Molecular Interactions in Cell

Events
Advanced Higher Biology
 Catalysis
• Speed up chemical reactions between a
million to a trillion times

• Carbonic anhydrase is said to convert 36

million molecules per minute

• Enzymes can only speed up a chemical

reaction that could take place anyway
 Case Study: Hydrolysis of Maltose
• This reaction can happen
without an enzyme if:

-Maltose and water molecule

collide at the right speed to
provide sufficient energy

O
-water molecule has to be in
H H the correct orientation

-water molecule hits the

Hydrolysis of
glycosidic bond at just the
maltose
right angle

Hydrolysis breaks the 1,4 – glycosidic bond
Addition of water provides atoms lost in the
dehydration reaction
• All this isn’t impossible but will
occur infrequently.
• Enzymes makes sure this
happens more frequently!
Proteases
• Proteases
hydrolyse peptide
bonds

• Liberate amino
acids

• Digestive system
 ATPases

• Hydrolyse ATP into ADP and Pi.

• Energy released is used to power a particular
reaction
OR
• Provide a phosphate to phosphorylate a
particular moelcule
 Nucleases
• Nuclease enzymes also take part in a hydrolysis
reaction

• Break phosphodiester bonds in RNA and DNA to

separate nucleotides form one another

• Endonucleases (restriction enzymes) recognise

and cut at particular base sequences
 Kinases

• Add phosphates to molecules

• Phosphate is negative so it will change the
shape of the enzyme
• Phosphorylation may activate or deactivate
(depends on enzyme)
Specificity of enzyme activity
related to induced fit
 Induced Fit Theory

• A change in the conformation of an enzym

e in response to substrate binding that ren
ders the enzyme catalytically active.
1. Active site lined with many amino acid R groups
2. Charged groups in active site complement charged
groups on substrate
3. Bind in correct position
4. Enzyme structure altered
5. Enzyme folds round substrate bringing catalytic R
groups of enzyme closer to substrate reactive groups
6. Enzyme flexes putting substrate under stress and
complex goes through several unstable intermediate
forms (transitional state)
7. Bonds are made and broken and electrons are moved
with catalytic R groups acting as go-between
8. Enzyme-substrate complex formed
9. Product diffuses away and enzyme returns to original
shape
 Inhibition of enzymes
• Decrease rate of reaction

1. Competitive

2. Non-competitive
 Competitive Inhibitors Vmax
High No inhibitor

Reaction
Rate Competitive inhibitor

Low
Low Substrate High
Concentration

•Low concentration of substrate relative to inhibitor = inhibitor will enter active

site first
•As substrate concentration increases reaction rate increases as more chance
substrate will enter first
•At very high substrate concentrations Vmax will be reached as inhibitor will
hardly ever enter first
 Case Study: Succinate Dehydrogenase

Inhibition is
reversible as
malonate is
smaller so can
come out of
active site.
 Case Study:
Sulphonamide
• Binds permanently to bacterial enzyme
• Enzyme is the start of the folic acid
synthesis pathway
• Bacterium unable to make folic acid and
dies
• Humans not affected as do not synthesise
our own folic acid
 Non-competitive inhibition
Vmax
High
No inhibitor

Reaction
Rate Non-competitive
inhibitor

Low
Low Substrate High
Concentration

•Enzyme is non-functional when non-competitive inhibitor is present

•Substrate cannot enter active site as the shape of the cleft has changed
•Inhibitor ‘lowers’ enzyme concentration so Vmax also lower
Summary of Inhibition
 Allosteric effects
• Allosteric enzymes have at least 2 binding sites

• Small molecules can bind far from the active site

an so affect active site shape
-enzyme r-groups reshuffle and make new
bonds

• Shifting of amino acids result in small

adjustments throughout the rest of the enzyme
including conformation of the active site
Positive Modulators (activators)
Negative Modulator (inhibitor)
Summary of Allosteric Enzymes
 What to do now…
• Read p66 ‘Covalent Modification’ to p67
‘Role of end-product inhibition in control of
metabolic pathways’ and make notes

• You will be doing a practical next week

based on the information above