Enzymes/Metabolism Flashcards

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1
Q

What are biochemical processes?

A

Chemical reactions that occur in all cell to produce products required by cells.

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2
Q

What is metabolism?

A

The sum of all biochemical processes in a body.

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3
Q

What do chemical reactions often occur in?

A

Series of steps.

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4
Q

Why do chemical reactions occur in steps?

A

Because cells require a certain amount of energy to maintain the processes of generating products from reactants.

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5
Q

What are the steps of a chemical reaction?

A

Initial reactants -> product A -> product A (using enzyme and cofactor) -> Final product (using enzyme)

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6
Q

What allows the process of a chemical reaction to continue?

A

The final product being removed.

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7
Q

How can the final product be removed?

A

It can be stered or expelled.

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8
Q

What is an anabolic reaction?

A

The synthesis of simple molecules to form more complex ones (monomers into polymers).

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9
Q

What do anabolic reaction require?

A

They usually require energy, this energy usually comes from catabolic reactions.

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10
Q

What type of reaction is an anabolic reaction? Why?

A

Endergonic, because the energy of the reactants is less than that of the products.

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11
Q

What is a catabolic reaction?

A

The breakdown of complex molecules into simpler ones (polymers into monomers).

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12
Q

What do catabolic reactions release?

A

Usually release energy when the chemical bonds are breaking.

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13
Q

What type of reaction is a catabolic reaction? Why?

A

Exergonic, because there is less energy in the products than there was in the reactants.

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14
Q

Draw the cycle of catabolic, anabolic and energy reactions.

A

Check book for answer.

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15
Q

What is the role of internal membranes?

A

Different organelles provide different environments for different chemical reactions to occur in. The internal plasma membrane of cells divide these organelles so they can maintain their own optimum environments and therefore contain their required enzymes.

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16
Q

What is an enzyme?

A

A biological catalyst, usually a protein, that speeds up chemical reactions in cells by lowering the activation energy required.

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17
Q

What are the two types of enzymes?

A

Intracellular and extracellular.

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18
Q

What are intracellular enzymes?

A

Enzymes inside cells.

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19
Q

What are extracellular enzymes?

A

Produced by cells but take effect outside the cells, e..g amylase in saliva.

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20
Q

Are enzymes changed after reactions?

A

Enzymes remain unchanged and can be reusable but over time temperature/acidity can change their shape making them no longer complementary to their substrate.

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21
Q

Can enzymes be used in all types of reactions?

A

Enzymes are only specific to ONE type of reaction.

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22
Q

Why do we need enzymes?

A
  • Without enzymes, the chemical reactions would occur too slowly to maintain life.
  • Over 100 reactions take place in a single cell, enzymes allow organisation of these reactions by having specific functions in a particular place.
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23
Q

What is activation energy?

A

The minimum amount of initial energy required to start a chemical reaction.

24
Q

How is activation energy supplied?

A

Usually supplied in the form of heat energy that reactants absorb from their surroundings.

25
Q

What do enzymes do to activation energy?

A

Enzymes lower the activation energy required for a reaction to take place by destabilising chemical bonds by weakening them.

26
Q

How does an enzyme bind to a substrate and how does an enzyme controlled reaction occur?

A
  • Enzymes have different shapes that allow them to bind to specific reactants (substrates).
  • When an enzyme controlled reaction occurs the enzyme and substrate molecule join for a short time to form an enzyme-substrate complex.
  • Each enzyme has a precise location where the substrate can attach called the active site.
27
Q

What are the two models for enzymes?

A
  • Lock and key model.
  • Induced fit model.
28
Q

What is the lock and key model?

A

The original model, that the folding of the enzyme protein, forms a groove or pocket shaped active site that is highly specific for a particular substrate. The substrate must be of a complementary shape in order for binding to occur - like a lock and key.

29
Q

What is the induced fit model?

A

The more widely accepted model, in which the shape of the enzyme is not fixed. The bonds that form between the enzyme and its substrate are thought to slightly modify the shape of the enzyme so that the substrate can be accommodated.

30
Q

What do the enzymes in the induced fit model have?

A

They have broad specificity. Meaning, substrates still only bind to a few enzymes of a similar shape but there can be a conformational shape change in the active site.

31
Q

What happens to the bonds in the substrate in the induced fit model?

A

The bonds in the substrate molecule are stretched and bent during this interaction which lowers the activation energy required to start the reaction.

32
Q

What happens to the active site after the product is released in the induced fit model?

A

After the product is released the active site returns to its original shape.

33
Q

What is enzyme denaturing?

A

When an enzyme is exposed to heat/acidity not within its optimum range, the shape of the active site may change and its substrate will no longer bind with it.

34
Q

Why can enzymes denature?

A

Enzymes are sensitive to changes in temperature and pH and different enzymes have different optimum ranges of these factors.

35
Q

What happens to enzymes in their optimum temperature?

A

At the optimum temperature molecules are more active and collide more often which increases the opportunity for the substrate to collide with its enzyme.

36
Q

What happens to enzymes at temperatures lower than their optimum?

A

Lower temperatures means lower enzyme action which slows chemical reactions as less substrates are binding with their enzymes.

37
Q

What happens to enzymes at temperatures higher than their optimum?

A

As the temperature increases the amino acids that make up the protein move around more, causing the. hydrogen bonds between them to break, altering the shape of the active site (denaturing).

38
Q

What happens to enzymes in the human body if it overheats?

A

It can cause the enzymes in the brain to denature which can lead to seizures and eventually death as the chemical reactions are not occurring.

39
Q

What is the optimum temperature for most enzymes in the human body?

A

37ºC

40
Q

Do enzymes have the same optimum pH?

A

Some enzymes can work in a broad range of pH, others have a narrow pH range. Not all enzymes have the same optimum pH.

41
Q

What does an enzyme’s optimum pH depend on?

A

The sensitivity of an enzyme to pH depends on the enzyme’s environment, e.g. pepsin in the stomach must have a tolerance for a low pH (acidic) environment.

42
Q

What happens to an enzyme if not in its optimum pH range?

A

If the pH becomes too acidic/alkaline, the shape of the enzyme can change and it becomes denatured.

43
Q

What does increasing the substrate concentration do?

A

Increasing the concentration of substrate increases the amount of product produced until the enzyme molecules are working at maximum capacity.

44
Q

What does increasing the enzyme concentration do?

A

Increasing the amount of enzymes increases the amount of products produced until the substrate is depleted or until the product starts to inhibit enzyme action.

45
Q

What are enzyme concentrations regulated by?

A
  • Controlling the production of the protein.
  • Breaking down the enzyme.
  • Activating the enzyme in response to a stimulus.
46
Q

What are enzyme inhibitors?

A

Some enzymes have two or more active binding sites. These enzymes can move between active states (when activation molecules bind with them) or inactive states (when inhibitors bind with them).

47
Q

What is feedback inhibition?

A

When the product of a reaction inhibits enzyme activity.

48
Q

How does feedback inhibition occur?

A

If a large amount of product is present it can act as an inhibitor by binding to the active site making the enzyme no longer able to bind to its substrate.

49
Q

Why does feedback inhibition occur?

A

To control the concentration of products in a cell.

50
Q

What are the two types of inhibitors?

A
  • Competitive
  • Non-competitive
51
Q

What are competitive inhibitors?

A

Competitive inhibitors have the same share as the enzyme’s substrate and can block the active site.

52
Q

What are non-competitive inhibitors?

A

Non-competitive inhibitors can attach to other sites on the enzyme and cause the shape of the active site to change.

53
Q

What are co-factors?

A

Small inorganic substances e.g. magnesium or zinc ions.

54
Q

What are co-enzymes?

A

Non-protein, organic substances that are required for enzyme activity. Small compared to the enzymes. Can be made from dietary vitamins and act as carriers of substances to and from reactants that are catalysed by enzymes.

55
Q

What do co-factors and co-enzymes do?

A

Some enzymes are inactive until they bind with other molecules or ions that change their conformation. This alters the shape and charge of the enzyme so it can capture substrates and react more efficiently.