ENZYME ACTION

Enzymes are globular proteins that act as catalysts which by reducing the activation energy required, alter the rate of reaction without changing themselves. They
can be used repeatedly and are effective in small amounts. The activation energy is the initial amount of energy required to activate a reaction, and by lowering this
enzymes allow reactions to take place at a lower temperature and enables some metabolic processes to occur rapidly at the human body temp.
Enzyme structure:
 Specific 3-D Shape caused by amino acid sequence
 A specific functional region known as the ‘active site’ made up of a relatively small number of amino acids
 The enzyme acts on molecules called substrates and fits in to form enzyme-substrate complexes held in the active site by temporary bonds

Induced fit model:

 Active site forms as the enzyme and substrate interact, the enzyme has a fixed general shape but as it interacts it
changes shape to mould around the substrate
 The enzyme puts strain on the substrate which distorts a bond in the substrate and lowers the activation energy needed

FACTORS THAT AFFECT ENZYME ACTION

Measuring enzyme-catalysed reactions:
 Two changes most frequently measures: formation of products, disappearance of substrate
 Explanation of graphs: talking about how easy it is to come in contact with a substrate, and how
full active sites are
Effect of temperature:
 Rise in temperature = increased kinetic energy = more frequent
successful collisions = more enzyme-substrate complexes
 Rise in temperature causes hydrogen bonds to break past the optimum
and causes active site to change shape, slowing rate of reaction
 At some point enzyme becomes ‘Denatures’ and stops working (shown
as a falling curve)
Measuring rate of change: (introduction of some graph maths)
 Measuring the gradient at a chosen point, by measuring the gradient of tangent (straight
line touches the curve but doesn’t cut across it)
Effect of enzyme concentration:
 Enzymes aren’t used up and can be reused therefore work efficiently at
very low concentrations
 As long as excess of substrate, increase in amount of enzyme is
proportionate
 The limiting factor will be the substrate concentration at the point of
saturation and therefore the rate of reaction will stabilise, with empty active
sites

 Increase or decrease in pH will reduce rate of reaction – beyond a point

Effect of substrate concentration:
Effect of pH: enzyme becomes denatured  At low substrate concentrations enzyme molecules only have a limited
 It works by altering the charges on amino acids in the active site, means number of substrates to collide with – therefore active sites not working to
enzyme- substrate complexes cannot be formed, and also depending on how full capacity and most efficient
significant the change is, may cause bonds in the tertiary structure to break  As long as excess of enzyme, increase in amount of enzyme is
 Active site partly determined between hydrogen and ionic bonds between – proportionate
NH2 and –COOH groups, change in H+ ions alters bonding and changes  The limiting factor will be the enzyme at the point of saturation and
active site therefore the rate of reaction will stabilise, with full active sites and not
ENZYME INHIBITION
Competitive inhibitors: bind to the active site and directly block it

Non-competitive inhibitors: bind to the allosteric site of an enzyme