Enzymes

Salazar, C Darang, E
Mendez, R Baqueros, M
 Objectives
By the end of this lesson, you will
learn the following;
• Classification and Nomenclature of
Enzymes

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• Enzyme – Substrate Binding
• Lock – and – Key Model
• Induced – Fit Model
• The Michaelis – Menten Approach to
Enzyme Kinetics
• Cofactors and Coenzymes
• Enzyme Inhibition
• Enzyme Inhibition in the Treatment of
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Enzymes
• Enzymes are proteins that help speed up metabolism, or the chemical
reactions in our bodies
• They act as biological catalysts.

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Enzymes
Classification
Classifications of Enzymes Reaction Type Description

Catalyze redox reaction and can be

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Oxidoreductases categorized into oxidase and
reductase.
Catalyze the transfer or exchange of
Transferases certain groups among some
substrates
Accelerate the hydrolysis of
Hydrolases
substrates
Promote the removal of a group from
the substrate to leave a double bond
Lysase
reaction or catalyze its reverse
reaction
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Enzymes
Classification

Classifications of Enzymes Reaction Type Description

Facilitate the conversion of

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Isomerases isoisomers, geometric isomers or
optical isomers.
Catalyze the synthesis of two
molecular substrates into one
Ligases
molecular compound with the release
energy
Catalyze the movement of ions or
Translocases molecules across membranes or their
separation within membranes

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The Substrate will be attached to the enzyme’s opening,
the Active Site

The Active Site is shaped specifically for the substrate to

attach to. Hence, the Lock-and-Key model.

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Lock–and–Key Model
Enzyme-Substrate Binding

• This suggests that the enzyme and the substrate posses a specific shape
that fits exactly into one another

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Induced–Fit Model
Enzyme-Substrate Binding
• This describes that only the proper substrate is capable of inducing the proper
alignment of the active site that will enable the enzyme to perform its catalytic
function

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Characteristics of Enzymes
Ideal Conditions of Enzymes
• pH
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• Temperature

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my love

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Enzymes
Examples
• Different enzymes in digestion breaks down biomolecules found in your food

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 Enzymes
Examples

• Amylase = Carbohydrates
• Lipase = Lipids

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• Pepsin & Trypsin = Proteins
• Nuclease = Nucleic Acids

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Michaelis – Menten Approach
Michaelis-Menten Equation

𝐸 + 𝑆 ↔ 𝐸𝑆 → 𝐸 + 𝑃

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• It takes the form of an equation relating reaction velocity to substrate
concentration for a system where;
• S = Substrate
• E = Enzyme
• ES = Enzyme – Substrate Complex
• P = Product

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Michaelis – Menten Approach
Michaelis-Menten Equation

𝑉𝑚𝑎𝑥 [𝑆]
𝑣=
𝐾𝑀 + 𝑆

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𝐾𝑀 is the substrate concentration at
which the reaction velocity is 50% of
the Vmax.

• v represents the velocity of the reaction

• Vmax represents the maximum velocity achieved by the system
• KM is the Michaelis constant; sometimes represented as KS instead
• [S] is the concentration of the substrate S.

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 Michaelis – Menten Approach
Graphic Presentation

• This is a plot of the Michaelis-

Menten equation’s predicted

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reaction velocity as a function of
substrate concentration, with the
significance of the kinetic
parameters Vmax and KM graphicall
y depicted.

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 Michaelis – Menten Approach
Derivations

• The best derivation of the Michaelis-Menten equation was provided by

George Briggs and J.B.S. Haldane in 1925 (2), and a version of it follows:

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• PARAMETERS:
• kon is the bimolecular association rate constant of enzyme-substrate binding
• koff is the unimolecular rate constant of the ES complex dissociating to regenerate
free enzyme and substrate
• kcat is the unimolecular rate constant of the ES complex dissociating to give free
enzyme and product P. 17
Michaelis – Menten Approach
Derivations

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 Michaelis – Menten Approach
Derivations

• The steady-state approximation is the first important assumption involved in

Briggs and Haldane’s derivation.

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• This is also the reason that well-designed experiments measure reaction velocity only
in regimes where product formation is linear with time.
• As long as we limit ourselves to studying initial reaction velocities, we can assume that
[ES] is constant:

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Michaelis – Menten Approach
Derivations

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Michaelis – Menten Approach
Derivations
We now make a couple of substitutions to arrive at the familiar form of the
Michaelis-Menten equation. Since Vmax is the reaction velocity at saturating
substrate concentration, it is equal to kcat [ES] when [ES] = [ET]. We also

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define KM in terms of the rate constants as follows:

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Michaelis – Menten Approach
Derivations

• Comparing KM [= (koff + kcat)/kon] and KD [= koff/kon], it is obvious that KM must always be

greater than KD. Michaelis and Menten assumed that substrate binding and dissociation

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occurred much more rapidly than product formation (kcat << koff, the rapid equilibrium
approximation), and that therefore the KM would be very close to the KD. The larger
the kcat is relative to koff, the greater the difference between KD and KM. Briggs and Haldane
made no assumptions about the relative values of koff and kcat, and so Michaelis-Menten
kinetics are a special case of Briggs-Haldane kinetics. The opposite extreme,
where kcat >> koff, is called Van Slyke-Cullen behavior.

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 Cofactors and Coenzymes
Enzyme Sidekicks

• Enzymes don’t always

work alone.
• Cofactors are typically

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metal ions (i.e. iron).
• Coenzymes are organic
molecules (i.e. vitamins)
• They may bind the
substrate or to the
active site

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 Enzyme Inhibitions
Inhibitors
• Competitive Inhibitors
• Tend to sit on the Active Site,
blocking the substrate from binding.

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• Non–Competitive Inhibitors
• These inhibitors bond to
somewhere around the enzyme that
isn’t the active site, which we call
the “Allosteric Site”

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 Enzyme Inhibitions in the Treatment
of AIDS
• Protease Inhibitor Drugs
• atazanavir (Reyataz)
• darunavir (Prezista)

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• fosamprenavir (Lexiva)
• indinavir (Crixivan)
• lopinavir/ritonavir (Kaletra)
• nelfinavir (Viracept)
• ritonavir (Norvir)
• saquinavir (Invirase)
• tipranavir (Aptivus)
• atazanavir/cobicistat (Evotaz)
• darunavir/cobicistat (Prezcobix) 25
References
• https://www.youtube.com/watch?v=qgVFkRn8f10
• https://www.youtube.com/watch?v=6EDBlowVST0&t=314s
• https://depts.washington.edu/wmatkins/kinetics/michaelis-menten.html

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• https://www.healthline.com/health/hiv-aids/protease-inhibitors#how-they-work

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Answer the questions below:
• What are enzymes?
• Give 3 Enzyme Classifications.
• Give 3 examples of an enzyme.

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• Differentiate the lock-and-key and the induced-fit model.
• What are the 2 types of Inhibitors?
• This site is where the Non-Competitive Inhibitor sits on, what is this
site called?
• What are these ions/organic molecules that helps the enzyme
function properly?
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