General
Principles
For a given enzyme concentration and for relatively low substrate
concentrations, the reaction rate increases linearly with substrate
concentration; the enzyme molecules are largely free to catalyse
the reaction, and increasing substrate concentration means an
increasing rate at which the enzyme and substrate molecules
encounter one another.
However, at relatively high substrate concentrations, the reaction
rate asymptotically approaches the theoretical maximum; the
enzyme active sites are almost all occupied by substrates
resulting in saturation, and the reaction rate is determined by the
intrinsic turnover rate of the enzyme.
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