysis and comparison, detailed overview | Saccharomyces cerevisiae |
malfunction | yeast strains with a single gene disruption of BAT1 or BAT2 are constructed and only DELTAbat1 cells show the slow-growth phenotype. There is no mitochondrial localization in mutant Bat1-MTS, whereas mutant Bat2+MTS is relocalized into the mitochondria. Bat1 and Bat2 isozymes deletion mutants phenotype analysis and comparison, detailed overview. The bat1 mutations affect valine but not leucine and isoleucine biosynthesis, lacking of Bat1 has the less effect on leucine biosynthesis | Saccharomyces cerevisiae |
metabolism | the enzyme is involved in the branched-chain amino acid biosynthesis. The mitochondria are the major site of valine biosynthesis, and mitochondrial BCAT, Bat1, is important for valine biosynthesis in Saccharomyces cerevisiae. Unlike in higher eukaryotes, the Saccharomyces cerevisiae BCATs, Bat1 and Bat2, can function in both anabolic and catabolic pathways as the final step in the biosynthesis and the first step in the degradation of BCAAs | Saccharomyces cerevisiae |
physiological function | isozymes Bat1 and Bat2 play distinct roles in branched-chain amino acid aminotransferase (BCAT) BCAAs biosynthesis | Saccharomyces cerevisiae |