Biochemistry (Nursing)

Module #11 Student Activity Sheet

Name: _________________________________________________________________ Class number: _______

Section: ____________ Schedule: ________________________________________ Date: ________________

Lesson title: ENZYMES (Mechanism and Factors Influencing Materials: Book, pen and notebook
of Enzymatic Action, Clinical Enzymology)
Learning Targets: References:
At the end of the module, students will be able to: Espino-Cabatit (1988) Biochemistry 12th ed.
1. Describe the mechanism of action of enzymes; UST Press, Manila
2. Identify and explain the factors that affect enzyme activity;
and, Moore, J. T., & Langley, R. H. (2011).
3. Describe the medical applications of enzymes. Biochemistry For Dummies, 2nd Edition. In
Director.

Vasudevan, D. (1395). Textbook of

BIOCHEMISTRY for Medical Students (7th
Editio). Jaypee Brothers MedicalL Publishers
(P) LTD.

Tyler, V.E., L.R. Brady and J.E. Roberts,

Pharmacognosy 9th ed. Lea and Febiger,
Philadephia

A. LESSON PREVIEW / REVIEW

As previously learned from the last session, How does papaya whiten the skin?

Discuss your answer:

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B. MAIN LESSON

MODE OF ENZYME ACTION:

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 Biochemistry (Nursing)
Module #11 Student Activity Sheet

Name: _________________________________________________________________ Class number: _______

Section: ____________ Schedule: ________________________________________ Date: ________________

1. The surface of the substrate contacts a specific region of the surface of the enzyme molecule called active sites
2. A temporary intermediate compound forms, called an enzyme-substrate complex
3. The substrate is then transformed into products.
4. the products are released.
5. The enzyme is recovered unchanged
*Activation Energy: the minimum amount of energy that is required to activate atoms or molecules to a condition in
which they can undergo chemical transformation or physical transport.

THEORIES EXPLAINING THE MODE OF ENZYME ACTION

I. FISCHER’S LOCK AND KEY THEORY

● Enzyme – substrate (F-5) complex theory
1. The active site of the enzyme and substrate have complementary structures, hence they fit together as
a key fits a lock
2. While they are bounded in the enzyme-substrate complex, catalytic reaction occurs
3. The products of the reaction leave the surface of the enzyme & combine with another molecule of the
substrate
Examples:
General Reaction:
1. E + S == E – S complex
!"#$%#&'()*+,##-#).'/0&1#2#+345(+
Eg.
1. sucrase + sucrose == sucrase – sucrose complex
2. sucrase- sucrose complex == glucose + fructose + sucrose

II. KOSHLAND'S INDUCED FIT THEORY

● In this model, the substrate still needs to fit into the enzyme like a key, but instead of simply fitting into the
“keyhole,” some type of modification is induced in the substrate, enzyme, or both. The modification begins
the process of the reaction.
● At first, substrate binds to a specific part of the enzyme. This leads to more secondary binding and
conformational changes. The substrate induces conformational changes in the enzyme, such that precise
orientation of catalytic groups is effected

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 Biochemistry (Nursing)
Module #11 Student Activity Sheet

Name: _________________________________________________________________ Class number: _______

Section: ____________ Schedule: ________________________________________ Date: ________________

FACTORS THAT INFLUENCE EZNZYME ACTION:

1. Concentration of substrate
● 6#&'3&+31.718'3#'9#:0;:1.71+#<#6#+345(+#7&18'3
2. Concentration of enzyme
● 6#&'3&+31.718'3#'9#+345(+#<#6#+345(+#7&18'3
3. Temperature
● Optimum temperature of enzyme in the body = 37°C
● With each 10°C rise in temperature usually doubles or triples reaction rate
● Rapid inactivation of the enzyme occurs at temperatures much above body temperature
● Low temperatures slow down the action of enzyme but do not destroy them
4. pH
● each enzyme has its specific optimum pH at which it exerts its maximum activity
● it loses activity rapidly on either side of this opt.
Eg. Pepsin – 1.5 to 2.2
Lactase – 5.7
Trypsin – 7.8
5. Presence of accelerators
● Activate the enzyme
Eg. Metallic ions such as Ferrous, Ferric, Co, Mn, Mg, Mo
6. Presence of inhibitors
● Have the ability to combine with enzyme in a reversible and irreversible reaction and hence block enzyme
catalysis
Eg. Antibiotics – streptomycin
Antienzymes – antitrypsin from soybeans
Antimetabolites – sulfanilamide
Others (Poisons/Drugs) – formaldehyde, chloroform, CCl4, cyanides, heavy metals like Ag and Hg
7. Environmental hazards
Eg. 1. Hg (mercury)
a. Hg from phenyl mercuric acetate
o Fungicide to prevent cellulose from rotting
b. Methyl mercuric acetate
o Prevent rotting of seed grains
2. Cd (cadmium)
o Derived from cigarette smoke
o 1 pack = 15 mcg
3. Pb (lead)
o Present in gasoline
o Yellow-painted pencils

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 Biochemistry (Nursing)
Module #11 Student Activity Sheet

Name: _________________________________________________________________ Class number: _______

Section: ____________ Schedule: ________________________________________ Date: ________________

CLINICAL ENZYMOLOGY:
● Enzymes are commonly used in medicine as:
1. Analytical tools or reagents in measuring quantities of various constituents in biologic fluids
Eg. Urease, alcohol dehydrogenase
Enzyme Used for Testing
Urease Urea
Uricase Uric acid
Glucose Oxidase Glucose
Cholesterol oxidase Cholesterol
Lipase Triglycerides
Reverse Transcriptase Polymerase Chain Reaction

2. As index for pathology of diseases:

Eg. of some serum enzymes:
● α – amylase in pancreatitis – normal serum level is elevated
● =8)7:+#>#6#83#7&01+#)73&.+71818:?#)+.9'.71+/#/0'/+37*#73/#)+)18&#0*&+.:#73/#831+:1837*#';:1.0&18'3"#
● @.+718383+#AB':)B'C837:+#D@AEF#>#6#83#;*''/#791+.#GH
o It is a sensitive indicator in the early stages of myocardial ischemia.
o Three CK isoenzymes
▪ MM(CK3) – found in skeletal and heart muscle
▪ MM(CK2) – found in heart muscle
▪ BB(CK1) – found in the brain
● I*C7*83+#AB':)B717:+#>#6#83#.8&C+1:?#';:1.0&18J+#K703/8&+?#&8..B':8:#73/#&B'*+:17:8:
● I&8/#AB':)B717:+#L#6#83#&7.&83'(7#'9#1B+#).':171+#'.#).':171+#&73&+.
● =7&17:+#/+B5/.'M+37:+#D=NOF#>#6#83#J8.7*#B+7)?#B+7.1#73/#:C+*+17*#(0:&*+#/8:+7:+
● I:)7.171+#1.73:7(837:+#DI%PF#>#6#83#(5'&7./87*#8397.&18'3
● I*7383+#1.73:7(837:+#DI=PF#>#6#83#*8J+.#/8:+7:+#D*8J+.#&+**#/7(7M+F
● Q*017(5*#1.73:9+.7:+#>#6#83#*8J+.#/8:+7:+?#;8*87.5#';:1.0&18'3DM7**:1'3+#9'.(718'3F?#73/#7*&'B'*8:(
● 5’ Nucleotidase – Moderately increased in hepatitis and highly elevated in biliary obstruction.

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 Biochemistry (Nursing)
Module #11 Student Activity Sheet

Name: _________________________________________________________________ Class number: _______

Section: ____________ Schedule: ________________________________________ Date: ________________

CHECK FOR UNDERSTANDING

You will answer and rationalize this by yourself. This will be recorded as your quiz. One (1) point will be given to correct
answer and another one (1) point for the correct ratio. Superimpositions or erasures in you answer/ratio is not allowed. You
are given 20 minutes for this activity:

1. To overcome an energy barrier between reactants and products, energy must be provided to get the reaction started.
This energy, which is recovered as the reaction proceeds, is called:
A. Potential energy D. Activation energy
B. Initiation energy E. Kinetic energy
C. Reaction energy
ANSWER: ________
RATIO:___________________________________________________________________________________________
_________________________________________________________________________________________________
2. The following statements are correct about reaction rate, EXCEPT:
I. Reaction rates are not sensitive to temperature.
II. Enzymes can accelerate the rate of a reaction.
III. Reaction rate is the speed at which the reaction proceeds toward equilibrium
IV. Reaction rate is governed by the energy barrier between reactions and products
A. I only D. III only
B. I and II E. None of the choice
C. I and IV
ANSWER: ________
RATIO:___________________________________________________________________________________________
_________________________________________________________________________________________________
3. Koshland in 1959 proposed
A. Fluid mosaic model C. Lock and Key model
B. Induced fit model D. Reflective Index model

ANSWER: ________
RATIO:___________________________________________________________________________________________
_________________________________________________________________________________________________
4. In case of induced fit model
A. The substrate changes its shape slightly C. None of them changes shape
B. The enzyme changes its shape slightly D. Both changes shape

ANSWER: ________
RATIO:___________________________________________________________________________________________
_________________________________________________________________________________________________
5. Enzyme and a reactant molecule relationship can be described as:
A. Non complementary binding
B. A permanent mutual alteration of structure
C. One in which the enzyme is changed permanently
D. A temporary association
E. An association stabilized by covalent bond

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 Biochemistry (Nursing)
Module #11 Student Activity Sheet

Name: _________________________________________________________________ Class number: _______

Section: ____________ Schedule: ________________________________________ Date: ________________

ANSWER: ________
RATIO:___________________________________________________________________________________________
_________________________________________________________________________________________________

For 6 to 10. Answer the question accordingly.

How do pH and temperature affect enzymatic action?

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 Biochemistry (Nursing)
Module #11 Student Activity Sheet

Name: _________________________________________________________________ Class number: _______

Section: ____________ Schedule: ________________________________________ Date: ________________

C. LESSON WRAP-UP

ONE-SENTENCE SUMMARY

Write one sentence summary on how do enzymes work.

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