EC Number   |
Protein Variants |
Reference |
|---|
   3.4.21.97 | A143Q/L229R |
mutant enzyme A143Q/L229R shows approximately a 20% decrease in helical content relative to the mutant enzyme A143Q, mutant enzyme A143Q/L229R has significant lower thermal stability than the mutant enzyme A143Q |
653320 |
| 3.4.21.97 | A143Q/L229R |
mutation has little effect on the stability of the dimer, significant lower thermal stability than the mutant enzyme A143Q. The ratio of turnover number to Km-value is 1826fold lower than that for mutant enzyme A143Q |
653320 |
| 3.4.21.97 | A143Q/R137E |
the ratio of turnover number to Km-value is 6.3fold lower than that for the wild-typelike mutant A143Q |
650227 |
| 3.4.21.97 | A143Q/R232H |
mutant enzyme A143Q/R232H essentially maintains wild-type catalytic activity, shows little change in the CD spectra compared to mutant A143Q enzyme, thermal stability is similar to that of mutant A143Q enzyme. The ratio of turnover number to Km-value is 5.1fold lower than that for mutant enzyme A143Q |
653320 |
| 3.4.21.97 | A143Q/S225Y |
mutant enzyme with large conformational changes with 40% lower helical content relative to the mutant enzyme A143Q, mutant dimer has similar stability to the mutant A143Q dimer. Many of the conformational differences between the mutant A143Q and the mutant enzyme A143Q/S225Y are likely the direct result of the mutation itself. alphaF helix tilts away from the wild type dimer two-fold axis in the S225Y mutant, creating a space near the two-fold axis to accomodate the new Tyr side chain. The S225Y mutation is the likely trigger for the change in the monomer conformation and the dimer organization, significant lower thermal stability than the mutant enzyme A143Q. The ratio of turnover number to Km-value is 1273fold lower than that for mutant enzyme A143Q |
653320 |
| 3.4.21.97 | A143Q/S225Y/L229R |
mutation has little effect on the stability of the dimer, mutant enzyme with large conformational changes with 40% lower helical content relative to the mutant enzyme A143Q, significant lower thermal stability than the mutant enzyme A143Q. The ratio of turnover number to Km-value is 1680fold lower than that for mutant enzyme A143Q |
653320 |
| 3.4.21.97 | A143T/A144T |
mutant displays better stability than wild-type and has esterase activity toward specific small ester compounds, e.g., Boc-L-Ala-4-nitrophenol |
732540 |
| 3.4.21.97 | A143V |
inability of the mutant virus to effect I-site cleavage in infected cells, mutation has no gross effect on the rate of virus production or on the amounts of extracellular virions, noninfectious enveloped particles and dense bodies |
653074 |
| 3.4.21.97 | H47A |
inactive mutant, active if coexpressed with AW5 which encodes the first 179 amino acids of assemblin with the addition of Ile, Gln, Thr |
95597 |
| 3.4.21.97 | H47A |
mutation prevents I-site cleavage (cleavage at an internal site of assemblin, converting it to a two-chain form that remain active). Imidazole restores I-site cleavage to mutant |
665654 |
