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Enzymes are protein catalysts and like all catalysts, speed up the rate of a chemical reaction without being used up in the process.

They achieve their effect by temporarily binding to the substrate and, in doing so, lowering the activation energy needed to convert it to a product.  

The rate at which an enzyme works is influenced by several factors, e.g.,

·          The concentration of substrate molecules (the more of them available, the quicker the enzyme molecules collide and bind with them).

·          The temperature. As the temperature rises, molecular motion - and hence collisions between enzyme and substrate - speed up. But as enzymes are proteins, there is an upper limit beyond which the enzyme becomes denatured and ineffective.

·          The presence of inhibitors.

·       Competitive inhibitors are molecules that bind to the same site as the substrate - preventing the substrate from binding as they do so - but are not changed by the enzyme.

·  Noncompetitive inhibitors are molecules that bind to some other site on the enzyme reducing its catalytic power.

·          pH. The conformation of a protein is influenced by pH and as enzyme activity is crucially dependent on its conformation, its activity is likewise affected. 

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