title: Theoretical analysis of compartmented coupling in linear enzyme systems.
abstract: Exact equations which describe the kinetic patterns of enzyme/enzyme complexes, when compartmented coupling occurs between them, are presented. Compartmented coupling refers to the creation of a local environment in which the concentration of an intermediate, shared by two enzymes, is higher than its solution concentration. This results in a higher coupling enzyme activity, a condition reflected in a shorter transition time for the system. In this paper, equations are presented which allow experimenters to quantitate the effect of compartmented coupling in terms of changes in the apparent Km and Vmax values. The equations presented in this paper are more exact than those previously derived since they do not incorporate first order assumptions before derivation.
authors.affiliation: Institute of Biochemistry, Carleton University, Ottawa, Ontario, Canada.
authors.forename: S P
authors.initials: SP
authors.lastname: Brooks
authors.forename: K B
authors.initials: KB
authors.lastname: Storey
authors.forename: C H
authors.initials: CH
authors.lastname: Suelter
mesh_terms: D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D009097:Multienzyme Complexes / Q000378:metabolism
chemical_list: D004798:Enzymes; D009097:Multienzyme Complexes