EC Number   |
Protein Variants |
Reference |
|---|
   3.4.14.4 | R510K |
mutation detected in human cancer, substitution mildly decreases enzyme activity for Arg-Arg-2-naphtylamide substrate |
755384 |
| 3.4.14.4 | R510Q |
mutation detected in human cancer, strong decrease in activity |
755384 |
| 3.4.14.4 | R510W |
mutation detected in human cancer, almost abolishes activity. Mutation significantly increases the enzyme flexibility, particularly that of the binding site including the H450ELLGH455 motif, and influences the substrate interactions with the catalytic His568 |
755384 |
| 3.4.14.4 | R582Q |
mutant exhibits an order of magnitude higher activity with all four dipeptide derivatives examined, compared to the wild type, due to a change in the H-bond networking in the R582Q variant active-site region |
732012 |
| 3.4.14.4 | S504G |
mutation in S2 subsite, mutant does not show decreased binding of peptides with N-terminal arginine |
731407 |
| 3.4.14.4 | W300F |
mutant with slight increase in activity compared to wild-type enzyme |
707660 |
| 3.4.14.4 | W300L |
mutant with higher activity compared to wild-type enzyme |
707660 |
| 3.4.14.4 | Y318F |
the potential functional role of the well-conserved tyrosine 318 residue in the active center of human DPP III is investigated |
683209 |
| 3.4.14.4 | Y395F |
the potential functional role of the well-conserved tyrosine 395 residue in the active center of human DPP III is investigated |
683209 |
| 3.4.14.4 | Y644F |
the potential functional role of the well-conserved tyrosine 644 residue in the active center of human DPP III is investigated |
683209 |
