How do enzymes speed up chemical reactions?

An enzyme is a protein catalyst that alters the rate of a chemical reaction without being used up in
the reaction itself. In enzymatic reactions the molecules at the beginning of the process, called
substrates are converted into different molecules, called products.

Every chemical reaction involves the breaking and forming of bonds and this requires energy. The
activation energy is defined as the initial energy required to start the reaction. In most chemical
reactions this is provided in the form of heat. The human body temperature is 37°C. Enzymes
provide the activation energy for reactions to proceed at normal temperatures in biological systems.
Enzymes catalyse reactions by lowering the activation energy, enabling the reactant molecules to
absorb enough energy to reach the transition state even at moderate temperatures. Enzymes can
only hasten reactions that would eventually occur anyway, that is, reactions in which ΔG is negative
(spontaneous).

Enzymes are substrate specific. The specificity of an enzyme for its substrate results from the shape
of an enzyme. This is due to a compatible fit between the active site of an enzyme and the substrate.
The enzyme binds to its substrate forming an enzyme-substrate complex. When the substrate and
the enzyme are joined the catalytic action of the enzymes converts the substrate to the product.

Active Site

The active site is the catalytic centre of the enzyme and it is typically a pocket or groove on the
surface of the enzyme. It is usually formed from only a few amino acids and it is not rigid. The side
chains of the amino acids in the enzyme interact with the chemical groups of the substrate. This
causes the enzyme to change shape and fit even better around the substrate. This is known as
induced fit. Induced fit brings the chemical groups of the active site into new positions thereby
enhancing the ability of the enzymes to catalyse the reaction.

Mechanisms Used By Enzymes to Lower the Activation Energy

Most metabolic reactions are reversible and the enzyme can catalyse either the forward or
backward reaction, depending on which direction has a negative ΔG.

Enzymes use a variety of different methods to lower the activation energy and speed up a reaction.

First, in reactions involving two or more reactants the active site provides a template on which the
substrates can come together in the proper orientation for a reaction to occur between them.

Second, as the active site of an enzyme clutches the bound substrate, the enzyme may stretch the
substrate towards their transition-state form, stressing and bending critical chemical bonds that
must be broken during the reaction. The activation energy is proportional to the difficulty of
breaking the bonds, so distorting the substrate helps it to approach the transition state and thus
reduces the amount of energy that must be absorbed to achieve that state.
Third, the active site may also provide a microenvironment that is more conductive to a particular
type of enzyme than the solution itself would be without the enzyme. For example if the active site
contains amino acids with acidic R groups, the active site may be a pocket of low pH in an otherwise
neutral cell. In such cases the acidic amino acid may facilitate H + transfer to the substrate as a key
step in catalysing the reaction.

A fourth mechanism of catalysis is the direct participation of the active site in the chemical reaction.
Sometimes this process even involves brief covalent bonds being formed between the substrate and
the side chain of an amino acid of the enzyme. Subsequent steps of the reaction restore the side
chains to their original states, so that the active site is the same after the reaction as it was before.

Rate of Catalysis

The rate at which a particular amount of enzyme converts a substrate to a product is partly a
function of the initial concentration of the substrate. The more substrate molecules that are
available, the more frequently they access the active sites of the enzyme molecules. However, there
is a limit to how fast the reaction can be pushed by adding more substrate to a fixed concentration
of enzymes. At some point the concentration of substrate will be high enough that all the enzyme
molecules will have their active sites engaged. As soon as the product exits an active site another
substrate molecule will enter. At this substrate concentration the enzyme is said to be saturated,
and the rate of the reaction is determined by the speed at which the active site converts substrate to
product. When an enzyme population is saturated the only way to increase the rate of product
formation is to add more enzymes.