EC Number   |
Protein Variants |
Reference |
|---|
   3.6.1.B17 | D284A/E285A |
site-directed mutagenesis, inactive mutant showing no ATP hydrolysis. A mutant NS3-hel carrying a two amino acid substitution (D284A-E285A) in the conserved motif II, which corresponds to the Mg2+ co-factor binding loop |
-, 735052 |
| 3.6.1.B17 | H51A |
site-directed mutagenesis, the mutation in the protease catalytic site abolishes autoproteolysis of the enzyme |
-, 735052 |
| 3.6.1.B17 | more |
construction of enzyme-deficient mutant rh57-1, the mutant is affected in the glucose metabolism and shows reduced function of protein synthesis, rh57-1 mutants show resistance to antibiotics, phenotypes, overview |
-, 734916 |
| 3.6.1.B17 | more |
generation of two recombinant variants of DENV NS3: the first single polypeptide mimics the NS2B-NS3 complex containing the full-length NS3 (618 amino acids) linked to the NS2B hydrophilic region (47 amino acids), this variant named NS3-FL, also carried a mutation in the protease catalytic site (H51A) to avoid autoproteolysis. The second variant NS3-hel represents a truncated NS3, containing the helicase domain (amino acids 171 to 618), ATPase/helicase defective NS3-hel mutant (NS3Amut) conserves the RNA annealing activity |
-, 735052 |
