Enzymes are thought to work by reducing the activation energy for a given equilibrium reaction. This may be via the formation of an intermediate state complex between enzyme and substrate. Enzyme kinetics deals with the way in which enzyme-catalyzed reactions are modified by variations in variables such as:
Some reactions do not obey the normal kinetic phenomena; binding of substrate at one site may alter the binding of further substrate at a second site on the same enzyme. This is an allosteric interaction resulting in co-operativity - one active site modulating the function, usually increasing the sensitivity, of another.
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