structural analysis indicates that proteins of the aromatic-amino-acid aminotransferase family have conserved structural elements that might play a role in substrate binding. Streptococcus mutans AroAT (SmAroAT) belongs to the type I folding group of PLP-dependent aminotransferases
structural analysis indicates that proteins of the aromatic-amino-acid aminotransferase family have conserved structural elements that might play a role in substrate binding. Streptococcus mutans AroAT (SmAroAT) belongs to the type I folding group of PLP-dependent aminotransferases
structural analysis indicates that proteins of the aromatic-amino-acid aminotransferase family have conserved structural elements that might play a role in substrate binding. Streptococcus mutans AroAT (SmAroAT) belongs to the type I folding group of PLP-dependent aminotransferases
inhibition of transaminase enzymes by (aminooxy)acetate (AOA), a broad-spectrum inhibitor of pyridoxal phosphate-dependent enzymatic reactions, strongly inhibits the growth of Candida albicans in minimal medium with selected amino acids as the sole nitrogen source in an amino acid concentration-dependent manner
inhibition of transaminase enzymes by (aminooxy)acetate (AOA), a broad-spectrum inhibitor of pyridoxal phosphate-dependent enzymatic reactions, strongly inhibits the growth of Candida albicans in minimal medium with selected amino acids as the sole nitrogen source in an amino acid concentration-dependent manner
the enzyme CaAro9p participates in the catabolism of aromatic amino acids and lysine at high concentrations of these compounds, with no biosynthetic role
the enzyme CaAro9p participates in the catabolism of aromatic amino acids and lysine at high concentrations of these compounds, with no biosynthetic role
production of indole-3-acetic acid in the gene disruption mutant is not significantly reduced compared to the activity of the wild-type strain. Aromatic amino acid aminotransferase-1 activity is reduced by 50% when tyrosine is used as the amino acid donor, whereas there is a 30% reduction when tryptophan is used, compared to the activity of the wild-type strain
ISS1 mutant plants, but not wild-type, use primarily Trp-I indole-3-pyruvic acid synthesis when grown on indole-supplemented medium. In contrast, both ISS1 mutants and wild-type use primarily Trp-D indole-3-pyruvic acid synthesis when grown on unsupplemented medium. Iss1 mutant seedlings produce 8-fold higher levels of indole-3-pyruvic acid when grown on indole and have a 174fold increase in Trp in young seedling
mutation in Aro8 leads to substantial changes in the absolute and relative intracellular concentrations of amino acids. Deletion of Aro8 leads to de novo production of phenylethanol during growth on a glucose synthetic medium with ammonium as the sole nitrogen source. The mutation also stimulates phenylethanol production when combined with other mutations that deregulate aromatic amino acid biosynthesis
production of indole-3-acetic acid in the gene disruption mutant is not significantly reduced compared to the activity of the wild-type strain. Aromatic amino acid aminotransferase-1 activity is reduced by 50% when tyrosine is used as the amino acid donor, whereas there is a 30% reduction when tryptophan is used, compared to the activity of the wild-type strain