Enzymes Flashcards

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1
Q

What is an enzyme

A

A globular protein with a specific shape. It is a biological catalyst

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2
Q

What is a catalyst

A

Something that speeds up the rate of reaction

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3
Q

Why are enzymes useful in small amounts

A

Because they don’t run out so can be re used

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4
Q

What is an enzyme substrate complex

A

When the substrate fits into the active site of the enzyme

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5
Q

How is the substrate held within the active site

A

By temporary bonds between amino acids in the active site and on the substrate

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6
Q

What is the induced fit model

A

Before enzyme and substrate interact, the active site isn’t complementary to substrate. Proximity of a substrate leads or change in enzyme that forms functional active site, via induced fit so ESC is formed. As it changes shape, the enzyme puts a strain on the substrate which distorts bonds and lowers activation energy needed to break bonds and products are formed, the enzyme is unchanged

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7
Q

Why is the lock and key model disproved

A

Because the enzyme is not a rigid structure, the active site is altered by the substrate

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8
Q

How do enzymes work

A

By lowering the activation energy level so reactions can take place at a lower temperature

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9
Q

How does the function of an enzyme relate to its tertiary structure

A

Tertiary structure of active site allows complimentary substrates to bind, forming enzyme substrate complexes

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10
Q

Describe the specificity of an enzyme

A

Enzymes are specific as the have differently shaped active sites which are only complimentary to it’s substrate

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11
Q

What is the effect of enzyme concentration on rate of reaction

A

Increasing enzyme concentration will speed up the rate of reaction as long as there’s substrate. Once substrate is bound, the reaction will no longer speed up

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12
Q

What’s the effect of substrate concentration on rate

A

Initially, an increase leads to an increased rate (more substrates colliding with enzymes so more product) it then levels off (enzymes saturated)

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13
Q

What is a competitive inhibitor

A

Have similar shape to substrate so it occupies the active site

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14
Q

Effect of competitive inhibitor on rate of reaction

A

They reduce the rate as they prevent E-SCs because they fit in the active site but remain unreacted. This is temporary as it eventually leaves the enzyme

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15
Q

How does a non competitive inhibitor work

A

They prevent products from being formed as they bind to a site OTHER than the active site (allosteric) which distorts the tertiary structure, so it can’t catalyse a reaction

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16
Q

Which inhibitors are affected by substrate conc

A

Competitive: if substrate conc is increased, the effect is reduced

17
Q

The effect of non competitive inhibitors on the rate of reaction

A

It slows the reaction rate because it prevents E-SCs

18
Q

The affect of ph on rate of reaction

A

Change in pH away from the optimum affects the rate of enzyme action. If more extreme, the enzyme becomes denatured (on a graph the rate is like normal distribution with optimum at max)

19
Q

How does an extreme pH affect enzymes

A

It alters the charges on the amino acids that make up the active site, this means the substrate can no longer attach. It may cause the bonds in the tertiary structure to break (ionic)

20
Q

How does temperature affect the rate of reaction

A

Rise in temp increases the kinetic energy so they collide more often (more E-SCs) so the rate increases but at around 45 degrees bonds break and the active site changes shape (slows rate) at 60 degrees the enzyme denatures

21
Q

What happens at each stage when a substrate reacts with enzyme

A

Enzyme collides/ binds to enzyme. Active site forms to fit enzyme by induced fit as enzyme substrate complex forms. ESC breaks down to give products and the enzyme remains unchanged