2.4 Enzymes Flashcards

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1
Q

What is the difference between a catabolic and an anabolic pathway?

A

Catabolic- metabolites broken down to smaller ones, releasing energy
Anabolic- energys used to synthesize larger molecules from smaller ones

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2
Q

What is a co factor?

A

A substance that has to be present to ensure an enzyme catalysted reaction takes place at the appropriate rate. Some are part of the enzymes structure, others (mineral ion cofactors and organic coenzymes) form temporary associations with the enzymes

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3
Q

What is the lock and key hypothesis

A

Substrate fits in enzyme way key fits in lock

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4
Q

What is the induced fit hypothesis

A

Substrate changes shape of active site

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5
Q

What is the name of amount of energy needed to start a reaction?

A

Activation energy

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6
Q

Do enzymes increase or reduce activation energy required for a reaction?

A

Reduce

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7
Q

How does temperature effect enzyme activity? 2

A

Kinetic energy- mols move faster, increase rate of successful collision
increasing beyond optimum reduces rate of reaction as breaks hydrogen bonds, hold tertiary structure, denture enzyme, not complimentary to substrate

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8
Q

What is the optimum temperature and what happened to the rate of reaction at this temperature?

A

The temperature at which the enzyme works at its fastest rate
The rate of reaction is at its maximum

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9
Q

What is Q10?

A

Temperature coefficient -

Rate of reaction at (T+10)/ Rate of reaction at T

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10
Q

What is the effect of pH on enzyme activity?

A

Increased pH interferes with hydrogen bonds, change tertiary structure, chance active site, not complimentary to substrate, rate of reaction decreases

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11
Q

What is a buffer?

A

Resists changes in pH

Can donate/accept hydrogen ions

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12
Q

Enzymes work within a narrow range of pH. What does this mean for the rate of reaction and change of pH?

A

Small changes in pH will slow the rate of reaction

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13
Q

What is the effect of substrate concentration on enzyme-catalysed reactions? (6)

A

1 Increases because more ESCs can form
2 more product forms
3 substrate conc is limiting factor because as it increases the RofR increases
4 if substrate conc increases further, reaction reaches maximum rate, adding more substrate will not ii crease RofR
5 because enzymes are fully saturated/ active sites are fully occupied with substrate
6 so no additional substrate can successfully collide with active site

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14
Q

What is the effect of enzyme concentration on RofR

A

1 more active sites available
2 more successful collisions occur between enzyme and substrate
3 more ES complexes
4 enzyme conc is limitimg factor, as it increases, so does r of r
5 if increased further, no increase r of r because active sites of extra enzymes won’t be occupied
6 sub is now limiting factor

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15
Q

What are the two types of enzyme inhibition?

A

Competitive

Non competitive

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16
Q

What is a competitive inhibitor?

A

Similar shape to active site
Blocks active site, prevent substrate from binding
Prevents formation of ESCs

17
Q

What is a non competitive inhibitor?

A

Binds to part of enzyme (allosteric site) changes shape of active site prevents es complexes because no longer complimentary to substrate

18
Q

Give an example of a prosthetic group and which enzyme it affects (2)

A

Zinc ion

carbonic anhydrase

19
Q

Give an example of an ionic cofactor and which enzyme it affects (2)

A

Chloride ion

amylase

20
Q

Give an example of a coenzyme and which enzyme it affects (2)

A

Vitamin B12

Cobalamin

21
Q

Which 2 of the 3 cofactors are not permanently bound to the enzyme they affect?

A

ionic cofactors

enzymes