Enzymes Flashcards

(33 cards)

1
Q

What are anabolic reactions?

A

Reactions that build larger, more complex molecules from smaller, simpler ones, requiring an input of energy, typically from ATP

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2
Q

What are catabolic reactions?

A

Reactions that break down large, complex molecules into smaller, simpler ones and in the process release energy. Eg hydrolysis

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3
Q

How do enzymes catalyse reactions?

A

By lowering the activation energy

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4
Q

What level of protein structure do enzymes have?

A

They are tertiary globular proteins

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5
Q

Lock and key hypothesis means�

A

The substrate fits perfects into the enzyme active site

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6
Q

Theory of induced fit means�

A

The shape of the active site changes to fit more perfectly around the substrate, putting pressure on the bonds in the substrate to lower the activation energy

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7
Q

What is formed when the substrate binds to the enzyme’s active site?

A

An enzyme substrate complex

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8
Q

Which enzymes work inside the cell?

A

Intracellular

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9
Q

Which enzymes work outside the cell?

A

Extracellular

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10
Q

The active site and substrate shapes are�

A

Complementary

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11
Q

Enzymes only catalyse one substrate, so they are described as�

A

Specific

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12
Q

The rate of an enzyme catalysed reaction increases with increasing temperature due to…

A

Increased kinetic energy causing increased frequency of successful collisions

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13
Q

When the temperature is too high enzymes will…

A

Denature, meaning the hydrogen bonds break and the shape of the active site is lost

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14
Q

Enzyme controlled reactions will be fastest at a temperature and pH described as the

A

Optimum

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15
Q

The four factors that can limit the rate of an enzyme controlled reaction are

A

Temperature, pH, enzyme concentration, substrate concentration

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16
Q

What does a buffer do?

A

Maintain a constant pH

17
Q

What happens when pH is only slightly above or below the optimum?

A

Small changes in pH cause small reversible changes in enzyme structure, causing inactivation of the enzyme. This will reduce the rate of reaction

18
Q

What happens when pH is far above or below the optimum?

A

Ionic bonds and hydrogen bonds are broken, so the enzyme will permanently denature and lose its shape

19
Q

What happens when you increase the substrate concentration in an enzyme controlled reaction?

A

More successful collisions will occur forming more enzyme substrate complexes and more products. However eventually a plateau will be reached as all the enzyme active sites are occupied at one time. Enzyme concentration becomes the limiting factor.

20
Q

What happens when you increase the enzyme concentration in an enzyme controlled reaction with excess substrate present?

A

More successful collisions will occur forming more enzyme substrate complexes and more products. However eventually a plateau will be reached as the substrate concentration becomes the limiting factor.

21
Q

What is inhibition?

A

Inhibition is when enzyme action is slowed down or stopped by another substance

22
Q

What is a competitive inhibitor?

A

A competitive inhibitor is structurally similar to the substrate and binds to the enzyme active site, blocking it.

23
Q

What is turnover number?

A

An enzyme’s turnover number is the maximum number of substrate molecules it can convert to product molecules per unit time.

24
Q

What is a non competitive inhibitor?

A

Non-competitive inhibition involves an inhibitor binding away from the active site at an allosteric site, altering the active site’s shape so the substrate can no longer bind

25
What effect will increasing substrate concentration have when a competitive inhibitor is present?
If the substrate concentration is increased so will the rate of reaction.
26
What effect will increasing substrate concentration have when a non competitive inhibitor is present?
There will be no change to the rate of reaction
27
What do you call a site that is not the active site?
Allosteric site
28
Give an example of a non competitive inhibitor and which reaction it affects
Cyanide is a respiratory inhibitor
29
Why are enzymes useful in industry?
They lower the activation energy of a reaction so it occurs at a lower temperature, saving energy and increasing efficiency
30
What are immobilised enzymes?
Enzymes which are held in an inert support or matrix, for example immobilised in beads
31
Give the advantages of immobilising enzymes
They can be re-used, they are more stable at extremes of temperature and pH, they do not contaminate the product, enzymes can be combined or used in continuous processes
32
Give the disadvantages of immobilised enzymes in alginate beads
The substrate must diffuse into the gel, which takes time. The gel can alter the shape of the active site. Both of these lower the reaction rate. It can be expensive to initially set up and to sterilise the system if contaminated
33
What is a biosensor?
An instrument that uses enzymes to detect a specific molecule in a mixture of molecules. Eg glucose in blood. They are used for medical and environmental monitoring