EC Number   |
Protein Variants |
Reference |
|---|
    4.1.2.8 | D60N |
site-directed mutagenesis, substitution of asparagine for aspartic acid in the alphaAsp60Asn variant. alphaAsp60 has an essential role in stabilizing charge development on the IGP indole ring during C-C bond scission |
695226 |
| 4.1.2.8 | Q114N |
betaGln114Asn mutation, which shortens the betaGln114 side chain connecting the betaL3 loop with the rest of the protein, resulted in two fractions of enzyme |
691963 |
| 4.1.2.8 | T183V |
site-directed mutagenesis, substitution of valine for threonine in the alphaThr183Val variant, resulting in impaired catalysis at the alpha-site and loss of allosteric communication |
695226 |
| 4.1.2.8 | up |
PtINS has about two to fivefolds higher transcript level than that of PtTSA (tryptophan synthase alpha-subunit). After treatment with 2,1,3-benzothiadiazole the relative transcript level of PtINS (indole synthase) over PtTSA (tryptophan synthase alpha-subunit) is significantly enhanced in the plant |
748938 |
| 4.1.2.8 | Y110V |
betaThr110Val mutation, which replaces a hydrogen bonding partner to the substrate carboxylate with a methyl group severely decreased the ability to form the aminoacrylate external aldimine E(AA) and consequently severely impaired beta-reaction and alphabeta-reaction |
691963 |
