G238W |
study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol |
Bacillus thuringiensis |
G238W/W242A |
double mutant with enhanced activation and affinity for phosphatidylcholine interfaces above that of wild-type PI-PLC |
Bacillus thuringiensis |
G48W/W47A |
double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol |
Bacillus thuringiensis |
I43W/W47A |
double mutant with recovered kinetic interfacial activation, lower specific activity than wild-type PI-PLC |
Bacillus thuringiensis |
M49W/W47A |
double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol |
Bacillus thuringiensis |
additional information |
tryptophan rescue mutagenesis, reinsertion of a Trp at a different place in helix B in the W47A mutant or in the loop of the W242A mutant |
Bacillus thuringiensis |
N243W/W242A |
double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol |
Bacillus thuringiensis |
Q45W/W47A |
double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol |
Bacillus thuringiensis |
S236W/W242A |
double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol |
Bacillus thuringiensis |
W242A |
mutant with much weaker binding to interfaces and lower kinetic interfacial activation |
Bacillus thuringiensis |
W47A |
mutant with much weaker binding to interfaces and lower kinetic interfacial activation |
Bacillus thuringiensis |