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THE ENZYMES
INTRODUCTION
Early man observed the results of catalytic activity when he found fruit juices fermenting,
milk souring and meat spoiling. Nineteenth-century scientists noted that reactions that occur with
ease in the systems might never take place when the same reactor are stirred and brewed together
in a test tube. Enzymes as these vital forces, are now called are inseparable from living cells.
They are in fact protein molecules that exhibit extraordinary catalytic powers greater than that of
synthetic catalysts. They exhibit high degree of specificity and they function in dilute. aqueous
solutions under very mild conditions, temperature and pH. There are close to 2,000 known
enzymes but we shall not catalog them all. Rather, we shall survey the properties and
characteristics common to most enzymes.
LEARNING OUTCOMES
At the end of this unit, you should be able to:
discuss the general concept of chemical catalysis
describe the chemical nature of enzymes
enumerate the different types of enzymes, nomenclature and examples
discuss the factors that affect enzyme activity
explain enzyme kinetics using the Michaelis Menten model
explain and illustrate how KM and V can be used to characterize competitive
and non-competitive inhibition
discuss the significance of coenzymes to living systems
give examples of coenzymes
LEARNING CONTENTS
1. CATALYSTS
Most of us are quite sentimental about old notes and letters. We keep them with loving
care and try to relive the past through them every once in a while. Look at one of the oldest
letters you have that was written on white paper. Most likely it has begun to turn pale brown. If
you press it with a hot iron it will scorch to a darker brown. And if you leave the hot iron on it
long enough, it will even catch fire.
The paper which is actually cellulose began to burn as it was produced by plants. The
burning was not obvious; the change was so slow that there was no heat or light evident to
indicate that a reaction was really taking place. The heat of the iron merely hastened the change.
Catalysts speed up chemical reactions, too. They alter the speed of reactions without changing
the products that would have been formed in its absence. Of course, the iron did exactly that.
But there is something special about the catalyst. It is not used up as it changes the speed of the
reaction. It is not permanently changed to anything else. It is available to function all over once
again.
The effect of the catalyst is to lower the activation energy required for the reaction. In
our illustration in Fig. 5-1, less energy is needed to begin the reaction when a catalyst is present
and
3. ENZYME NOMENCLATURE
Consider this example
RCH2OH + coenzyme -----> RCHO + coenzyme-H2
To name the enzyme that catalyzes the above reaction we first name the substance the
enzyme acts on, in this case alcohol, then we indicate what the enzyme does and then we add the
suffix - ase thus the name of the enzyme for the above reaction is alcohol dehydrogenase
The enzyme molecule may consist of a fairly simple single polypeptide or it may be a
more complex molecule composed of several polypeptides and other nonprotein parts. There are
some special terms used in enzymology and it will be helpful if we define them first before we
continue. Take the case of a complex enzyme molecule cited earlier which consists of protein
part and a non-protein portion. The protein part of such an enzyme is called the apoenzyme and
the non-protein part, the smaller portion, the coenzyme or prosthetic group. Together the
apoenzyme and the coenzyme makeup the holoenzyme as illustrated in Fig 5-2
Effect of pH
Whereas the reaction rate is directly proportional to concentration of the reactant in a one
step reaction, there is a maximum rate (Vmax) in the case of first order catalyzed reaction. It
occurs because the enzyme becomes saturated with high concentration of substrate molecules.
This behavioral pattern may be explained by the following reaction sequence
E +S ↔E-S complex --→E + P
Where E and S are the enzyme and substrate respectively and E-S complex is the
necessary intermediate that must be formed before the product (P) is produced and the original
enzyme E is regenerated. Aside from the saturation phenomenon, the formation of the E-S
complex in an enzyme catalyzed reaction can also explain the following:
a. the means by which enzymes lower activation energy.
b. the specificity of an enzyme to its substrate - since E-S is a true molecule, then
specific chemical bonds are required between E and S which only the same E
and its true S can satisfy.
c. The relative amounts of E with respect to its S- since E is regenerated and can
be used again and again. Only a small amount of E is necessary to transform a
large amount of S to P.
The relation between reaction velocity and substrate concentration is expressed
mathematically by the Michaelis-Menten equation . The Michaelis constant, Km. is characteristic
of the particular enzyme.
Our bodies cannot synthesize these vitamins and they must be present in our diets in trace
amounts for proper metabolic activities. It goes without saying that the complex enzymes are
inactive without their coenzymes. This may be the molecular basis for the appearance of specific
deficiency diseases when vitamins are lacking in the diet.
SUMMARY
Enzymes are the largest group of biological proteins and they catalyze almost every
reaction that occurs in living organisms.
Enzymes just like any other catalyst hasten biochemical reactions by lowering the
activation energy of its reactant molecule known as substrate. But unlike other catalysts,
enzymes have a high degree of specificity, are efficient only within a narrow range of pH and at
an optimum temperature,
In an enzyme catalyzed reaction increasing the substrate concentration increases the
reaction rate until the active sites of the enzyme are saturated such that reaction rate levels off at
a Vmax value even at higher [S] concentrations. The [S] at which the reaction rate is half that of
Vmax is called the KM (Michaelis constant). Each enzyme displays a characteristics KM for its
substrate. The relationsthip between observed velocity v, Vmax, and KM is mathematically
expressed as the Michaelis-Menten equation
The two types of inhibition discussed are called competitive and noncompetitive. A
competitive inhibitor lowers the velocity of an enzyme-catalyzed reaction by competing with the
true substrate for the active site to form an enzyme inhibitor complex that is non-productive
Noncompetitive inhibitor on the otherhand interacts not with the active site but with another
region of the enzyme which nonetheless causes changes in the conformation of the enzyme
rendering it inactive. Allosterism is a special kind of non competitive Inhibition that is widely
observed as an effective regulation of enzymatic reactions in living organisms.
Vitamins are organic substances required in small amounts as coenzymes of some
complex enzymes. They are not synthesized in the body and must therefore be supplied in our
diets. Complex enzymes without their Vitamin coenzymes are inactive
KEY TERMS/CONCEPTS
Enzymes
Apoenzyme
Coenzyme
Active site
Positive effector
Negative effector
TEACHINGLEARNING ACTIVTIES
Activity 1
1. Enzyme Practice. Label the diagram
ASSESSMENT TASK
I. Answer the questions briefly
1. Define enzyme activity.
2. What effect does an enzyme have on the energy of activation of a reaction?
3. Explain the term optimal pH of an enzyme.
4 and 5. The optimal temperature for a given enzyme is 37 °C. What will probably happen to the
enzyme and its activity when (a) the temperature is lowered to 0 °C and (b) the
temperature is raised to 100 °C?
REFERENCES
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Hein, Morris (2005). Introduction to General, Organic and Biochemistry, John Wiley and Sons
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http://bcs.whfreeman..com./lehninger6e/#t_824263/
Voet, J. and Judith Voet. (2011) Biochemistry, 4th Edition. Wiley and Sons
Osmosis: https://www.youtube.com/watch?v=tpBAmzQ_pUE
A case study: Obesity and the metabolic syndrome. A three-pronged program, targeting
education, close follow-up and a dietary supplement, significantly decrease body weight and
body fat - DOI: 10.15761/IOD.1000143
Genetic medicines: treatment strategies for hereditary disorders - Timothy P. O'Connor &
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