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Literature summary for 2.6.1.42 extracted from

  • Kingsbury, J.M.; Sen, N.D.; Cardenas, M.E.
    Branched-chain aminotransferases control TORC1 signaling in Saccharomyces cerevisiae (2015), PLoS Genet., 11, e1005714.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.6.1.42

Protein Variants

Protein Variants Comment Organism
K219A mutation in conserved pyridoxal phosphate-binding site, loss of activity. Mutant is nearly as effective aswild-type Bat1 or Bat2 at partially suppressing the rapamycin recovery and TORC1 activity defects of the Bat1 bat2 mutant Saccharomyces cerevisiae
K219R mutation in conserved pyridoxal phosphate-binding site, loss of activity. Mutant is nearly as effective aswild-type Bat1 or Bat2 at partially suppressing the rapamycin recovery and TORC1 activity defects of the Bat1 bat2 mutant Saccharomyces cerevisiae

Localization

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Synonyms

Synonyms Comment Organism
Bat1
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function branched-chain aminotransferase yeast mutants exhibit severely compromised target of rapamycin complex TORC1 activity, which is partially restored by expression of isoofrm Bat1 active site mutants, implicating both catalytic and structural roles of branched-chain aminotransferases in TORC1 control. Bat1 interacts with branched-chain amino acid metabolic enzymes and, in a leucine-dependent fashion, with the tricarboxylic acid-cycle enzyme aconitase. Branched-chain aminotransferase mutation perturbs tricarboxylic acid-cycle intermediate levels, consistent with a tricarboxylic acid-cycle block, and results in low ATP levels, activation of AMPK, and TORC1 inhibition Saccharomyces cerevisiae