EC Number   |
Protein Variants |
Reference |
|---|
   1.4.1.20 | D126N |
mutant without enzymatic activity |
699079 |
| 1.4.1.20 | D209G |
mutant named 1stA7, active with DL-propargylglycine |
699079 |
| 1.4.1.20 | D209G/Q18H/I336F |
mutant named 1stA7/1stB6, active with DL-propargylglycine |
699079 |
| 1.4.1.20 | E313G |
mutant named H7H10, active with DL-propargylglycine |
699079 |
| 1.4.1.20 | F110Y/G124C/G293A |
mutant named H14A12, active with DL-propargylglycine |
699079 |
| 1.4.1.20 | F124M/V125S/H126I/A127I/A128Y/R129Q |
the catalytic efficiencies of the mutant enzyme with aliphatic amino acids and aliphatic keto acids as substrates are 0.5% to 2% of that of the wild-type enzyme. The efficiencies for L-Phe and phenylpyruvate decreases to 0.0008% and 0.035% of that of the wild-type enzyme, respectively. Enzyme exists as monomeric or dimeric form, compared to wild-type enzyme which exists as hexameric enzyme form. Thermostability is lowered by mutation |
349649 |
| 1.4.1.20 | G124A |
12% of wild-type kcat with L-phenylalanine |
655468 |
| 1.4.1.20 | G124A |
mutant enzyme has lower activity towards L-Phe and enhanced activity towards almost all aliphatic amino acid substrates compared to the wild-type |
349654 |
| 1.4.1.20 | G124A |
mutant named 9F5, active with DL-propargylglycine |
699079 |
| 1.4.1.20 | G124A/E313G |
mutant named 25B12, active with DL-propargylglycine |
699079 |
