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CATALYSIS

ENZYMES
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Metabolism
• Metabolism is the sum of all the chemical
activities taking place in an organism.
• Two main types of metabolism:
– Anabolism
– Catabolism

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Properties of enzymes
• Most are proteinaceous and exhibit all the
properties of a protein but some RNA molecules
can also act as catalysts.
• Coded for by DNA
• Biological catalysts
• Enzymes are not used up and remain unchanged
at the end of the reaction.
• Does not change the result of the reaction
• Very efficient
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• They are highly specific both in the reactions that
they catalyze and in their choice of reactants,
which are known as substrates.
• Reversible
• Activity is affected by various factors such as pH,
temperature
• They typically help change one form of energy into
another, a more usable form.
• Enzymes typically do not act alone, they require
helper molecules.
– Cofactors
– Coenzymes
– Prosthetic groups
• Lower activation energy of reaction
• Possess active sites where the reaction takes place.
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Enzyme structure

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The mechanism of action of enzymes

• The Fisher template model


–Lock and key model
• Induced fit model

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Enzyme catalysis
• Enzyme catalysis can be analyzed as a three-
step process.

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Enzymes lower the activation energy

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FACTORS AFFECT ENZYME FUNCTION/
RATE OF ENZYME CATALYZED REACTION
• The rate of an enzyme-catalyzed reaction is
affected by the concentrations of both the
substrate and the enzyme that works on it.
• In addition, any chemical or physical factor
that alters the enzyme’s three-dimensional
shape—such as temperature, pH, and the
binding of regulatory molecules—can affect
the enzyme’s ability to catalyze the reaction.

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Temperature and pH

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ENZYME REGULATION
• Controlling the amount of enzyme produced.
• Feedback inhibition.
• Activation of enzyme molecules.
– pH
– The concentration of certain ions
– The addition of phosphate groups to certain amino
acids in the enzyme
• Allosteric modulation

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Controlling the amount of enzyme
produced

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Feedback inhibition

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ENZYME INHIBITION
• Enzyme inhibition may be:
– Reversible
– Irreversible
• Reversible inhibition occurs when an inhibitor forms weak
chemical bonds with the enzyme.
• In irreversible inhibition, an inhibitor permanently
inactivates or destroys an enzyme when the inhibitor
combines with one of the enzyme’s functional groups, either
at the active site or elsewhere.
– Many poisons are irreversible enzyme inhibitors.
• Reversible inhibition can be:
– Competitive
– Noncompetitive.
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Do Enzymes Work Alone?
1. Cofactors: Inorganic ions, such as the metal ions Zn2+
(zinc), Mg2+ (magnesium), and Fe2+ (iron), which
reversibly interact with enzymes.
2. Coenzymes: Organic molecules that reversibly
interact with enzymes, such as the electron carriers
NADH or FADH2.
3. Prosthetic groups: Non-amino acid atoms or
molecules that are permanently attached to
proteins, such as the molecule retinal. Retinal is
involved in converting light energy into chemical
energy.
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