proximity and orientation

Substrate binding has additional effects that enhance reaction rates, among which proximity and orientation gives the most obvious increase. There are two characteristics of enzyme-substrate binding, where the first one is that the binding brings together substrates and the reactive groups on the active site of the enzyme. The second one is that active site in the enzyme is extremely specific in the substrates, therefore making the reaction as efficient as possible. Proximity and orientation in enzyme-substrate interactions could align the reactive chemical groups and make them come together in an optimal orientation with the proper spatial relationship for a reaction to occur. Once the substrates are fixed this way, the enzymatic reaction behaves kinetically like an intramolecular process. It has been suggested that molecules are maximally reactive when their orbitals are aligned so the electronic energy of the transition state is minimized. The fewer nonproductive ways two groups are oriented, the faster they will react.

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