Rational modification of enzyme catalysis by engineering surface charge.
Changing the surface charge of subtilisin by site-directed mutagenesis produces enzymes with significantly shifted pH-activity profiles, higher catalytic activities and altered specificities. Insight into water as a dielectric, the role of ions in electrostatic shielding and the field effects on catalysis is obtained and suggests rules for tailoring pH-activity profiles.
Russell
A J
AJ
Fersht
A R
AR
D002021:Buffers; D002384:Catalysis; D004560:Electricity; D006863:Hydrogen-Ion Concentration; D007477:Ions; D007700:Kinetics; D009154:Mutation; D009994:Osmolar Concentration; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013381:Subtilisins / Q000502:physiology*; D013499:Surface Properties
D002021:Buffers; D007477:Ions; D013381:Subtilisins