Enzymes Flashcards

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1
Q

What is an enzyme?

A

A globular protein with a specific tertiary structure which catalyses metabolic reactions in living organisms.

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2
Q

Where can enzymes be found?

A

They can be both intracellular an extracellular.

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3
Q

What is the active site of an enzyme?

A

The area on an enzyme to which the specific substrate binds; other substrates will not bind.

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4
Q

What is the lock and key hypothesis?

A

The theory in which an enzyme’s active site is complementary to the substrate molecule, like a lock and key.

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5
Q

What is the induced fit hypothesis?

A

The theory an enzyme molecule changes shape to fit the substrate molecule more closely as it binds to it.

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6
Q

What is an enzyme-substrate complex?

A

The intermediary formed when a substrate molecule binds to an enzyme.

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7
Q

What is an enzyme-product complex?

A

The intermediate structure in which product molecules are bound to an enzyme molecule.

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8
Q

How do enzymes speed up reactions?

A

Enzymes reduce the activation energy so the reaction can proceed at a much lower temperature.

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9
Q

What is the effect of pH on enzymes?

A

At low pH the many H+ ions interfere with the H bonds by binding the amine group.
At high pH the OH- ions interfere with the H bonds by binding to the carboxyl group.
These both denature enzymes.

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10
Q

What is the effect of low temperature on enzymes?

A

Reaction rate will be very slow because enzyme and substrate molecules have low kinetic energy.

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11
Q

What is the effect of 40-50 degrees C on enzymes?

A

This is optimum temperature thus the enzymes will be at their most productive and reaction rate will be at its peak.

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12
Q

What is the effect of high temperature on enzymes?

A

The kinetic energy of the molecules will be too high for the H bonds of the enzymes to withstand thus the bonds will break, the enzyme will denature.

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13
Q

What is the effect of enzyme concentration on the rate of reaction?

A

Increasing enzyme concentration will increase the rate of reaction until substrate concentration becomes a limiting factor and the reaction reaches its V max.

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14
Q

What is the effect of substrate concentration on the rate of reaction?

A

Increasing substrate concentration will increase the rate of reaction until enzyme concentration becomes a limiting factor and the reaction reaches its V max.

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15
Q

How would you test the effect of temperature on enzyme activity?

A

Sample potato tissue with a cork borer and cut into disks of equal thickness.
Equal amount of disks in a range of temps in water baths.
Pour equal of volumes of pH 7 buffer and hydrogen peroxide into different tubes and allow to equilibrate.
Add peroxide buffer mixture to each potato tube and fix a stopper and side arm.
Time how long it take oxygen bubble to move (oxygen is produce in reaction).

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16
Q

How would you test the effect of pH on enzyme activity?

A

Mix a starch-agar solution and pour into pitri dish to form gel.
Cut wells into each plate and place the same volume of different pH buffer solutions bar control which is distilled water.
Incubate in a dry oven (35 degrees C for 24h).
Flood the plate and rinse with iodine measure the cleared zone- shows how much substrate turned to product.

17
Q

How would you test the effect of substrate concentration on enzyme activity?

A

As temperature but with equal temperatures and different volumes of hydrogen peroxide.

18
Q

How would you test the effect of enzyme concentration on enzyme activity?

A

As temperature but with equal temperatures and different numbers of potato disks in each tube.

19
Q

What is a competitive inhibitor?

A

A molecule that is similar in shape to the substrate and thus can fit into the active site temporarily, preventing enzyme substrate complexes from forming. Levels of inhibition depends on substrate concentration.

20
Q

What is a non competitive inhibitor?

A

A molecule that binds to an allosteric site, this denatures the tertiary structure of the enzyme permanently. Levels of inhibition depend inhibitor concentration.

21
Q

What is a cofactor?

A

An ion that binds to an enzyme and allows enzyme-substrate complexes to form more easily.

22
Q

What is a coenzyme?

A

A non protein organic molecule that binds temporarily to the active site and carry chemical groups between enzymes (taking part in the reaction).

23
Q

What is a prosthetic group?

A

A permanent coenzyme which contribute to the shape of the enzyme.

24
Q

Give a example of a metabolic poison.

A

Potassium Cyanide- binds to cytochrome oxidase and prevents aerobic respiration so kills through fatal lactic acid build up.

25
Q

Give an example of a coenzyme.

A

Vitamin B3- required for pyruvate dehydrogenase (involved in respiration) and used in the process of breaking down fats/carbs for energy.
B3 deficiency leads to a disease called pellagra.

26
Q

Give an example of a cofactor.

A

Chloride ions allow amylase to function properly (break down maltose molecules), without them the reactions will not take place.

27
Q

Give an example of a prosthetic group.

A

Carbonic anhydrase contains a zinc based prosthetic group where it is involved in catalysing the combination of water and CO2 to make carbonic acid which allows CO2 to be transported in the blood.