ENZYMES.

What are enzymes?

• They are protein catalysts that speed up the rate of a chemical
reaction without being used up in the process.
• They do not alter the chemical equilibrium between the reactants and
products.

Structure of an enzyme.
─Globular protein which is a tertiary structure.
─Consists an active site for substrate binding.
─Some enzymes contain a prosthetic group which can be a coenzyme or
a metal ion.
─Enzymes are named with a suffix –ase.
• Fig.1: Structure of an enzyme (Botnam, 2021).
Characteristic properties of enzymes.
∞Highly specific
∞Very efficient
∞Has active sites which are unique clefts.
∞Holoenzymes
∞Optimum temperature gives the maximum activity
∞Optimum pH gives the maximum activity.
∞Regulated activity
(Infinita Biotech, 2021).
Catalytic activity.
• Simple enzymatic reaction can be as follows:
E + S → [ES] → [EP] → E + P
E: enzyme
S: substrate
ES: enzyme-substrate complex
P: product
• Substrate acted upon the enzyme will be converted to
product in the reaction.
• The substrate must be converted to transition state for the
reaction to proceed. (Cooper, 2018).
• The catalytic activity of enzymes involves the binding of
their substrates to the active site to form an enzyme–
substrate complex.
• This results in lowering of the activation energy. (Cooper,
2018).
Fig.2: Enzymatic catalysis of a reaction between two substrates (Cooper,2018).
Lock and key hypothesis.
• Proposed by Emil Fischer in1894.
• Shape of the substrate and the active site of the enzyme fit
like a lock and key. (Aryal, 2018)
Fig.3: Lock and key model (Aryal, 2018).
Induced-fit hypothesis
• Proposed by Daniel E. Koshland, Jr., in 1958.
• States that binding of the substrate subjects enzyme’s
active site to undergo conformational changes.
Fig.4: Induced-fit model (Cooper,2018).
How enzyme lowers activation energy?
• Enzymes bring reactants together.
• Substrates are brought together in right orientation.
• ES complex can also lower the activation energy by bending
the substrate molecules helping to reach the transition state.
• In some enzymes the active site residue form temporary
covalent bonds with substrate molecules lowering the Ea.
• Fig.5: Effect of an enzyme on the activation
energy of a reaction. (Ferrier and Harvey,
2011, p.55).
pH VS enzyme activity.
• Every enzyme exhibits peak activity at optimum pH.
• At extreme pH levels the enzyme can become denatured and
lose its shape permanently.
Fig.6: Effect of pH on enzyme-catalyzed
reactions. (Ferrier and Harvey, 2011).
Temperature VS enzyme activity.
• Rate increases with temperature initially due to increase in
kinetic energy.
• If extreme temperatures are reached the rate decreases
and the enzyme denatures.

Fig.7: Enzyme activity with temperature. (Anon,2020).

Enzyme conc. VS enzyme activity.
• Increasing the enzyme conc. Will speed up the reaction as
long as substrates are available to bind to.
Fig.8: Effect of enzyme concentration on enzyme
activity. (Cram, 2017).
 Substrate conc. VS enzyme activity.
• Increasing the substrate conc. Will increase the rate to a
certain point.
• This is because when all enzymes are occupied and further
addition will have no impact on the rate.

Fig.9: Substrate concentration and

enzyme activity. (Anon, 2021).
Cofactors and coenzymes.
• Required for effective function of the enzyme.
o Cofactor…
Non-protein substance or a metal ion.

o Coenzyme…
A cofactor is an organic molecule which has Low molecular weight that
bind to an Apoenzyme to form a holoenzyme.
Apoenzyme: inactive protein
Haloenzyme: Cofactor + apoenzyme
Fig.10: Coenzymes and cofactors. (Go conqr, 2018).
Control of metabolic pathways by inhibition.
• Inhibitor: substances that influence the activity of enzymes
by preventing the substrate from binding.

• Three types of inhibition:

Competitive inhibition
Non-competitive inhibition
Feedback inhibition
(Bitesize, 2021).
• Competitive inhibition.
o Inhibitor molecule binds directly onto the active site of the enzyme,
preventing the substrate binding.

Fig.11: Competitive inhibition. (Aryal, 2018).

• Non-Competitive inhibition
o Inhibitor binds to a site in the enzyme other than the active site.
o Binding changes the shape of active site.
o Reaction rate decreases.

Fig.12: Non-Competitive inhibition (Aryal, 2018).

• Feedback inhibition
o This is when the end product of the metabolic pathway binds to the
enzyme at the start of the pathway. (Metabolic pathways, 2021).
Fig.13: Feedback inhibition
Bitesize,2021).
Allosteric regulation.
• Type of regulation where an activator or inhibitor binds to
the enzyme other than the active site.
• Allosteric site: Place where the regulatory molecule binds.

• Fig.14 allosteric regulation.

• (Khan academy, 2021).
How enzymes combine their functions to
form metabolic pathways.
• Glycolysis is a ten-step phenomenon in which cells break one glucose
molecule into two pyruvate molecules.
• This metabolic pathway, in which the product of one reaction becomes the
substrate for the next, is an example of a synchronized series of chemical
reactions.
• The enzymes in a metabolic route can be somewhat physically
interconnected, permitting the product of one reaction to be effectively
routed to the next enzyme in the route.
• Pyruvate dehydrogenase, for example, is a three-enzyme complex that
catalyzes the conversion of pyruvate to acetyl CoA. Intermediate products
are transported rapidly from one enzyme to the next inside this complex.
The methods used to inhibit those pathways.
• Cells can enhance a pathway by raising the levels of a required enzyme
or using activators to transform that enzyme into an active
conformation.
• Cells can reduce the quantity of an enzyme or employ inhibitors to
make the enzyme inactive to delay or stop a process.
• The first intermediate in glycolysis, the glucose-6-phosphate inhibits
hexokinase, the enzyme that generates it.
Fig.15: Glycolysis (Bioscience notes, 2018).
BIBILOGRAPHY
IMAGES
• Fig.1: Botnam, 2021. Enzyme diagram. [image] Available at:
https://botnam.com/enzymes/. [Accessed 17 July 2021]
• Fig.2: Cooper, G., 2018. Enzymatic catalysis of a reaction between two
substrates . 8th ed. Oxford: Oxford University Press. P.65.
• Fig.3: Microbe notes, 2018. Lock and key model. [image] Available at:
https://microbenotes.com/enzymes-properties-classification-and-signi
ficance
/. [Accessed 18 July 2021].
• Fig.4: Cooper, G., 2018. Induced fit . 8th ed. Oxford: Oxford
University Press. P.65.
• Fig.5: Ferrier, D. and Harvey, R., 2011. Effect of an enzyme on the
activation energy of a reaction. Philadelphia: Lippincott Williams &
Wilkins. P.55.
• Fig.6: Ferrier, D. and Harvey, R., 2011. Effect of pH on enzyme-catalyzed
reactions. Philadelphia: Lippincott Williams & Wilkins. P.58.
• Fig.7: Anon, 2020. The Effect of Temperature on Enzyme Kinetics.
Available at:
https://chem.libretexts.org/Courses/Pacific_Union_College/Kinetics/09%3
A_Enzyme_Kinetics/9.08%3A_The_Effect_of_Temperature_on_Enzyme_
Kinetics
. [Accessed July 18, 2021].
• Fig.8: Cram, 2017. effect of enzyme concentration on rate of reaction.
[image] Available at:
https://www.cram.com/flashcards/ocr-as-biology-factors-affecting-enzym
e-activity-8252255
. [Accessed 18 July 2021].
• Fig.9: Anon, 2020. Temperature, pH, and enzyme concentration on the rate
of a reaction. Available at: https://
chem.libretexts.org/Courses/University_of_Arkansas_Little_Rock/CHEM_
4320_5320%3A_Biochemistry_1/05%3A_Michaelis-Menten_Enzyme_Kinet
ics/5.5%3A_Temperature%2C_pH%2C_and_enzyme_concentration_on_the
• Fig.11: Aryal, S., 2018. Competitve inhibition. [Image] Microbe notes.
Available at: https://microbenotes.com/enzyme-inhibition/. [Accessed
18 July 2021].
• Fig.12: Aryal, S., 2018. Non-Competitve inhibition. [Image] Microbe
notes. Available at: https://microbenotes.com/enzyme-inhibition/.
[Accessed 18 July 2021].
• Fig.13: Bitesize. 2021. Feedback inhibition. [Image] Available at:
https://www.bbc.co.uk/bitesize/guides/zwnffg8/revision/7.
[Accessed 18 July 2021].
• Fig.14: Khan academy, 2021. Allosteric regulation. [image] Available at:
https://www.khanacademy.org/science/ap-biology/cellular-energetics/
environmental-impacts-on-enzyme-function/a/enzyme-regulation
. [Accessed 18 July 2021].
• Fig.15: Bioscience Notes, 2018. Glycolysis. [Image] Available at:
https://www.biosciencenotes.com/glycolysis/. [Accessed on 12 August
2021].
CONTENT
• Anon, 2020. The Effect of Temperature on Enzyme Kinetics. Available
at:
https://chem.libretexts.org/Courses/Pacific_Union_College/Kinetics/
09%3A_Enzyme_Kinetics/9.08%3A_The_Effect_of_Temperature_on
_Enzyme_Kinetics
. [Accessed July 18, 2021].
• Aryal, S., 2018. Enzyme inhibition. [online] Microbe notes. Available at:
https://microbenotes.com/enzyme-inhibition/. [Accessed 18 July
2021].
• Aryal, S., 2018. Enzymes- Properties, Classification and Significance.
[online] Microbe notes. Available at:
https://microbenotes.com/enzymes-properties-classification-and-signi
ficance/
. [Accessed 18 July 2021].
• Bitesize. 2021. Metabolic pathways. [online] Available at:
• Cooper, G., 2018.The cell. 8th ed. Oxford: Oxford University Press. P.63 to
P69.
• Ferrier, D. and Harvey, R., 2011. Biochemistry. 5Th ed. Philadelphia: Lippincott
Williams & Wilkins, p.53 to p.62.
• Go conqr, 2018. COfactors and coenzymes. [Online] Available at:
https://www.goconqr.com/slide/13957006/cofactors-enzymes-and-prostheti
c-groups-unfinished-
. [Accessed 18 July 2021].
• Infinita Biotech. 2021. Characteristics Of Enzyme Catalysi`s. [online]
Available at:
https://infinitabiotech.com/blog/characteristics-of-enzyme-catalysis/.
[Accessed 17 July 2021].
• Khan academy, 2021. allosteric regulation. [Online] Available at:
https://www.khanacademy.org/science/ap-biology/cellular-energetics/enviro
nmental-impacts-on-enzyme-function/a/enzyme-regulation
. [Accessed 18 July 2021].
• Nature education. 2014. Cell Metabolism. [online] Available at:
https://www.nature.com/scitable/topicpage/cell-metabolism-14026182/.
[Accessed 12 August 2021].