Enzymes
Properties of enzymes
Recap
WHAT IS ANABOLISM AND ENZYME CATALYZES BOTH
CATABOLISM? ANABOLIC AND CATABOLIC
REACTIONS.
What are enzymes
Enzymes are biological catalysts.
A catalyst speeds up a chemical reaction but remains unchanged at the end
of the reaction.
As well as catalyzing all the metabolic reactions of cells (such as
respiration, photosynthesis and digestion), they also act as motors,
membrane pumps and receptors.
Enzyme Structure
Enzymes are proteins, and their function is determined by their
complex structure.
The reaction takes place in a small part of the enzyme called the active
site, while the rest of the protein acts as "scaffolding".
The active site is a region, usually a cleft or depression where another
molecule (substrate) can bind.
Cont’d
The shape of the active site allows the substrate to bind perfectly.
Temporary bonds form between the substrate and the R groups of the enzyme’s
amino acids.
This combination is called the enzyme substrate complex.
Enzymes are globular proteins with a precise 3D tertiary structure with the R
groups outside of the molecule, making them soluble in water.
How enzymes work
Intracellular enzymes are found inside cells e.g. hydrolase found inside lysosomes
which break down materials taken in by phagocytosis.
Extracellular enzymes act outside of cells. These include digestive enzymes in the
alimentary canal.
Each type of enzyme will only bind to one type of substrate.
The active site will only allow one shape to fit, just like a lock and a key.
An induce fit occurs when the enzyme
changes slightly so that it can
Induce fit accommodate and hold the substrate in
exactly the right position for the
reaction to occur.
The arrival of the substrate molecule
causes a change in the shape of the
enzyme.
The products
Enzymes are specific for the substrate.
The interaction between the R groups and the substrate can either break the
molecule forming two or more products or encourage formation of products by
combining substrates.
When the reactions is completed the products or products leave the active site.
The maximum number of substrate molecules that can be convert to products
per minute is known as the enzyme’s turnover number.
Activation energy
One way to increase the rate of a chemical reaction is to increase its energy, or activation energy.
Our normal body temperature is 37o C. I can rise to 40o C but no more without major damage
happening to the body.
Enzymes are the solution to this problem because they decrease the activation energy of the reaction
that they catalyze.
Cont’d
They do this by holding the
substrate in such a way that their
molecules can react more easily.
Reactions catalyzed by enzymes
take place rapidly at a much
lower temperature than they
would without them.
Activation
energy
H202 and catalase
Catalase (found in many foods and tissues) break down hydrogen peroxide to water and
oxygen.
A large amount of oxygen bubbles are released in the reaction for the first minute. However, it
gets slower as time goes by until the reaction stops.
This is because when the substrate and enzyme were first mixed, they bonded at incredible
speeds as more substrate bind to all the available active sites.
(The rate of the reaction depends only on how many enzymes are there and the speed at which
each enzyme molecule can bind with another substrate molecule)
Cont’d
However, as more and more substrate is converted to products there are fewer and fewer substrate
molecules to bind with enzymes.
Enzymes may be waiting for a substrate molecules to move in their direction and by chance hit their
active site.
As fewer substrates are left the reaction gets slower and slower, until it eventually stops.
The effect of enzyme concentration
Total
volume of
oxygen
collected
Time
The explanation
The graph shows that the initial the initial rate of the reaction increases linearly as enzyme concentration
increases.
In these conditions reaction rates is directly proportional to the enzyme concentration.
If you double the number of enzyme molecules, then twice as many active sites will be available for the
substrate to slot into.
As long as there is plenty of the substrate available the initial rate of a reaction inreases with enzyme
concentration.
The effect of
substrate
concentration
The explanation
As substrate concentration increases the initial rate of the reaction also increases.
The more substrate the more often an enzyme active site can bind with one.
However, if the substrate concentration continues to increase while the enzyme concentration remains
constant there comes a point where every enzyme site is working continuously.
The additional substrate will just clump up until an active site becomes vacant.
The enzyme is working at its maximum possible rate, known as Vmax.
Temperature and
enzyme activity
Temperature and enzyme activity
At low temperature reactions occur slowly.
This is due too slow movements of the molecules.
As temperature rises the enzymes and substrate move faster and more collision occurs.
They will have sufficient activation energy to react.
Above a certain temperature the enzyme molecules vibrates too energetically causing some of the bonds
holding the enzyme molecule in shape to break. This is especially true for hydrogen bonds.
The molecules then loses its shape and becomes denatured.
Most enzymes work best at a pH of 7.
pH and enzyme
activity
Cont’d
pH is the measure of the concentration of hydrogen in a solution.
The lower the pH the more concentrated the solution is with hydrogen.
Hydrogen ions can interact with the R groups of amino acids this influences the way in which they bond
with each other and therefore affects the tertiary structure.
A pH that is ver different from the optimum pH will denature the enzyme.
Cont’d
NH2 or COOH groups may ionize of parts of the tertiary polypeptides to become NH3 and COO.
However, if the pH is low (acidic) this will cause the COOH groups to remain unionized.
If the pH is high the NH3 groups do not ionize.
Either of these conditions can therefore cause ionic bonds between R groups in the enzyme molecules to
break, thus denaturing the enzyme.
Enzyme inhibitors; competitive
inhibition
A substance that slows down or stops an enzyme-controlled reaction is said to be an inhibitor.
If the inhibitor binds only for a short time, then it is a competitor for the active site.
If there is a lot of substrate present, then the chances of the substrate colliding with the active
site is great.
However, if the concentration of the inhibitor rises or the substrate concentration falls more
likely the inhibitor with collide more with the active site than the substrate.
This is called competitive inhibition.
Cont’d
Competitive inhibition is reversible.
It can be reversed by increasing the concentration of the substrate.
Sometimes the inhibitor permanently bonds to the active site and
permanently blocks the substrate.
This type of inhibition is irreversible.
Noncompetitive inhibition
Sometimes the inhibitor can bind to another part of the enzyme instead of the active site,
called the allosteric site.
This bonding seriously distorts the molecule of the enzyme and its active site making it
unsuitable for the substrate.
The enzyme’s function is blocked no matter how much substrate is present this is called
noncompetitive inhibition.
It can be reversible or irreversible, depending on whether the inhibitor bonds briefly or
permanently with the enzyme.
Cont’d
Heavy metals such as lead and mercury may affect enzyme activity.
They can permanently bind to the SH groups within the molecule, within or outside the active site.
This breaks the disulphide bridges that help to maintain the tertiary structure of the enzyme.
This alters the shape of the active site and prevents the substrate from binding.
Enzyme
catalyzed
reactions
Explanation
In an enzyme catalyzed reaction,
the initial rate of the reaction is
changed with the presence of an
inhibitor.
The cell metabolic pathway
The reaction of enzymes are often a sequence of reactions called a metabolic pathway.
A enzyme B enzyme C enzyme D
1 2 3
One way of making sure that the cell does not become oversupplied with substance D is for this substance
to act as an inhibitor of an enzyme for earlier steps in the reaction.
For example substance D might inhibit enzyme 1.
This means that the more substance D there is the less substance A is converted to B and therefore less of D
is made.
Cont’d
This is called end product inhibition.
Inhibitors that seriously disrupts enzyme-controlled reactions are metabolic poisons and prevent vital
chemical reactions from taking place in the body.
