14.enzymes-1 2

Enzymes
Learning objectives
By the end of this session, you are expected to be able
to:
1. Define the following terms (Enzymes, Catalyst, Coenzyme,
Cofactor, Activator, Substrate, Product, An inhibitor,
Competitive inhibitor, Non competitive inhibitor)
2. Describe the structure and function of enzymes including
structure that provides specificity
3. Explain the mechanism of action of enzymes including the
role of coenzymes and cofactors
4. Explain factors that affect enzyme activity including
temperature, substrate concentration and inhibitors
5. List the 6 types of enzymes using the common names
6. Discuss the use of enzymes in Medicine
Terms and definitions
 Enzymes are proteins that catalyze (accelerate)
chemical reactions. Sometimes they are called
biological catalysts.
 Enzymology is branch of science which deals with
the study of Enzymes
 Catalyst is a substance that increases the rate of a
chemical reaction but is not consumed or changed.
 Substrate is the reactant upon which an enzyme
reacts.
 Product is the substance produced by the enzyme-
catalyzed conversion of a substrate.
 Apoenzyme is an enzyme, often discussed as the
portion prior to bind with the associated cofactor.
 Coenzyme is an organic molecule that when combine
with an apoenzyme forms a complete enzyme called
holoenzyme.
 Cofactor is a non protein chemical compound that is
bound to a protein and is required for the protein’s
biological activity.
 Activator is an effector molecule that increases the
catalytic activity of an enzyme when it binds to a
specific site on the enzyme.
• Holoenzyme is the complete enzyme-cofactor

complex
 Activation energy is the energy required for a molecule
to form an activated complex or the minimum energy
required to start a chemical reaction.
 Allosteric effector is a small molecule that reacts
either with a non binding site of an enzyme molecule or
protein molecule and causes a change in the function of
the molecule.
 Prosthetic group is a cofactor that is so tightly bound
to the enzyme that is considered to be part of the
enzyme structure.
Introduction
• Enzymes are long, linear chains of amino acids
that fold to produce a three dimensional product.
• Each unique amino acid sequence produces a specific

structure, which has unique properties.
• Enzymes are biological catalysts that speed up a

chemical reaction.
Characteristics of enzymes
1.Speed up chemical reactions.
2. They are required in minute amounts.
3. They are highly specific in their action.
4. They are affected by temperature.
5. They are affected by pH.
6. Some catalyze reversible reactions.
7. Some require coenzymes.
8. They are inhibited by inhibitors.
Mechanism of action
• Enzyme functions by binding to one or more of the
reactants in a reaction. The reactants that bind to
the enzyme are known as the substrates of the
enzyme. Enzymes are substrate specific.
• The exact location on the enzyme where substrate

binding takes place is called the active site of the
enzyme. The shape of the active site just fits the
shape of the substrate, somewhat like a lock fits a
key. In this way only the correct substrate binds to
the enzyme.
 Once the substrate or substrates are bound to the
enzyme, the enzyme can promote the desired
reaction in some particular way. That way depends
on the nature of the reaction and the nature of the
enzyme.
• An enzyme may hold two substrate molecules in

precisely the orientation needed for the reaction to
occur
• Enzymes bind to substrates using two proposed
methods;
Lock and key model
Induced-Fit model
Lock and Key model
• The shape of protein allows enzymes and substrate
to fit.
• A specific enzyme is used for a specific reaction.
 This model explains enzyme specificity, but not all

properties of enzymes.
Diagram showing lock and key model
Induced-Fit model
• Substrate binds to the active site and induces a
change in shape of the active site so that is
complimentary fit.
• This is why some enzymes act on more than one

substrate.
• The general description of enzyme combining with
substrate to allow formation of product is
represented as: S + E  E-S  E + P
• Where S = substrate, E = enzyme, E-S = enzyme-

substrate complex and P= product
Factors affecting enzyme activity
1. Temperature
• All enzymes work within a range of temperature
specific to the organism.
• Increases in temperature generally lead to
increases in reaction rates and vice versa.
• There is a limit to the increase because higher
temperatures lead to a sharp decrease in reaction
rates.
• The optimum temperature should be considered and
used.
• Optimum temperature is the temperature at which

an enzyme shows its highest catalytic activity.
• The "optimum" temperature for human enzymes is

usually between 35 and 40 °C.
• The average temperature for humans is 37 °C.

2. pH
• Most enzymes are sensitive to pH and have specific
ranges of activity. All have an optimum pH.
• The pH can stop enzyme activity by denaturating

(altering) the three dimensional shape of the
enzyme by breaking ionic, and hydrogen bonds.
 Most enzymes function between a pH of 6 and 8;

however acid phosphatase works best at a pH of 2-
4 and alkaline phosphatase at a pH of 7-8.
3. Concentration of substrate and enzyme
• The rate of an enzyme-catalysed reaction depends
on the concentrations of enzyme and substrate.
• As the concentration of either is increased the rate

of reaction to produce product increases.
• For a given enzyme concentration, the rate of

reaction increases with increasing substrate
concentration up to a point.
4. Time
 Measurements are taken over time since the rate of
producing product is dependent on substrate
concentration which will decline as product is
produced.
 Analysis takes place when substrate is in excessive

and over a few minutes when Vmax is present.
5. Inhibition of enzyme activity
• Some substances reduce or even stop the catalytic
activity of enzymes in biochemical reactions. They
block or distort the active site. These chemicals are
called inhibitors, because they inhibit reaction.
• Enzyme inhibitors are substances which alter the

catalytic action of the enzyme and consequently
slow down, or in some cases, stop catalysis.
• There are three common types of enzyme inhibition;
1. competitive,
2. non-competitive
3. substrate inhibition.
• Inhibitors that occupy the active site and prevent a

substrate molecule from binding to the enzyme are
said to be active site-directed (or competitive)
Diagram showing competitive inhibition
• Inhibitors that attach to other parts of the enzyme
molecule, perhaps distorting its shape, are said to
be non-active site-directed (or non competitive).
• Substrate inhibition will sometimes occur when

excessive amounts of substrate are present. The
reaction velocity decreasing after the maximum
velocity has been reached.
Uncompetitive inhibition
• In uncompetitive inhibition the inhibitor can not bind
to the free enzyme, but only to the ES-complex.
• The EIS-complex thus formed is enzymatically

inactive. This type of inhibition is rare, but may
occur in multimeric enzymes.
Nomenclature of enzymes
• An enzyme's name is often derived from its

substrate or the chemical reaction it catalyzes, with
the word ending in -ase.
• Examples are amylase, urease, lipase
• Isoenzymes (or isozymes) are different enzymes

that catalyze the same reaction.
Classification of enzymes
• According to The International Union of
Biochemistry and Molecular Biology, enzymes are
divided into six functional classes;
1. Oxidoreductases
2. Lyases
3. Ligases
4. Isomerases
5. Transferases
6. Hydrolases
Uses of enzymes in medicine
 Enzyme levels in serum or other fluids can be used
to help in diagnosis of organ disease. For example,
serum ALT is used to monitor for inflammation of
the liver due to hepatitis or side effects from HIV
medications that may harm the liver.
• The laboratory uses enzymes in analysis of test such
as glucose oxidase for measuring patient’s glucose in
urine.
• Many inhibitors are used as pesticides or drugs.

Since an enzyme inhibitor is a molecule that binds to
enzymes and decreases their activity. For example
some HIV medications are used to block enzyme
activity of the human immunodeficiency virus.
Inhibitors have also been used to treat tumours and
malignancies
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Enzymes

• Holoenzyme is the complete enzyme-cofactor

• Each unique amino acid sequence produces a specific

• Enzymes are biological catalysts that speed up a

• The exact location on the enzyme where substrate

• An enzyme may hold two substrate molecules in

• A specific enzyme is used for a specific reaction.

 This model explains enzyme specificity, but not all

• This is why some enzymes act on more than one

• Where S = substrate, E = enzyme, E-S = enzyme-

• Optimum temperature is the temperature at which

• The "optimum" temperature for human enzymes is

• The average temperature for humans is 37 °C.

• The pH can stop enzyme activity by denaturating

 Most enzymes function between a pH of 6 and 8;

• As the concentration of either is increased the rate

• For a given enzyme concentration, the rate of

 Analysis takes place when substrate is in excessive

• Enzyme inhibitors are substances which alter the

• Inhibitors that occupy the active site and prevent a

• Substrate inhibition will sometimes occur when

• The EIS-complex thus formed is enzymatically

• An enzyme's name is often derived from its

• Isoenzymes (or isozymes) are different enzymes

• Many inhibitors are used as pesticides or drugs.

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