EC Number   |
Protein Variants |
Reference |
|---|
   3.4.23.B5 | A57I |
mutation has a strong influence on substrate specificity |
647845 |
| 3.4.23.B5 | A57V |
99.7% of wild-type activity, 26.6% residual activity in presence of 1 microM amprenavir |
734565 |
| 3.4.23.B5 | C88T |
mutant enzyme shows an increased preference for hydrophobic amino acids at P4 and P2 position in a series of VSQNYPIVQ analogs |
647845 |
| 3.4.23.B5 | D32A |
construction of an active site mutant which is inactive and more stable to degradation during recombinant expression and purification |
-, 670761 |
| 3.4.23.B5 | E15R |
mutant enzyme shows similar kinetic parameters to that of the mutant enzyme |
647845 |
| 3.4.23.B5 | G541R |
size exclusion chromatography shows that the multimerization properties are similar among expressed wild-type and mutant ectodomain peptides. Circular dichroism measurements reveal decreased thermal stability of the G541R mutant as compared to wild-type. The G541R mutant also renders the peptide more susceptible to Lys-C protease cleavage. A monoclonal antibody does not bind to the G541R mutant peptide, suggesting a structural difference from wild-type |
682976 |
| 3.4.23.B5 | G60F |
mutant enzyme shows an increased preference for hydrophobic amino acids at P4 and P2 position in a series of VSQNYPIVQ analogs |
647845 |
| 3.4.23.B5 | H37D |
mutation has a strong influence on substrate specificity |
647845 |
| 3.4.23.B5 | K61L |
10.3% of wild-type activity, 95% residual activity in presence of 1 microM amprenavir |
734565 |
| 3.4.23.B5 | L92I |
mutant enzyme shows an increased preference for hydrophobic amino acids at P4 and P2 position in a series of VSQNYPIVQ analogs |
647845 |
