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Unit 3 AOS 1

Catalysts are substances that increase the rate of chemical reactions without themselves
becoming chemically changed.
Most reactions in the body would proceed far too slowly to maintain life if it were not for
the presence of catalysts.
Biological catalysts are called enzymes.
Metabolism is the overall chemical activity of cells.
Anabolic: reactions that build things up.
Catabolic: reactions that break things down.
Enzymes
Enzymes are proteins that act as biological catalysts.
Catalysts are substances that regulate and increase (speed up) the rate of chemical
reactions in living systems but are not used up or changed in those reactions.
Enzymes are important because they control metabolic processes and the reactions in cells
would proceed so slow, as to not occur at all.
Enzymes:

 are proteins
 are substrate specific
 can be reused over and over again
 are needed in small accounts and are neither reactants nor products
 make a reaction take place more easily (reduce the activation energy)
 can catalyse a reaction in either direction (most chemical reactions are reversible)
 do not change the direction of a reaction
 do not change the final product
Metabolic Pathways
Metabolic pathways are a series of chemical reactions occurring within a cell.
In each pathway, a principal chemical is modified by a series of chemical reactions.
Enzymes catalyse these reactions, and often require dietary minerals, vitamins, and other
cofactors in order to function properly.
The Active Site
Each enzyme is highly specific
Specificity related to its 3D shape
The active site is the surface that fits with the substrate.
Denaturing of Proteins
When proteins such as enzymes are denatured, they can no longer perform their function.
The activity of a protein depends on its 3D structure and intramolecular bonds, particularly
hydrogen bonds.
Since hydrogen bonds are easily broken by excessive heat or pH, it will cause the protein to
unfold and lose shape, and it is said to be denatured. It destroys the active site (specific
arrangement of atoms on surface).
Properties of Enzymes

 Proteins
 Specific
 They can be intracellular and extracellular
 Proteins denatured at high temperatures or acidic conditions (begins to unfold and
loses its 3D shape).
 Enzymes are not changed or used up during the reaction.
 Enzymes can be used over and over again
 Small amount of enzyme required for reaction to proceed.
 Reversible (reaction can proceed in both directions in many cases).
Mechanism of Enzyme Action
1. Enzyme binds with substrate
2. Enzyme-substrate complex
3. Enzyme releases product
Theories of Enzyme Action
Lock and Key
Substrate molecules have the right shape to fit in active site.

Induced Fit
Interaction between enzyme and substrate molecule changes shape of enzyme active site to
fit substrate molecule.
Specificity of Enzymes
Enzymes are highly specific. They are needed for specific chemical reactions.
Most enzymes are named for the type of reaction they catalyse.
Enzymes are named by adding the suffix (-ase) to the name of the substrate on which it acts.
Eg. Lipase acts on a lipid, proteases (pepsin; trypsin) act on proteins, oxidases act on oxygen.
How do enzymes perform their roles of catalysts?
Every reaction requires a certain amount of energy called activation energy for the reaction
to take place.
Enzymes act by reducing the amount of activation energy needed for a reaction to take
place, ensuring the reaction takes place more easily.
Cofactors and Coenzymes
Some enzymes are produced in an inactive form and must be activated in some way. They
require another chemical component, attached to the protein, to be active. These additional
components are called cofactors.
Coenzymes are very small organic molecules – less complex than proteins – that are
associated with particular enzymes and are essential for their activity. Most organic
coenzymes are derived from vitamins.
Coenzymes
Most coenzymes are carrier molecules, transferring electrons or ions from one reactant to
another in a biological reaction.
NADH, NADPH and FADH2 are important coenzymes which transfer electrons or ions during
cellular respiration and/or photosynthesis.
ATP is a coenzyme; it transports a phosphate group.
Factors affecting Enzyme Action
Temperature
An increase in temperature will increase the activity of reactions until 50-60 degrees where
enzymes become denatured.
Warming increases the rate of most chemical reactions, including enzyme-catalysed
reactions. This is because the extra heat energy is taken up by the molecules so they move
faster, which increases the rate between substrate and enzyme.
However, too much heat can damage the structure of an enzyme. Enzymes are proteins,
and all proteins are denatured by heat when a certain critical temperature is reached.
Most enzymes have an optimum temperature range, which is the temperature at which the
enzyme’s catalytic activity is the greatest. This is the range immediately below the critical
temperature at which denaturation of enzyme molecules begins to occur.

pH
pH is the measure of hydrogen molecules. It varies from an acidic to an alkaline level.
Altering the pH level may change the shape of the active site and so alter the ‘fit’ between
enzyme and substrate. The optimal pH is that at which the fit is best and so the enzyme’s
activity is greatest.

Concentration of the enzyme


The more enzyme present, the faster the activity (even though enzymes are only needed in
small amounts). The second graph plateaus because the enzyme conc. is limiting reaction.
All active sites are used.

Concentration of Substrate
The rate of product formation (enzyme activity) increases as substrate conc. increases; until
saturation (substrates occupy all of the active sites.

Enzyme Inhibitors – Natural


Some chemicals called inhibitor molecules can stop enzymes functioning. They may mimic
the substrate and block/compete for the active site or change the shape of it.
Poisons and drugs are examples of enzyme inhibitors, eg. Arsenic, insecticides or nerve gas.
Inhibitors
A nonspecific inhibition effects all enzymes in the same way. It includes any physical or
chemical changes which ultimately denatures the protein.
Specific inhibitors exert their effects upon a single enzyme.
Most poisons and drugs also work by inhibiting enzymes in bacteria, viruses or cancerous
cells.
A competitive inhibitor is any compound which closely resembles the structure of the
substrate.
The inhibitor competes for the same active site as the substrate molecule. It prevents any
substrate molecules from reacting with the substrate temporarily.

A non-competitive inhibitor binds with an enzyme in another part of the molecule, not the
active site. They alter the shape of the enzyme and therefore the ability of the substrate
molecule to bind with the active site.

How does enzyme inhibition work?


In general, enzyme inhibition involves the inhibitor interacting with the enzyme reducing or
stopping its ability to work as a catalyst.
Key components of metabolic pathways and their regulatory systems are natural inhibitors.
Thus, the regulation of metabolism can be viewed in part as mechanisms of inhibition.
Inhibition
Inhibitor binding is either reversible or irreversible. Irreversible inhibitors usually react with
the enzyme and change it chemically. Whereas reversible inhibitors bind non-covalently and
different types of inhibition are produced depending on whether these inhibitors bind to the
enzyme, the enzyme-substrate complex or both.