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Enzymes:

Define enzyme:
- A globular protein that acts a biological catalyst to speed up rates of reactions without being
altered by lowering antinational energy.

Describe the structure of an enzyme:


- They’re a globular protein with a specific tertiary structure. They’re soluble because
hydrophilic R groups point to the surface while the hydrophobic ones point to the centre.
Their tertiary structure is determined by the sequence of amino acids in its primary structure
and their active site has a complementary shape to 1 specific substrate.

The function of Enzymes:


They’re biological catalysts – (i.e. they speed up chemical reactions without being used up).

Explain how enzymes break down substrates?

- Substrates fit inside their enzyme’s complementary active site in a key lock mechanism
- The amino acids in the active site bind weakly with the substrate to form an enzyme substrate
complex
- The interactions between the R groups of the enzyme and substrate cause changes in the
substrate structure to form the new products
- Now the products can’t fit in the active site and detach from the enzyme’s active site

Explain how enzymes lower activation energy of reactions?

- They hold the substrate in the active site temporarily


- During the formation of the enzyme substrate complex a strain is exerted onto the substrate
- This strain results in the formation of new bonds or the breaking of existing bonds in the
substrate
- This helps to break the substrate down to smaller products or join substrates into a bigger
product.

Q. Explain How enzymes break down substrates so quickly?

- They’re catalysts that speed up rate of reaction by lowering


activational energy without being used up. Once reactions
are complete the enzymes detach from product and bind to
another substrate.
Types of Enzymes:
Intracellular:
- Those are enzymes that catalyse reactions within the cells (E.g – Respiratory Enzymes)

Extracellular:
- Those are enzymes secreted by cells to catalyse reactions OUTSIDE these cells (Digestive
enzymes like pepsin and amylase)
Factors that affect Enzyme Activity
- Temperature
- pH
- Enzyme Concentration
- Substrate Concentration
Factor How does it affect ? Graph
Temperature Enzymes and substrate particles move slowly at low temperatures
due to lower kinetic energy.

Less likely for collisions to occur


The optimum temperature is point when enzyme activity is highest

High temperatures cause particles in the enzyme to vibrate rapidly


leading to the breaking of hydrogen bonds. Resulting in active site to
irreversibly lose its shape and DENATURE

pH Lower or higher pH values ionise the R groups in amino acids


changing the charges and causing ionic bonds in protein to break
which denatures the enzyme

When an enzyme denatures it no longer fits the substrate in the


active site. This causes rate of reaction to slow down eventually
stopping when all enzymes denature.

Enzyme Conc Enzyme conc is LIMITING at beginning. Reaction rate increases


steadily when enzyme concentration increases.

This is because more collisions between enzyme and substrate occur


per unit time. So more enzyme substrate complexes form.

Reaction rate levels off when substrate concentration becomes the


limiting factor because there are now too many empty active sites
and no more substrates.

Substrate Substrate conc is LIMITING at beginning. Reaction rate increases


Conc steadily when substrate concentration increases.

This is because more collisions between enzyme and substrate occur


per unit time. So, more enzyme substrate complexes form.

Reaction rate levels off when ENZYME concentration becomes the


limiting factor because now all of enzyme active sites are saturated
(occupied with substances)
Initial rates:

Importance and Observations from initial


rate:

Maximum Rate of Reaction

The only limiting factor at beginning of


reaction is the one being investigated and
initial rate can tell us.

Initial rate is calculated by drawing a


tangent on the point and calculating the
gradient. (V/T)

Effect of Temp and Ph on enzymes.

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