Enzymes Flashcards

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1
Q

What are enzymes

A

biological catalysts and globular proteins

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2
Q

What are the two forms of enzyme

A

Intracellular or Extracellular

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3
Q

What is an extracellular enzyme

A

enzymes active outside of the cell

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4
Q

What is an intracellular enzyme

A

enzymes active inside of the cell

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5
Q

Give an example of an intracellular enzyme

A

Catalase

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6
Q

Give an example of an extracellular enzyme

A

Amylase

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7
Q

What does catalase do

A

Converts hydrogen peroxide, which is harmful to cells and a by product of many processes, into water and oxygen - preventing damage to cells and tissues.

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8
Q

What does Amylase do

A

Hydrolyses starch into simple sugars. Digestion is usually carried out by extracellular enzymes, as macromolecules are too large to enter the cell.

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9
Q

What forms when an enzyme and substrate combine

A

An enzyme-substrate complex

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10
Q

What can denature enzymes

A

Heat and pH

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11
Q

What is the shape of the active site determined by

A

The complex tertiary structure of the protein that makes up the enzyme.

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12
Q

What determines the shape of an enzyme

A

the order of amino acids (if altered the 3D shape changes)

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13
Q

Is enzyme substrate complex temporary or fixed

A

Temporary

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14
Q

What two types of enzyme reactions are there

A

Catabolic or Anabolic

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15
Q

What is a catabolic reaction

A

When a single substrate is drawn into the active site and broken apart into two or more distinct molecules. E.g. Cellular respiration and hydrolysis

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16
Q

What is an anabolic reaction

A

When two or more substrates are drawn into the active site, forming bonds between them and releasing a single product. E.g. Protein synthesis and photosynthesis

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17
Q

What do enzymes do to activation energy

A

Lower it

18
Q

What is activation energy

A

Amount of energy needed for a substrate to be unstable enough for a reaction to occur and products form

19
Q

How do enzymes speed up chemical reactions

A

They influence the stability of bonds in reactants.

20
Q

What does lock and key model suggest

A

Enzyme and substrates are a rigid shape that locked in together.

21
Q

What does induced fit model suggest

A

Prior to binding substrate and active site aren’t completely complementary in shape. When substrate binds the active site alters shape and moulds around substrate.

22
Q

What evidence is there to support induced fit model

A

X-ray diffraction techniques allow for 3D pictures of molecules to be formed. Can take pictures of enzyme before and after bond to see if it changes shape.

23
Q

What are changes in shape known as

A

Conformational changes

24
Q

How does a conformational change support the enzyme

A

It maximises the ability of the enzyme to catalyse the reaction

25
Q

What do lower temperatures do to reactions

A

Prevent or slow them down

26
Q

What do higher temperatures do to reactions

A

Speed them up

27
Q

What happens if temperature is too high

A

Rate at which enzyme catalyses a reaction drops sharply. Enzymes starts to denature

28
Q

How does pH affect enzymes

A

Below or Above optimum pH of enzyme, solutions with too much H+ ions (acidic) and OH- ions (alkaline) can cause bonds to break.

29
Q

How can you estimate an enzymes optimum pH

A

Where an enzyme functions can be an indicator of its optimal pH.

30
Q

How can you investigate the effect of pH on the rate of enzyme - catalysed reactions

A

Use buffer solutions of different pHs to measure the rate of reaction at different pH values. Buffer solutions will maintain their pH. Use same volume of each buffer solution when adding to reaction mixture.

31
Q

How can you work out the pH of a solution if the hydrogen ion (H+) concentration is known

A

Put in calculator: -log(H+)

32
Q

How does Enzyme concentration affect rate of reaction

A

If enzyme concentration is fixed but the concentration of substrate is increased past a certain point, all available active sites eventually become saturated and any further increase in substrates won’t increase rate of reaction. Substrates will begin to ‘queue up” for an active site instead.

33
Q

What is it known as when substrates must queue up for an active site

A

Vmax (velocity = V)

34
Q

What are the two types of reversible inhibitors

A

Competitive inhibitors and Non competitive inhibitors

35
Q

What do competitive inhibitors do

A

Have a similar shape to that of the substrate molecules and therefore compete with substrate for active site.

36
Q

What do non competitive inhibitors do

A

Bind to enzyme at an alternative site which alters the shape of the active site

37
Q

What else other than reducing or stopping enzyme activity can reversible inhibitors do

A

Act as regulators in metabolic pathways so that no single enzyme can ‘run wild’ and continuously and uncontrollably generate more and more of a particular product.

38
Q

How can metabolic reactions be controlled

A

Using the end - product of a particular sequence of metabolic reactions as a non - competitive, reversible inhibitor.

39
Q

How is the process of enzymes converting substrates to products slowed down by itself

A

The end - product of the reaction chain binds to alternative sites of the original enzyme, changing the shape of the active site ad preventing the formation of more enzyme substrate complexes.It can then detach and be used elsewhere. Allows active site to reform.

40
Q

What happens as you increase concentration of inhibitors

A

Rate of reaction decreases or can stop completely

41
Q

How can you counter competitive inhibitors

A

Increase substrate concentration

42
Q

Does increasing substrate concentration help counter non - competitive inhibitors

A

No