EC Number   |
General Information |
Reference |
|---|
    2.6.1.57 | evolution |
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 |
-, 758603 |
| 2.6.1.57 | malfunction |
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 |
-, 759287 |
| 2.6.1.57 | metabolism |
enzyme CaAro8p is involved in the catabolism of histidine, lysine, and aromatic amino acids as well as in L-Lys, L-Phe, and L-Tyr biosynthesis |
-, 759287 |
| 2.6.1.57 | metabolism |
enzyme Cayer152Cp is active with aromatic amino acids but does not play an important role in vivo in aromatic acid catabolism and biosynthesis |
-, 759287 |
| 2.6.1.57 | metabolism |
the enzyme CaAro9p participates in the catabolism of aromatic amino acids and lysine at high concentrations of these compounds, with no biosynthetic role |
-, 759287 |
| 2.6.1.57 | more |
homology modeling of the AroH structure using the structure of Saccharomyces cerevisiae Aro8 (PDB ID 4JE5) as template |
759250 |
| 2.6.1.57 | physiological function |
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 |
738333 |
| 2.6.1.57 | physiological function |
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 |
739763 |
| 2.6.1.57 | physiological function |
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 |
-, 723490 |
| 2.6.1.57 | physiological function |
RNAi suppression of the enzyme decreases 2-phenylethanol production |
723053 |
