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Literature summary for 2.6.1.42 extracted from

  • Antunes, D.; Chowdhury, A.; Aich, A.; Saladi, S.; Harpaz, N.; Stahl, M.; Schuldiner, M.; Herrmann, J.M.; Rehling, P.; Rapaport, D.
    Overexpression of branched-chain amino acid aminotransferases rescues the growth defects of cells lacking the Barth syndrome-related gene TAZ1 (2019), J. Mol. Med., 97, 269-279 .
    View publication on PubMed

Cloned(Commentary)

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

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Saccharomyces cerevisiae 5829
-
mitochondrion
-
Saccharomyces cerevisiae 5739
-

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P38891
-
-
Saccharomyces cerevisiae P47176
-
-
Saccharomyces cerevisiae ATCC 204508 P38891
-
-
Saccharomyces cerevisiae ATCC 204508 P47176
-
-

Substrates and Products (Substrate)

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

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

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Saccharomyces cerevisiae

General Information

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