Enzymes

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ENZYMES

 Enzymes are proteins that act as biological catalysts to increase the rate of a
chemical reaction, by lowering the activation energy (reduce the amount of
energy required).
 Enzymes are not consumed in a reaction, they are recycled.
 Living organisms require enzymes to ensure reactions occur at a faster rate
and they can also control biochemical pathways. Such as individual reactions
are catalysed by a specific enzyme.
 Intracellular enzymes speed up and control metabolic reactions within the
cell. While extracellular enzymes are secreted by the cell and catalysed
reactions outside of the cell.
 Lock & Key Model
o The active site is highly specific for a particular substrate.
o The active site on the enzyme has the right shape for the specific
substrate, in which they bind forming an enzyme-substrate complex.
This causes the substrate to form new products.

 Induced Fit Model


o As the substrate and enzyme bond, the enzyme changes its shape, so
the two molecules can fit together more closely.

 Factors That Affect Enzyme Activity


1. Temperature
- Activity of enzymes increases with increasing temperature due to the
molecules becoming more excited and collide more often. The increase
in these collisions allows for the substrate to bump into its enzyme and
enter its active site. Enzyme activity continues to increase with increase
temperature until its optimum temperature.
- When temperatures are too high the bonds in the protein break,
causes it to lose its functional shape. The enzyme becomes denatured
as the substrate can no longer fit into the active site. This reduces the
enzymes activity.
2. Changing pH
- Each enzyme has an optimum pH (work at its fastest rate). Some
enzymes can work in a wide range of pH while others work in a narrow
pH range.
- Buffer solutions are better for enzyme activity than non-buffered
solutions (e.g. water) because proteins can influence the pH of a
solution by donating hydrogen ions or hydroxyl ions.
- In acidic solutions, proteins gain hydrogen ions which can cause their
shape to change (bond between the 3D structure may break). This
causes the enzyme to become denatured.

3. Substrate and Enzyme Concentration


- Increased amounts of substrate will result in more products being
made until all enzyme molecules are at maximum capacity 
saturation point.
- Increased amount of enzyme will yield more product exponentially
until the product starts to inhibit the enzyme or the substrate is
depleted.
- Enzyme concentrations are regulated in response to the needs of a cell
(control expression, rate of degradation or activation due to a stimulus)

 Cofactors and Coenzymes


o Some enzymes are inactive until they bind with other molecules or ions
that change their conformation (shape and charge of the active site).
These molecules/ions catalyse reactions more efficiently.
1. Cofactors
- Ions (Zn2+, Ca2+,, Mg2+) that assists enzyme activity by helping the
enzyme to fold properly into its 3D structure (binding to the amino
acids) or to facilitate the reaction by being present at the active site

2. Coenzymes
- A small molecule (non-protein, organic) that carrying groups of atoms
to or from the reactions that are catalysed by enzymes.
- They can be reversibly loaded or unloaded with the groups of atoms
they carry.
- NAD and NADPH are examples found in photosynthesis and cellular
respiration (can accept electrons and protons during biochemical
reactions and transfer them to another reaction of the process).

 Inhibiting Enzymes
o Non-competitive Inhibitor
 The product of the reaction inhibits enzyme activity, as if a large
amount of product is present, it will act as an inhibitor by binding
to a site on the enzyme (other than the active site) – slowing the
rate of reaction.
 When the inhibitor binds to the enzyme, the active site of the
enzyme changes shape – no affinity for its substrate.
 If the product is removed, inhibition is reduced as the substrate
can enter the active site, and the product will again be formed –
maintains concentration levels of the products in the cells 
referred to as reversible inhibition

o Competitive Inhibitor
 The inhibitor competes with the substrate for the active site of
the enzyme.
 Some inhibitors bind irreversibly, as the enzyme can no longer
perform its function.
 Questions
1. Recap 3.3 (pg 72)
2. Recap 3.4 (pg 74)
3. Recap 3.5 (pg 75)
4. Enzyme exam questions worksheet

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