Enzymes

Biological molecules which allow life to take place at a

great pace
 Importance of Enzymes
Catalyse biological reactions i.e. metabolism (the
chemical reactions which take place within an
organism)
Increase the speed by many orders of magnitude
Each enzyme speeds up a particular reaction. It will
take only a particular class of reactants (called
substrates). This is termed specificity.
If the enzyme is not formed properly (e.g. a genetic
defect) then the correct reaction may not take place,
leading to disease
Chemical reaction rates
Usually get faster
with temperature
Rate depends on
e-Ea/RT
Ea is activation
energy
R is a constant
T is temperature
Activation energy
High Ea means a slower
reaction
Low Ea means a faster
reaction
Catalysts lower Ea for a
particular reaction to
speed it up
Catalysts aren't used up
and don't change overall
energetics of reaction
 Enzyme Behaviour

Optimal conditions are required to maximise

efficiency of enzyme catalysis. Different enzymes
have different optimal conditions.
 Polypeptides
Enzymes are generally a type of protein
Proteins are made from polypeptides (chains of
amino acids joined together) as well as cofactors
(compounds which bind to enzyme) and coenzymes
(compounds which transfer groups of atoms between
enzymes)
20 amino acids used to make polypeptides
Joined together using a peptide bond
Amino acids
 Zwitterionic forms of amino acids

Neutral form of amino acid Zwitterionic form of amino

(easy to represent) acid (present in solution)
Some amino acids side groups are
charged at different pH

High pH

Low pH
Joining together to make a peptide bond

tetrapeptide
Levels of structure (I)
Levels of structure (II)
 Interactions between side groups

These can break down at high T: denaturation of protein

1. Hydrogen bonds; 2. disulfide bonds; 3. ionic bonds; 4. non-polar interactions

Different representations of proteins

PTEN: a phosphatase
 Features of how enzymes work
Bind the substrate(s): needs a binding site
Might bring more than one substrate together
Catalyse the reaction: needs a catalytic site
Not always the same as the binding site
Side groups from the amino acids act to assist the
correct substrate by interactions with the substrate, fit
the substrate into a groove, lower activation energy
Charged side groups may only bind at particular pH range
 Models of enyme catalysis

A: lock and key; B: induced fit; C: population shift

Lock and key model
Induced fit model
Example: Hexokinase