An investigation of the structure and function of antistaphylococcal endolysins using kinetic methods

Abstract

Peculiarities of the structures and functions of phage phi11 and phi80α antistaphylococcal endol ysins were investigated by kinetic measurements. In spite of the high level of homology in their primary struc tures, both enzymes possess some differences in their optimal conditions for functioning. As has been shown, phage phi11 endolysin is activated by metal cations (Ca 2+ , Mg 2+ ). Sulfhydril groups can play an important role in catalytic processes for both phage phi11 and phi80α endolysins.