Enzymes Flashcards

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1
Q

What is an anabolic enzyme?

A

Building up new substances and structures to form new cells and whole organisms

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2
Q

What is a catabolic enzyme?

A

Breaking down substances such as the metabolic pathways in respiration or digestion

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3
Q

What is an active site and what is it complementary to?

A

Specific to the substrate complementary to the substrate

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4
Q

What is the name given to the enzyme and substrate combination?

A

Enzyme substrate complex

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5
Q

What is the name given to the enzyme and product combination?

A

Enzyme product complex

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6
Q

What is the activation energy of an enzyme and what does the energy prevent?

A

Enzymes lower activation energy and the energy prevents molecules from breaking down spontaneously

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7
Q

What is activation energy?

A

The energy required to start the reaction

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8
Q

What kind of protein is an enzyme?

A

globular

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9
Q

What level of structure is important ?

A

Tertiary

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10
Q

What does the lock and key hypothesis assume?

A

The substrate is exactly complementary to the active site

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11
Q

What is the induced fit theory?

A

The substrate isn’t an exact fit. When it binds it caused the enzyme to bend around the substrate resulting in the close fit.

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12
Q

What is an intracellular enzyme?

A

Act within the cell

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13
Q

Why is catalase important?

A

Hydrogen peroxide is a toxic product of metabolic pathways, catalase breaks it down into water and oxygen

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14
Q

What is the equation for the breakdown of hydrogen peroxide?

A

2H2O➡️ 2H2O+ O2

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15
Q

Why do large molecules need to be broken down?

A

They cannot enter cells directly

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16
Q

What is an extra cellular enzyme?

A

Enzymes can be secreted from the cell the break down large molecules so the products can be absorbed. Enzymes released from the cells in this way are extra cellular

17
Q

Give an example of an organism that digests it’s food outside of its body extracellularly

A

Saprophytic fungi

18
Q

What does amylase do?

A

Starch is broken down into maltose using the extracellular amylase

19
Q

Where is amylase released from in the human body?

A

Salivary glands and pancreas

20
Q

What does trypsin do? And where is it produced?

A

Breaks down proteins into smaller polypeptides. Produced in the pancreas secreted into the small intestine

21
Q

how does substrate concentration affect the rate of reaction?

A

higher concentration= faster reaction as more substrate means more likely to be collisions between the enzyme and substrate

22
Q

what is saturation point with the amount of substrate ?

A

after a certain point all of the active sites are full and this is all the enzymes can cope with so adding more substrate makes no difference

23
Q

what effect does enzyme concentration have on the rate of reaction?

A

more enzyme molecules results in more collisions to form enzyme substrate complexes so increases the rate of reaction

24
Q

what happens when the amount of substrate is limited with enzyme concentration?

A

there comes a point when there’s too many enzyme molecules to deal with the amount of substrate so adding more has no effect

25
Q

how does pH affect enzyme activity?

A

enzymes work best at the optimum pH value, for most human enzymes this pH is 7, however above and below the optimum pH the H+ and OH- ions found in acids and alkalis can mess up the ionic bonds and hydrogen bonds that hold the enzymes tertiary structure in place this results in a denatured enzyme

26
Q

what does the temperature coefficient (Q10) show?

A

this is a value that shows how much the rate of reaction changes when the temperature is raised by 10 degrees

27
Q

what effect does temperature have on the rate of reaction?

A

rise in temp makes the enzymes molecules vibrate more, if the temp goes above a certain level this vibration breaks some of the bonds that hold the enzyme in shape , the active site then changes so the enzyme and substrate no longer fit together at this point the enzyme is denatured

28
Q

what do enzyme inhbitors generally do?

A

prevent an enzyme from doing its job, it can be competitive or non competitive, reversible or non reversable

29
Q

how does a competitive inhibitor work?

A

the molecule or part of it has a similar shape so the substance can block the active site. The inhibitor and molecule therefor compete with the active site

30
Q

describe statins

A

used to reduce blood cholesterol, they’re reversible and inhibit an enzyme used in cholesterol synthesis

31
Q

describe asprin

A

they are reversible, they inhibit the active site of a cox enzyme so prevent the synthesis of prostaglandins and thromboxane which are chemicals responsible for producing pain and fever

32
Q

in non competitive inhibition where does the inhibitor bind and why does this have an effect?

A

the allosteric site and causes the tertiary structure to change which changes the active site

33
Q

what is a cofactor and co enzyme and how tightly do they bind to the protein?

A

some enzymes need a non-protein component to carry put their function, they bind loosely

34
Q

which enzyme requires Cl- ions and why are they required?

A

amylase, to form the correctly shaped active site

35
Q

how can precursor enzymes be activated?

A

cofactors and a change in pH