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The theory of enzyme-substrate complex was established by Michaelis and Menton in 1913.According to their theory,enzyme combines with substrate to form enzyme-substrate complex.The transient complex has a lower energy of activation than that of substrate alone.This results in the acceleration of the reaction.The enzyme-substrate complex is broken down into enzyme and products of the reaction.
E+S -ES - - -ES - - -E+P
The different hypotheses of enzyme-substrate complex formation have been postulated.Early theory was postulated by Emil Fischer.According to this theory,the catalytic site of enzyme is preshaped to fit of the substrate.This hypothesis is called "lock and key" or rigid template.The next hypothesis has been proposed by Koshland in the late 1950s.The hypothesis was called "induced fit".Acccording to this theory,a catalytically active configuration of enzyme molecule and that of the active site can be induced only at the moment of attachment of the substate molecule,that is the substrate induces a conformotional change in the enzyme.
At the present time,model of "induced fit" is modified.Binding the substrate with the enzyme leads not only to the conformational change of the protein molecule,but also to a geometrical and electrontopographic rearrangement of the substrate molecules.
The modern "induced fit" hypothesis presumes the existence between the enzyme and the substrate of not only spatial or geometrical complementarity,but also electrostatic charge complementarity.
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