Salahaddin-University-Erbil

College of Education
Chemistry Department

Enzyme Catalysis

Supervisor Student
 Dr.Adil H.Ibrahim. .Zanyar Jabar
Class: 3rd Stage

CONTENTS

What is enzyme..?

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 Types of Enzyme.

Enzyme Functions.

Rate Limiting Step with Enzyme.

Mechanism of Enzyme Catalysis.

Enzyme Catalysis with Temperature and PH.

How Enzymes Speed Up the Chemical Reactions.

Michaelis-Menten Kinetics.

Summary

References.

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What is enzyme..?

Enzymes are biological catalysts. They are specific to one type of reaction
and to one or a small group of reactants called substrates. A catalyst speeds
up the rate of a reaction without being changed itself. They are necessary as
most biological and organic reactions which are taking place in the body of
animals and plants, indeed they are very slow.
Most enzymes are proteins, and Within the enzyme, generally catalysis
occurs at a localized site, called the active site. this is the region of an
enzyme where substrate molecules bind in order to undergo a chemical
reaction. The active site consists of amino acid residues.
Most enzymes are globular proteins with the exception of a few RNA
enzymes (ribozymes). They have an active site made up of a few amino
acids.

Types of Enzyme

According to the International Union of Biochemists (I U B), enzymes are

divided into six functional classes and are classified based on the type of
reaction in which they are used to catalyze. The six types of enzymes are:

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 1. Oxidoreductases.

2. Transferases.

3. Hydrolases

4. Lyases.

5. Isomerases.

6. Ligases.

Enzyme Functions.

Enzymes lower the activation energy, Ea, of a particular reaction. They can
do this because they have a high affinity for a transition state.
The activation energy is the minimum energy needed for a reaction to
occur. Enzymes assist in the reaction so that less energy is needed. This
means the reaction can occur more easily. This speeds up the rate of the
reaction as it allows the product to be formed faster.

An enzyme has a high affinity for the transition state (even higher than for

its substrate). Therefore when the substrate binds, it is quickly forced into
the transition state. This is a state that exists between the substrate and the
product. The enzyme is said to facilitate the formation of the transition
state.

The transition state has a high energy, making it very unstable. It can only
exist transiently. The transition state spontaneously turns into the
more stable product with lower energy. The enzyme will have a low affinity
for the product and so the product is released.

Rate Limiting Step

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 The rate limiting step in any reaction is its slowest step. It sets the pace for
the entire reaction. After all, a production line can only be as productive as
its slowest worker. In enzymatic reactions, the conversion of the enzyme-
substrate complex to the product is normally rate limiting. The rate of this
step (and therefore the entire enzymatic reaction) is directly proportional
to the concentration of ES.

The concentration of ES changes as the reaction progresses. Therefore, the

rate of product formation also changes over time. When the reaction
reaches equilibrium (steady state) the concentration of ES (and therefore
the rate) remains relatively constant.

Mechanism of Enzyme Catalysis.

[(NH2, COOH, SH, OH)] are termed as Active centers. The molecules of
substrate which have complementary shape, fit into these cavities just as
key fits into a lock (Lock-and-Key theory). By virtue of the presence of
active groups, the enzyme forms an activated complex with the substrate
which at once decomposes to yield the products. Thus the substrate
molecules enters the cavities, forms complex and reacts, and at once the
products get out of the cavities. Michaelis and Menten (1913) proposed the
following mechanism for enzyme catalysis

E+S ES ⎯⎯→ P + E

Complex Where E = enzyme; S = substrate (reactant); ES = activated

complex; P = product.

Examples of Enzyme Catalysis

Some common examples of the biochemical reactions catalyzed by
enzymes are:

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Enzyme Catalysis with Temperature

The rate of an enzyme catalyzed reaction is increased with the

rise of temperature but up to a certain point. Thereafter the
enzyme is denatured as its protein structure is gradually
destroyed.

Thus the rate of reaction drops and eventually becomes zero

when the enzyme is completely destroyed. The rate of an enzyme
reaction with raising of temperature gives a bell-shaped curve.
The temperature at which the reaction rate is maximum is called
the optimum temperature, as in below:

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For example, the optimum temperatures, of enzyme reactions
occurring in human body is 37°C (98.6°F). At much higher
temperatures, all physiological reactions will cease due to loss of
enzymatic activity. This is one reason why high body temperature
(fever) is very dangerous.

Enzyme Catalysis with PH

The rates of enzyme-catalyzed reactions vary with pH and often

pass through a maximum as the pH is varied. If the enzyme obeys
Michaelis-Menten kinetics the kinetic parameters k0 and kA often
behave similarly. The pH at which the rate or a suitable parameter
is a maximum is called the pH optimum and the plot of rate or
parameter against pH is called a pH profile. Neither the pH
optimum nor the pH profile of an enzyme has any absolute
significance and both may vary according to which parameter is
plotted and according to the conditions of the measurements.

Each enzyme has an optimum pH but it also has a working range

of pH values at which it will still work well. This depends on the
type of enzyme.

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 There are optimum PHs of some enzymes

How Enzymes Speed Up the Chemical Reactions.

Like all catalysts, enzymes work by lowering the activation energy of

chemical reactions. Activation energy is the energy needed to start a
chemical reaction. This is illustrated in Figure below. The biochemical
reaction shown in the figure requires about three times as much activation
energy without the enzyme as it does with the enzyme.
Enzymes generally lower activation energy by reducing the energy needed
for reactants to come together and react. For example:

 Enzymes bring reactants together so they don’t have to expend energy

moving about until they collide at random. Enzymes bind both reactant
molecules (called the substrate), tightly and specifically, at a site on the
enzyme molecule called the active site.
 By binding reactants at the active site, enzymes also position reactants
correctly, so they do not have to overcome intermolecular forces that
would otherwise push them apart. This allows the molecules to interact
with less energy.
 Enzymes may also allow reactions to occur by different pathways that
have lower activation energy.

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Michaelis-Menten Kinetics.

Michaelis–Menten kinetics is one of the best-known models of enzyme

kinetics. It is named after German biochemist Leonor Michaelis and
Canadian physician Maud Menten. The model takes the form of an equation
describing the rate of enzymatic reactions, by relating reaction rate which
is equal to (rate of formation of product) to (the concentration of a
substrate), its formula is given by:

.This equation concerns the steady state (which means equilibrium, in here
Enzyme-Substrate remains constant, It is formed as quickly as it breaks
down, but Constant rate of formation is fast.) of an enzymatic reaction with
one substrate
.Two terms that are important within Michaelis-Menten Kinetics are:
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 Vmax – the maximum rate of reaction when all enzyme active sites are
saturated with substrate
 Km – the substrate concentration that gives half maximal velocity. Km is a
measure of the affinity an enzyme has for its substrate, as a lower Km
means that less of the substrate is required to reach half of Vmax.

It describes how the initial rate of reaction, V0, is affected by the initial
substrate concentration, [S]0. It only looks at the start of the reaction. This
allows it to ignore the reverse reaction where substrate is formed from
product. This is because at the start of the reaction there is no product
present to become substrate.

Summary

In order for a reaction to occur, reactant molecules must contain sufficient

energy to cross a potential energy barrier, the activation energy. All
molecules possess varying amounts of energy depending, for example, on
their recent collision history but, generally, only a few have sufficient
energy for reaction. The lower the potential energy barrier to reaction, the
more reactants have sufficient energy and, hence, the faster the reaction
will occur. All catalysts, including enzymes, function by forming a
transition state, with the reactants, of lower free energy than would be
found in the unanalyzed reaction

There are a number of mechanisms by which this activation energy

decrease may be achieved. The most important of these involves the
enzyme initially binding the substrate(s), in the correct orientation to
react, close to the catalytic groups on the active enzyme complex and any
other substrates. In this way the binding energy is used partially in order
to reduce the contribution of the considerable activation entropy, due to
the loss of the reactants' (and catalytic groups') translational and
rotational entropy, towards the total activation energy. Other contributing
factors are the introduction of strain into the reactants (allowing more
binding energy to be available for the transition state), provision of an
alternative reactive pathway and the desolation of reacting and catalyzing
ionic groups.

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Reference

 ESSENTIALS OF PHYSICAL CHEMISTRY Arun Bahi, B.S.Bahi, G.D .

 PHYSICAL CHEMISTRY Atkins
 PHYSICAL CHEMISTRY ROBERT A. ALBERTY
 MODERN ELECTROCHEMISTRY J.O.M, BOCKRIS/A.K.N
 CHEMICAL PRINCIPLES STEVENE
 ELECTROCHEMISTRY STEPHEN. K. LOWER
 PHYSICAL CHEMISTRY IRA N. LEVINE

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