CHAPTER 2

INHIBITION OF ENZYME REACTIONS

Disusun Oleh :
1. Ansori
2. Afifatul Jannah
3. Adelia Dwi Valentin
4. Novita Sari
Competitive • A competitive inhibitor normally combines reversibly
with enzyme. Therefore, the effect of the inhibitor can be

Inhibition minimized by increasing the substrate concentration,

unless the substrate concentration is
greater than the concentration at which the substrate
itself inhibits the reaction.
Mechanism of
competitive
inhibition
Mechanism of
competitive
inhibition
Mechanism
Mechanism of • Therefore, since KMI is larger than KS, the reaction
rate decreases due to the presence of inhibitor
competitive according to Eqn Eq. (2.48). It is interesting to note
inhibition that the maximum reaction rate is not affected by the
presence of a competitive inhibitor.
Non-competitive • Noncompetitive inhibitors interact with enzymes in
many different ways. They can bind to the enzymes
Inhibition reversibly or irreversibly at the active site or at
some other region. In any case the resultant complex is
inactive.
 Mechanism of • Since substrate and inhibitor do not compete for a
same site for the formation of enzyme-substrate or
non-competitive enzyme-inhibitor complex, we can assume
inhibition that the dissociation constant for the first equilibrium
reaction is the same as that of the third equilibrium
reaction, as
Mechanism
 Mechanism of • As shown in the previous section, the rate equation can
be derived by employing the Michaelis-Menten
non-competitive approach as follows:
inhibition

Therefore, the maximum reaction rate will be decreased

by the presence of a noncompetitive inhibitor, while the
Michaelis constant KS will not be affected by the inhibitor.
 Grafik of effect
inhibitor in plot
Langmur and
Lineweaver-Burk
 Other Beside the effect of various concentration, the
rate of an enzyme reaction is influenced by pH,
Influences temperature and shear.

on Enzyme
Activity
Effect of pH • The rate of an enzyme reaction is strongly influenced
by the pH. Every enzyme has its own optimum pH, it is
shown by Fig. 2.13.
Effect of pH 1. Enzyme is a protein which consist of amino acid
residues

Why?? 2. The amino acid residues possess basic, neutral, or

acid side groups which can be positively or negatively
charged at any pH.
Let’s consider glutamic acid, which is acidic in the lower pH
range. As the pH increased, glutamic acid is ionized as
Effect of pH

When CA- = , pH is equal to pK, that is equals to 4.5

Why?? In other hand, we have lysine, which is basic in the higher

pH range. As the pH decreased, lysine is ionized as

Similiarly, the pK value is 10 at which half of the residues are

ionized.
Effect of pH 3. An enzyme is catallytically active when the amino
acid residue at the active site each possess a
particular charge.therefore, the fracttion of the
catallytically active enzyme depends on the pH.
Then let’s suppose, if the residue of glutamic acid
and lysine is present at the active site of an enzyme

Why?? molecule, the charged form of both must be present

if thtat wnzyme molecule is to fuction. The enzyme
will be most active when 4.5 ≤ pH ≤ 10.0.
 Effect of • The rate of a chemical reaction depends on the
temperature according to Arrhenius equation as

Temperature k = A e−E RT
Consequently, when ln k is plotted versus 1/T, a straight
line with slope -E/R is obtained.
• An increase in the temperature increases the rate of
reaction, but the temperature is limited to the usual
biological range.
• High temperature can caused denaturation.
• For many proteins, denaturation begins to occur at 45
to 50°C.
• Some enzymes are very resistant to denaturation by
high temperature, especially the enzymes isolated
from thermophilic organisms found in certain hot
environments.
Effect of • Enzyme is susceptible to mechanical force,
that can cause denaturation. The mechanical
Shear force that normally encounters is fluid shear,
which generated either by flowing fluid,
shaking of vessel or stirring by an agitator.
• The effect of shear on stability of an enzyme
is important for reactor design.
• Charm and Wong (1970) showed that the
enzymes catalase, rennet, and
carboxypeptidase were partially inactivated
when subjected to shear in a coaxial cylinder
viscometer
• Thomas and Dunnill (1979) studied the effect
of shear on catalase and urease activities by
using a coaxial cylindrical viscometer that was
sealed to prevent any air-liquid contact, found
that there was no significant loss of enzyme
activity due to shear force alone at shear rates
up to 106 sec-1. they said that Charm and
Wong’s observation was the result of a
combination of shear, air-liquid interface, and
some other effects which are not fully
understood.
• Then Jones and Lee (1988 ) were confirmed,
as cellulose deactivation due to the interfacial
effect combined with the shear effect was
found to be far more severe and extensive
than that due to the shear effect alone.
Any Question??