Nazabayev University UPCSE

Enzymes

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Enzymes
Most are Globular proteins that act as

biological catalysts Speed up chemical reactions that would occur very slowly at the temperature within cells. Precise three dimensional shape adopted by the enzyme includes a depression on the surface called the active site
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Active site
May be a relatively small part of the

large protein molecule. Only a few amino acids may be directly involved in the active site. The remainder maintain the three dimensional shape of the molecule

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Active site

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Lock and key theory

Either a single molecule with a

complementary shape or more than one molecule that together have a complementary shape, can fit into the active site

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Lock and Key theory

Substrate molecules form temporary

bonds with the amino acids of the active site to produce an enzyme substrate complex The enzyme holds the substrate molecules in such a way that they react more easily. When the reaction has taken place the products are released
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Lock and key Theory

The substrate is the key
The enzyme is the lock Each enzyme will only catalyse one

specific reaction because only one shape of substrate fits into its preciselyshaped active site

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Lock and Key Theory

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Induced fit theory

It has been found that the active site is

often flexible When the substrate enters the active site the enzyme molecule changes shape slightly, fitting more closely around the substrate

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Induced fit theory

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Activation Energy
To convert substrates into products

bonds must change both within and between molecules. Breaking chemical bonds requires energy whilst energy is released when bonds are formed. The energy required to break bonds and start a reaction is known as the activation energy
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Activation Energy
Without an enzyme heating a substrate would

provide the energy Heat energy agitates the atoms within the molecules and they become unstable and the reaction can proceed. In cells enzymes reduce the amount of energy needed; this allows the reactions to go ahead without raising the temperature
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Activation energy

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How do enzymes reduce the activation energy?

The specific shape of the enzymes

active site and its complementary substrates is such that the electrically charged groups on their surface interact. The attraction of oppositely charged groups may distort the shape of the substrates and assist in the breaking of bonds or the formation of new bonds
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How important are enzymes?

Enzymes present in all organisms
Catalyse a huge range of reactions Speed up reactions at least a million

times. Most biological reactions would not happen at all without enzymes

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Metabolism
Metabolism of an organism is the sum of all

the enzyme-catalysed reactions occurring within it. Some reactions are simple e.g. hydration of carbon dioxide by carbonic anhydrase CO2 + H2O H2CO3 This reaction allows CO2 to be transported in the blood from respiring tissues to alveoli
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Metabolism
Catabolic reactions Large molecules broken down to smaller ones Hydrolysis of Starch to Maltose by Salivary Amylase. Anabolic Reactions Fatty acid synthetase synthesises fatty acids within cells
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REGULATING ENZYMES: FEEDBACK INHIBITION

Enzymes often function in

a metabolic pathway, The products of one reaction become the reactants (substrate) for the next reaction. In feedback inhibition, the final product of the metabolic pathway inhibits an earlier reaction
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Finding the rates of enzyme controlled reactions

The rate of reaction is found by

determining the quantity of substrate used or the quantity of product formed in a given time. e.g. Catalase used to break down Hydrogen peroxide (H2O2) to water and oxygen Can measure the volume of oxygen given off in a known time
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Quantity of product measured over time to determine the progress of the enzyme reaction Volume of Oxygen produced is measured when catalase is added to hydrogen peroxide

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How do enzyme and substrate concentrations affect the rate of the reaction

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(A) enzyme concentration

The initial rate of reaction is directly

proportional to the enzyme concentration The more enzyme is present the greater number of active sites available Assuming that there is an excess of substrate

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(B) Substrate concentration

The enzyme concentration limits the rate

of the reaction. Every active site is occupied Substrate molecules cannot enter an active site until one becomes free again

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Effect of temperature on enzyme reactions

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Effect of temperature on enzymes

As the temperature rises, reacting

molecules have more and more kinetic energy. This increases the chances of a successful collision and so the rate increases. There is a certain temperature at which an enzyme's catalytic activity is at its greatest. (optimal temperature)
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Effect of temperature on enzymes

Above the optimum temperature the

enzyme structure begins to break down (denature) since at higher temperatures intra- and intermolecular bonds are broken as the enzyme molecules gain even more kinetic energy.

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Effect of pH on enzyme reactions

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Effect of pH on enzyme reactions

Each enzyme works within quite a small

pH range. There is a pH at which its activity is greatest (optimal pH). This is because changes in pH can make and break intra- and intermolecular bonds, changing the shape of the enzyme and, therefore, its effectiveness.
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Non-Competitive Inhibitors
An allosteric site is a location on an enzyme where

a regulating molecule can attach. This is non competitive inhibition (inhibitor is not competing with the substrate for binding to the active site).

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Competitive Inhibitors
Competitive inhibition involves a molecule that is

not the substrate molecule but that can bind with an enzyme's active site. If this non substrate molecule occupies the active site, then there is no room for the substrate to bind at that site.

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Permanent and Non-permanent Inhibitors

Most competitive inhibitors do not bind

permanently to the active site. They bind to the active site then leave. They are described as reversible as removal of the in inhibitor leaves the enzyme unaffected

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Permanent and Non-permanent Inhibitors

Many non-competitive inhibitor bind

permanently to enzyme molecules. The inhibitor is not reversibly (irreversible) Any enzyme molecules bound to an inhibitor are effectively denatured Inhibition is not always a bad thing as a number of metabolic pathways involves inhibition to control reaction rates
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