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Biology 1 > Enzymes > Flashcards

Enzymes Flashcards

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1
Q

Enzymes interact with a

A

substrate

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2
Q

Metabolism-

A

The sum of all chemical reactions/pathways that occur in order to sustain life

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3
Q

Anabolic reactions-

A

Building up of molecules
protein synthesis
growth
STRUCTURE

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4
Q

Catabolic reactions-

A 
Breaking down of molecules
digestion
respiration
Autolysis- programmed breaking of a cell
FUNCTION
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5
Q

Intracellular enzyme is …

Example …

A

An enzyme that stays within the cell

Eg. Catalase ensures hydrogen peroxide (a toxic byproduct of metabolism) is broken down into oxygen and water.

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6
Q

Extracellular enzyme is …

Example …

A

An enzyme that is secreted out of the cells
Eg. Amylase is produced by silvery glands and pancreas and excreted out to digest amylase into disaccharide maltose.
Eg. Trypsin is produced in the pancreas and recreated into the small intestine it helps break down proteins then allows aa to be absorbed.

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7
Q

How do fungi use extracellular enzymes? :
What is the organ that secretes the enzymes?
Where in the organ are the enzymes secreted and how?
What do they then absorb?

A

Fungal Hyphae
In the tips through vehicles to be exocytosed
The soluble products of digestion

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8
Q

Enzymes are _____

so they have a primary, secondary and tertiary structure.

A

Proteins

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9
Q

The enzyme tertiary structure is …

A

The folding of the enzyme molecule into alpha helix’ or beta pleats via interactions with R groups

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10
Q

What is the active site?

A

The active site is where the complimentary substrate binds to the enzyme

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11
Q

How do enzymes speed up chemical reactions?

A 
The molecules (enzyme and substrate) need to collide with sufficient energy (activation energy) in order for a reaction to begin.
Enzymes reduce the amount of activation energy needed as they enable molecules to collide more successfully
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12
Q

An enzyme is …

A

A biological catalyst

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13
Q

What is the lock and key hypothesis?

A

The substrate is held in a way where the correct R groups are close enough to bond. The R group from the active site of the enzyme interact with the substrate creating temporary bond which put strain on the substrate molecule.

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14
Q

What is the induced fit hypothesis?

A

There is an initial weak interaction between enzyme and substrate. This induces changes in the enzyme’s tertiary structure that strengthens the bind and puts strain on the substrates bonds.

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15
Q

What does temperature coefficient, Q10 mean?

A

A measure of how much rate of reaction increases with a temperature increase of 10 degrees c.
The Q10 is usually 2 (doubles) so the rate doubles avery 10 degrees c.

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16
Q

What is the effect of temperature on the rate of reaction?

A

The increase in temperature increases kinetic energy and increases the rate of reaction.

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17
Q

What happens if the temperature is too high?

A

The enzyme becomes denatured as there is too much genetic energy and the bonds that hod its structure in shape are broken and it’s act site is no longer complimentary to the substrate.

18
Q

What does a low pH do to enzymes?

A

Increases the concentration of H+ ions. It replaces or interrupts the hydrogen and ionic bonds within the tertiary structure of the enzymes.

19
Q

What does a high pH do to enzymes?

A

Lowers the concentration of H+ ions.

20
Q

Minor changes in pH do not denature enzymes, why?

A

There isn’t a high enough or low enough concentration for denaturation to occur so the changes are still able to revert back to the enzymes original state (renaturation).

21
Q

Why would a buffer be used in an experiment involving enzymes?

A

A buffer maintains the pH levels in a solution allowing the optimum to be maintained and control of the pH.

22
Q

What is a limiting factor?

A

A factor in a an experiment or process that limits the maximum rate or outcome.

23
Q

How could you achieve a higher maximum?

4 marks

A
  • Remove limiting factor
  • Increase number of enzyme molecules
  • Increase number of substrates
  • This enables more enzyme substrate complex
24
Q

What is an enzyme inhibitor?

A

A molecule that prevents the enzyme from carrying out their role as a catalyst.

25
Q

Why might enzyme inhibitors be necessary in an organism?

A

Need to slow down/stop a metabolic pathway to prevent too many products from accumulating. They help control metabolic activity.

26
Q

What is a competitive inhibitor?

A

A competitive inhibitor has a very similar shape to the substrate so it can also bind to the enzyme before the substrate does. It occupies the active site so fewer enzyme substrate complexes are formed.

27
Q

How would you overcome a competitive inhibitor?

A

Add more substrate

28
Q

What does the line on a graph look like for a competitive inhibitor?

A

Lower than the norm but meets the same v-max

29
Q

Examples of competitive inhibitors …

A

Statins- inhibit cholesterol synthesis

Aspirin- Irreversible preventing synthesis of chemicals of substances that cause pain and fever (prostaglandin and thromboxane)

30
Q

What is a non-competitive inhibitor?

A

A non-competitive inhibitor binds to the enzyme at a different site. Called an allosteric site. It changes the tertiary structure of the enzyme making the active site no longer complimentary tot he substrate. Can be reversible or permanent.

31
Q

What does the line on a graph look like for a non-competitive inhibitor?

A

Lower than the norm but doesn’t reach the same v-max and plateaus.

32
Q

Examples of non-competitive inhibitors …

A

Organophosphates- toxic and irreversible used in insecticides. They inhibit acetylcholinesterase an enzyme involved in nerve pulses causes paralysis and death.

Protein pump inhibitors- Stops H+ ions being pumped into the stomach reduces excess acid

33
Q

What is end product inhibition?

A

End product inhibition is where the product of a chemical reaction acts as a reversible non-competitive inhibitor to the enzyme that catalyses that same reaction.

34
Q

Example of end-product inhibition …

A

Phosphofructokinase- Inhibits the production of ATP

35
Q

A cofactor is …
It’s properties are …
Give an example where a inorganic ion cofactor is needed.

A

An inorganic component that alters the shape of the active site so it can function.

  • Increases reaction rate
  • Combine with enzyme or substrate
  • Amylase breaks starch into maltose. Amylase can only function properly if chloride is present.
36
Q

A coenzyme is …

It’s vitamin derived give 2 examples for Vitamin B3 and 1 for Vitamin B5

A

A biological component that alters the shape of the active site so it can function.
Vitamin B3-
NAD- Transfers h atoms between molecules in respiration
NADP- Carries out the same role in photosynthesis
Vitamin B5-
Coenzyme A- Breaksdown fatty acids
- Breakdown carbs in respiration

37
Q

A apoenzyme is …

A

The precursor enzyme before a cofactor is added.

38
Q

A holoenzyme is …

A

The active enzyme after the cofactor is added.

39
Q

A proenzyme is …

A

A precursor enzyme that requires a in environment before it becomes active.

40
Q

A prosthetic group is …

A

A type of coenzyme that is permanently attached to the enzyme eg. haem

Biology 1 (13 decks)

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