ENZYMES Lecture 14

ENZYMES
A protein with catalytic properties due to its

power of specific activation
Chemical reactions
• Chemical reactions need an initial input of energy = THE
ACTIVATION ENERGY
• During this part of the reaction the molecules are said to be in
a transition state.
Reaction pathway
Making reactions go faster
• Increasing the temperature make molecules move faster
• Biological systems are very sensitive to temperature changes.
• Enzymes can increase the rate of reactions without increasing
the temperature.
• They do this by lowering the activation energy.
• They create a new reaction pathway “a short cut”
An enzyme controlled
pathway
• Enzyme controlled reactions proceed 108 to 1011 times faster than

corresponding non-enzymic reactions.
Enzyme structure
• Enzymes are proteins
• They have a globular shape
• A complex 3-D structure
Human pancreatic amylase

The active site
• One part of an enzyme, the
active site, is particularly
important
• The shape and the chemical
environment inside the
active site permits a
chemical reaction to
proceed more easily
Cofactors
• An additional non-
protein molecule that is
needed by some enzymes
to help the reaction
• Tightly bound cofactors
are called prosthetic
groups
• Cofactors that are bound
and released easily are
called coenzymes
• Many vitamins are
coenzymes
Nitrogenase enzyme with Fe, Mo and ADP cofactors
)
The substrate
• The substrate of an enzyme are the reactants that are activated
by the enzyme
• Enzymes are specific to their substrates
• The specificity is determined by the active site
The Lock and Key
Hypothesis
• Fit between the substrate and the active site of the enzyme is
exact
• Like a key fits into a lock very precisely
• The key is analogous to the enzyme and the substrate
analogaous to the lock.
• Temporary structure called the enzyme-substrate complex
formed
• Products have a different shape from the substrate
• Once formed, they are released from the active site
• Leaving it free to become attached to another substrate
The Lock and Key
Hypothesis
S
E
E
E
Enzyme- Enzyme may

substrate be used again
complex P
Reaction coordinate
The Lock and Key
Hypothesis
• This explains enzyme specificity
• This explains the loss of activity when enzymes denature
The Induced Fit
Hypothesis
• Some proteins can change their shape (conformation)
• When a substrate combines with an enzyme, it induces a
change in the enzyme’s conformation
• The active site is then moulded into a precise conformation
• Making the chemical environment suitable for the reaction
• The bonds of the substrate are stretched to make the reaction
easier (lowers activation energy)
The Induced Fit
Hypothesis
Hexokinase (a) without (b) with glucose substrate
• This explains the enzymes that can react with a range of

substrates of similar types
Factors affecting
Enzymes
• substrate concentration
• pH
• temperature
• inhibitors
Substrate concentration: Non-
enzymic reactions
Reaction
velocity
Substrate concentration
• The increase in velocity is proportional to the substrate

concentration
Substrate concentration: Enzymic
reactions
Vmax
Reaction
velocity
Substrate concentration
• Faster reaction but it reaches a saturation point when all the
enzyme molecules are occupied.
• If you alter the concentration of the enzyme then Vmax will
change too.
The effect of pH
Optimum pH values
Enzyme
activity Trypsin
Pepsin
1 3 5 7 9 11
pH
The effect of pH
• Extreme pH levels will produce denaturation
• The structure of the enzyme is changed
• The active site is distorted and the substrate molecules will no
longer fit in it
• At pH values slightly different from the enzyme’s optimum
value, small changes in the charges of the enzyme and it’s
substrate molecules will occur
• This change in ionisation will affect the binding of the
substrate with the active site.
The effect of temperature
• Q10 (the temperature coefficient) = the increase in reaction
rate with a 10°C rise in temperature.
• For chemical reactions the Q10 = 2 to 3
(the rate of the reaction doubles or triples with every 10°C rise
in temperature)
• Enzyme-controlled reactions follow this rule as they are
chemical reactions
• BUT at high temperatures proteins denature
• The optimum temperature for an enzyme controlled reaction
will be a balance between the Q10 and denaturation.
The effect of
temperature
Q10 Denaturation
Enzyme
activity
0 10 20 30 40 50
Temperature / °C
The effect of temperature
• For most enzymes the optimum temperature is about 30°C
• Many are a lot lower,
cold water fish will die at 30°C because their enzymes
denature
• A few bacteria have enzymes that can withstand very high
temperatures up to 100°C
• Most enzymes however are fully denatured at 70°C
Inhibitors
• Inhibitors are chemicals that reduce the rate of enzymic
reactions.
• The are usually specific and they work at low concentrations.
• They block the enzyme but they do not usually destroy it.
• Many drugs and poisons are inhibitors of enzymes in the
nervous system.
The effect of enzyme inhibition
• Irreversible inhibitors: Combine with the functional groups
of the amino acids in the active site, irreversibly.
Examples: nerve gases and pesticides, containing
organophosphorus, combine with serine residues in the
enzyme acetylcholine esterase.
• Reversible inhibitors: These can be washed out of the
solution of enzyme by dialysis.
There are two categories.
1. Competitive.
2. Non compétitive.
1. Competitive: These
compete with the substrate
molecules for the active
E+I EI
site.
The inhibitor’s action is Reversible Enzyme inhibitor
proportional to its reaction complex
concentration.
Resembles the substrate’s
structure closely.
The effect of enzyme
inhibition
Succinate Fumarate + 2H++ 2e-
Succinate dehydrogenase
CH2COOH COOH CHCOOH
CH2
CH2COOH CHCOOH
COOH
Malonate
2. Non-competitive: These are not influenced by the
concentration of the substrate. It inhibits by binding
irreversibly to the enzyme but not at the active site.
Examples
• Cyanide combines with the Iron in the enzymes cytochrome
oxidase.
• Heavy metals, Ag or Hg, combine with –SH groups.
These can be removed by using a chelating agent such as EDTA.
Applications of inhibitors
• Negative feedback: end point or end product inhibition
• Poisons snake bite, plant alkaloids and nerve gases.
• Medicine antibiotics, sulphonamides, sedatives and stimulants

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ENZYMES

A protein with catalytic properties due to its

• Enzyme controlled reactions proceed 108 to 1011 times faster than

Human pancreatic amylase

Enzyme- Enzyme may

Hexokinase (a) without (b) with glucose substrate

• This explains the enzymes that can react with a range of

• The increase in velocity is proportional to the substrate

CH2COOH COOH CHCOOH

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