EC Number   |
Protein Variants |
Reference |
|---|
   3.4.13.9 | A195T/G306S |
mutation causes an increase in Tm-value of 0.1°C. Mutation causes an 1.7fold increase of the catalytic efficiency towards Leu-Pro |
-, 724145 |
| 3.4.13.9 | A212P |
naturally occuring mutation involved in prolidase deficiency |
707038 |
| 3.4.13.9 | D209A |
less than 0.1% enzymic activity, contains 0.7 Co per subunit, maximal activity with 0.5 mM Co2+, less than 20% residual activity with 10 mM Co2+ |
668623 |
| 3.4.13.9 | E127G/E252D |
mutation causes an decrease in Tm-value of 2.1°C. Mutation causes an 1.3fold increase of the catalytic efficiency towards Leu-Pro |
-, 724145 |
| 3.4.13.9 | E313L |
protein is highly misfolded, remains aggregated and recalcitrant during purification |
668623 |
| 3.4.13.9 | E327L |
no enzymic activity, contains 0.03 Co per sunbunit |
668623 |
| 3.4.13.9 | E36V |
mutation causes an increase in Tm-value of 0.6°C. Mutation causes an 1.1fold increase of the catalytic efficiency towards Leu-Pro |
-, 724145 |
| 3.4.13.9 | F822A |
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme |
680724 |
| 3.4.13.9 | G278D |
naturally occuring point mutation causing prolidase deficiency |
683061 |
| 3.4.13.9 | G39E |
at 35°C, 70°C and 100°C the mutant exhibits higher Vmax and kcat values than wild-type prolidase for Met-Pro. kcat/Km for Met-Pro is 70% of wild-type value at 35°C, kcat/Km for Met-Pro is 80% of wild-type value at 70°C, kcat/Km for Met-Pro is 1.2fold higher than wild-type value at 100°C. Relative specific activity towards Met-Pro at 100°C is 103% of wild-type activity. Relative specific activity towards Leu-Pro at 100°C is 85% of wild-type activity. Relative specific activity towards Phe-Pro at 100°C is 60% of wild-type activity. Relative specific activity towards Ala-Pro at 100°C is 35% of wild-type activity. Relative specific activity towards Gly-Pro at 100°C is 37% of wild-type activity. Relative specific activity towards Arg-Pro at 100°C is 132% of wild-type activity. Catalytic activity of the mutant enzyme has similar response to changes in pH as wild-type enzyme and shows optimal activity at pH 6.0, although the activity is 60% of wild-type activity |
707263 |
