EC Number   |
Protein Variants |
Reference |
|---|
   3.4.23.B2 | D25N |
totally inactive mutant enzyme, incapable of autoprocessing |
647805 |
| 3.4.23.B2 | K69H |
the isoelectric point of the mutant enzyme is pH 7.0 compared to that of the wild-type enzyme of 7.4. The purified mutant enzyme is less soluble at low pH when concentrating sample in preparation for crystallization |
647805 |
| 3.4.23.B2 | more |
generation of an protease-inactive mutant of SIVmac239, the phosphorylation pattern of the mutant Pr55Gag protein is unaltered compared to the wild-type, overview |
670087 |
| 3.4.23.B2 | more |
it is demonstrated that the SIVmac239 Pr55Gag isoform, SIV p43, suppresses proteolytic cleavage of Pr55Gag by viral protease |
682974 |
| 3.4.23.B2 | S4H |
mutation does not significantly affect the kinetic parameters of the enzyme but stabilizes it approximately 4fold to autolysis. Crystals of the variant SIV PR S4H appear to have the same morphology as those obtained from wild-type enzyme |
647818 |
| 3.4.23.B2 | S4H |
site-directed mutagenesis, the mutation of the major autodegeneration site stabilizes the enzyme without significantly affecting the kinetic parameters |
668793 |
