Introduction

Enzymes are very important molecules for cell functioning and continuity . An enzyme is a
protein molecule in the cell structure which helps to biologically increase the rates of certain
cellular reactions by decreasing the activation energy required for a reaction to occur (Raven
& Johnson, 1999). Enzymes can also be referred to as biological catalysts. Cell regulation
and expression are important processes for the normal/predictable cell growth; hence the rates
of the processes that occur within the cells must be controlled. The cells control the rates of
cellular reactions through enzyme-catalysis.
Biologically, some reactions which occur within the cell need to be slowed down and
sometimes some need to be prohibited completely in order to prevent abnormal cell growth
and malfunction. Since enzymes control the reaction kinetics within the cells; enzyme
inhibition/deactivation is the term which is frequently used to describe this process (Bailey &
Ollis, 1986). Enzyme inhibition can occur through the addition of substances (inhibitors)
which deactivates the enzyme and hence reducing the rate of the reaction or preventing the
process completely.
There are two types of enzyme inhibition mechanisms which affect cell growth (Ball, Scott &
Hill,2012 )

Reversible enzyme inhibition

Irreversible enzyme inhibition

Reversible enzyme inhibition

Competitive inhibition occurs when enzyme inhibitors binds themselves on the active site of
the enzyme thus denying the substrate(s) access to the enzymes active site hence the reaction
rate is decreased. The inhibitor and substrate are so similar that they compete for the same
active site on the enzyme. Competitive inhibition is reversible because the bond between the
inhibitor and the substrate is a non-covalent bond i.e. no electrons are shared between the
inhibitor and the enzyme, the interaction is purely electromagnetic (Ball, Scott & Hill, 2012).
In order to counteract the competitive enzyme inhibition, the concentration of the substrate(s)
is increased in order to increase the probability of the substrate(s) to reach the active site of
the enzyme before the inhibitor does.
Non-competitive inhibition
The inhibitor attaches itself on the enzymes at any location other than the active site hence
altering the shape of the enzyme so that the substrate cannot bind with the enzyme thus the
reaction is inhibited. The locations on the enzyme at which the inhibitor attaches itself on are
called allosteric sites. Increasing the concentration of the substrate(s) will not have any effect
on the reaction kinetics since the shape of the enzyme is completely changed (Raven &
Johnson, 1999).

Irreversible enzyme inhibition

The irreversible type of enzyme inhibition is similar to the reversible competitive enzyme
inhibition ; the only difference is that with the in the irreversible enzyme inhibition, the
bond between the enzyme and the inhibitor is a covalent bond in which electrons are shared
between the two species in the enzyme s active site( Hence Ball, Scott & Hill,2012) . The
covalent bonds holding the enzyme-inhibitor complex together is so strong that even high
concentrations of substrate(s) will not reverse the inhibition. The irreversible enzyme
inhibitors are hence described as poisons.
References
1. Bailey, J.E. & Ollis, D.F. (1986). Biochemical Engineering Fundamentals (2 nd ed.).
New York: McGraw-Hill Co.
2. Ball, D.W., Hill, J.W., Scott, R.J. (2012). Introduction to Chemistry: General,
Organic, Biological,(v.01). United States of America
3. Raven, H. P. & Johnson, G.B. (1999). Biology (5th ed.). Boston: The McGraw-Hill