EC Number   |
Protein Variants |
Reference |
|---|
   4.1.1.105 | G351A |
site-directed saturation mutagenesis, the mutant shows additional activity with phenolic substrates |
-, 744703 |
| 4.1.1.105 | G351I |
site-directed saturation mutagenesis, the mutant shows additional activity with phenolic substrates |
-, 744703 |
| 4.1.1.105 | G351L |
site-directed saturation mutagenesis, the mutant shows additional 3,4-dihydroxy-L-phenylalanine (L-DOPA) decarboxylase activity, and G351L shows approximately twelvefold and fivefold increases in Km values for L-tryptophan and 5-hydroxy-L-tryptophan compared to wild-type, as well as increased values for L-tyrosine and L-DOPA (2.44 and 3.4 mM), respectively |
-, 744703 |
| 4.1.1.105 | G351L |
the mutation adds L-tyrosine and 3,4-dihydroxy-L-phenylalanine decarboxylase activity while retaining stereospecificity and L-tryptophan decarboxylase activity compared to the wild type enzyme |
744703 |
| 4.1.1.105 | G351S |
site-directed saturation mutagenesis, the mutant shows additional L-tyrosine decarboxylase activity while retaining stereospecificity and L-tryptophan decarboxylase activity |
-, 744703 |
| 4.1.1.105 | G351S |
the mutation adds L-tyrosine and 3,4-dihydroxy-L-phenylalanine decarboxylase activity while retaining stereospecificity and L-tryptophan decarboxylase activity compared to the wild type enzyme |
744703 |
| 4.1.1.105 | G351V |
site-directed saturation mutagenesis, the mutant shows additional L-tyrosine decarboxylase activity while retaining stereospecificity and L-tryptophan decarboxylase activity |
744703 |
| 4.1.1.105 | more |
except for G351T, all engineered variants are opened for phenolic substrates compared to wild-type enzyme. Neither of the engineered enzymes turns over L-phenylalanine, L-histidine, or D-amino acids |
-, 744703 |
