Unit 6: Enzymes

1.0. Introduction

This unit will be focusing on enzymes as a large biological globular protein molecule whose role as catalyst assist
in facilitation of specific reactions within the cell that are essential for the all life-forms from viruses to man.

2.0 Learning Outcomes

At the end of this topic students should be able to:

i. describe what enzymes are.

ii. describe mode of enzyme action; and
iii. enumerate important properties of enzymes.

3.0 MAIN CONTENTS

3.1: What are enzymes

Enzymes are macromolecules, usually protein produced in living organisms an act as organic catalyst that speed up
chemical reactions, by lowering the activation energy, in the living organisms but themselves remain unchanged at
the end of the reaction.
It should be noted that activation energy is the energy required to make the substances react. As heat is often the
source of activation energy, enzymes often dispense with the need for this heat and so allow reactions to take place
at lower temperature (Fig. 1).

Fig. 1 Enzyme controlled reactions proceed 108 to 1011 times faster than corresponding non-enzymic reactions

Source: Image modified from "Potential, kinetic, free, and activation energy: ," by OpenStax College,
Biology, CC BY 3.0._ https://www.khanacademy.org/science/biology/energy-and-enzymes/introduction-to-
enzymes/a/enzymes-and-the-active-site
 In molecular terms, the enzyme combines with the substrate molecules to form an enzyme-substrate complex. In
such close contact the substrate molecules may be distorted and hence easily react to form an enzyme-product
complex which then split to release the product molecule and the enzyme. Enzymes are normally larger than the
substrate molecules they act upon. Only a small part of the enzyme molecule actually comes into contact with the
substrate. This region is called Active site.
It should be noted that the protein part of an active enzyme is called Apoenzyme, while the active enzyme that is
composed of apoenzyme and a co-factor is termed as Holoenzyme.

3.2: Mode of action of enzyme

The striking features or characteristics of enzymes are their catalytic power and specificity. Enzyme specificity is
better understood through the knowledge of enzyme active site (or substrate binding site). The active site of an
enzyme is typically a pocket or cleft in the three-dimensional structure of the enzyme.
The following are the features of active site
 The active site, as a region, is small compared to the rest of the protein.
 The active site is able to recognize and bind to the appropriate substrate molecule due to structural
complementarity between the substrate and binding site.
 Attractive forces involved in the recognition and binding of substrate include all the non-covalent
forces (van der Waals, hydrogen bonding, ionic interactions).
 Even small substrates bind to an enzyme via a combination of non-covalent interactions.

 "Lock and Key" versus "Induced Fit" hypotheses of substrate binding to explain mechanism of enzymatic actions

 The "Lock and Key" hypothesis of substrate binding was proposed by Emil Fischer (1890). It describes the
binding pocket as a rigid "lock" that is complementary to the substrate (i.e. the "key"). In this hypothesis,
there are no conformational changes upon substrate binding, and the protein enzyme is viewed as a rigid
structure.
 The "Induced Fit" hypothesis of substrate binding was proposed by Daniel Koshland (1959). It views the
binding of substrate as a structurally-interactive process. In other words, the protein structure is not viewed
as rigid, and the substrate binding site is not viewed as being exactly complementary to the substrate. The
binding of substrate slightly alters the active site structure, and likewise, the interaction with the active site
slightly alters the substrate structure.
o These structural changes may help to stabilize the transition state structure, and position catalytic
groups in the binding pocket to optimize the catalysis steps.
o The two models of substrate bindings is depicted below

Source https://www.mikeblaber.org/oldwine/BCH4053/Lecture26/Lecture26.htm
 Differences between lock and key and induced fit

Source of variation Induced fit Lock and key

Definition Explains the mode of enzyme – Explains the binding of perfectly
substrate binding when they are no matching substrate and enzyme with
complemantary in shape with each each other for a reaction
other
Shapes Shapes are not complementary Shapes are complementary with
before binding each other before binding
Nature of binding Active site is flexible Active site rigid
Proposed by Daniel E. Koshland Emil Fischer
Active site Not static Static
Source: https://www.differencebetween.com/difference-between-induced-fit-and-lock-and-key/

3.3: Properties of enzymes

1. It speeds up chemical reactions but remain undestroyed at the end of the reaction. i.e. it has the catalytic
properties.

2. It works in either direction. i.e. it catalyses the forward and backward reaction to the same extent. The direction in
which the reaction goes depends on the relative amounts of substrate and products present. The products are
continuously removed to maintain the reaction in living organism. e.g. A + B ↔C + D

3. An enzyme changes the rate only at which chemical equilibrium is reached; it does not affect the position of the
equilibrium.

4. An enzyme speeds up the rate of reaction by lowering the activation energy barrier.

5. It works rapidly and therefore is required in small quantity.

6. It is soluble in water and works in aqueous solution in living cells.

7. All enzymes operate only on specific substrates. Only substrates of particular shape will fit the active site of an
enzyme.

8. All enzymes are proteins, some may have other associated molecules.

9. Enzyme may be denatured by excessive heat, extreme pH or various chemicals. This is because enzymes are
soluble proteins. Such extremities or chemicals cause enzymes to coagulate by breaking down bonds in the molecule
making them insoluble. The molecular configuration of the active site is changed. Hence the enzyme can no longer
carry its catalytic function and is
said to be denatured. Such changed are irreversible. The phenomenon is known as denaturation.

10. The activity of an enzyme is affected by temperature.

11.Enzyme activity is affected by pH of the medium. It worked best at an optimum pH.

12.Some enzymes work efficiently only in the presence of appropriate co-factors

Note that co-factors is a non-protein substance which is essential for some enzymes to function efficiently.
There are three types
(a) Activators : are substances which are necessary for the functioning of certain enzymes. They may assist in
forming the E-S complex by moulding either the enzyme or substrate molecule into a more suitable
shape.e.g. (i) Enzyme thrombokinase, which converts prothrombin into thrombin during blood clotting, is
 activated by calcium ions ; (ii) Salivary amylase requires the presence of chloride ions before it converts
starch into maltose.
(b) Co-enzymes : are non-protein organic substances which are essential to the efficient functioning of some
enzymes, but are not themselves bound to the enzyme. Many coenzymes are derived from vitamins.e.g.
Nicotinamide adenine dinucleotide (NAD) act as a coenzyme to dehydrogenases by acting as a hydrogen
acceptor in the Krebs Cycle.
(c) Prosthetic groups : are organic , non-protein molecules and bound to the enzyme themselves.e.g. Haem is
an iron-containing prosthetic group. it may function as electron carrier and oxygen carrier in hemoglobin. It
is also found in catalases and peroxidases, which catalyse the decomposition of hydrogen peroxide to water
and oxygen.
4.0 Summary:

In this unit, you have learnt that

1. The need for enzyme in biological system

2. Mode of enzyme action
3. Properties of enzyme an relevance of co-factor for enzyme activity

5.0 Self – Assessment Questions.

1. Write concisely on concept of enzyme

2. Why are all enzymes are protein and not all protein are enzymes

6.0 Tutor Marked Assignment

1. Identify types of co-factors and briefly describe them. Of what importance are co-factors?
2. Enumerate important nature of enzymes in living cell.

7.0 References

1. Michael B. Enzyme specificity, Control of enzyme activity, Allosteric behavior. BCH Lecture Notes.
Retrieved from https://www.mikeblaber.org/oldwine/BCH4053/Lecture26/Lecture26.htm. Assessed on
line on 3rd Nov. 2019.

2. Khanacademy. Enzymes and the active site. Retrieved from

https://www.khanacademy.org/science/biology/energy-and-enzymes/introduction-to-enzymes/a/
enzymes-and-the-active-site Assessed on line on 3rd Nov. 2019.

3. Verma, V. (2009): Textbook of Plant Physiology. Published by Ane Books Pvt, Ltd. Darya Ganj, New
Delhi-110-002, India. Pp351-378.

8.0 Further reading

1. Dutta, A.C. (2009). Botany for Degree Students. Published by Oxford University Press,

New Delhi 110001.