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Bio 2 (Let's go Chagnon) > Proteins as Catalysts > Flashcards

Proteins as Catalysts Flashcards

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1
Q

They allow reactions in living cells to use less energy to start a reaction

A

Enzymes

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2
Q

What is the effect of enzymes on the activation energy?

A

It lowers the activation energy required for a reaction to occur.

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3
Q

Enzymes are ___ by the reaction

A

recycled

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4
Q

Most enzymes are___

A

proteins

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5
Q

Some enzymes are ___

A

RNA or ribosymes

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6
Q

Some enzymes work as a ___

A

complex of many enzymes

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7
Q

What are ribozymes?

A

RNA with enzymatic abilities

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8
Q

Assists in synthesizing proteins

A

Ribosomal RNA

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9
Q

Keeps reactants of the same pathway close together and accessible.

A

Pyruvate dehydrogenase Complex

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10
Q

What are the advantages of multienzymes complexes?

A
  • Product of one reaction can be directly delivered to the next enzyme
  • Possibility of unwanted side reactions is eliminated
  • All of the reactions can be controlled as a unit
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11
Q

Enzyme interacts with__

A

substrate (they bind to it)

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12
Q

Molecule that will undergo a reaction either to make or break a bond

A

Substrate

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13
Q

Catalyze only one particular reaction

A

Absolute specificity

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14
Q

Other enzymes will be specific for a particular type of chemical bond or functional group.

A

OK

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15
Q

The enzyme SUCRASE splits _____ into ____ and ___

A

splits sucrose into fructose and glucose

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16
Q

Enzymes are indicated by the suffix ____

A

–ASE (protein enzyme mostly)

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17
Q

The prefix SUCR- indicates what?

A

It indicates the substrate acted on by the enzyme

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18
Q

Region of the enzyme that binds the substrate and causes the change

A

Active site

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19
Q

Active site on enzyme binds on ____

A

Specific substrates

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20
Q

Formula for enzyme activity

A

E + S ES complex —-> E + P

E: enzyme, S: substrate, P: product

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21
Q

Binding substrate causes the enzyme to ____

A

Change shape, producing a better induced fit between the molecules

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22
Q

Induced Fit Model ways (3)

A
  • Substrate squeezes into active site
  • Active site changes shape slightly
  • Exerts force on substrate
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23
Q

The binding of the substrate and enzyme places stress on the glucose-fructose bond and the bond breaks

A

OK

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24
Q

Moving potential energy around during metabolism is done by _____

A

moving electrons (requires electron carriers)

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25
Q

To help carry electrons or small chemical groups, some enzymes require additional molecules called _______

A

cofactors (they are reusable, like enzymes)

i.e. ZN(+), Fe(+)

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26
Q

Usually metal ions (inorganic)

A

Cofactors

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27
Q

Non-protein molecules (organic), often used to carry electrons in RedOx reactions

A

Coenzymes

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28
Q

Cytoplasmic and mitochondrial coenzymes : _______ and _____

A

FAD and NAD(+)

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29
Q

Chloroplast coenzyme: ____

A

NADP(+) (used in plants during carbon fixation in photosynthesis)

30
Q

An enzyme without a coenzyme does not work. Why?

A

Coenzyme is the activator

31
Q

NAD(+) and FAD used in production of __

A

ATP

32
Q

Give the 4 factors that can change an enzyme’s 3D shape.

A

pH
temperature
salt
regulatory molecules (inhibition)

33
Q

When environmental conditions exceed the limitations of a protein the secondary, tertiary and quaternary bonds are overcome (broken), it is called _____

A

Denaturation of Protein

34
Q

Denaturation results from degradation of these bonds
The protein (enzyme) will no longer function
Damage is permanent (irreversible)

A

If the change is extreme

35
Q

What in conditions may only temporarily alter protein (reversible) but will affect the time it takes to convert substrate to product?

A

Mild change

36
Q

Enzyme activity may be affected by ___(2 factors)

A
  1. Concentration factors
  2. Efficiency factors due shape of enzyme

Environmental conditions can affect enzyme activity

37
Q

Concentration factors

A

Substrate

Enzyme

38
Q

Enzyme shape can be affected by (3)

A

pH
Temperature
Salt

39
Q

The activity of an enzyme may be increased with increasing T, up to an optimum T due to motion of molecules. However, temperatures too far above T optimum can denature the enzyme, destroying its function

A

OK

40
Q

pH can disrupt ionic bonds

A

okidou

41
Q

Dependent on the type of enzyme.

A

Optimum levels

42
Q

Function at an optimum pH and temperature

A

Enzymes

43
Q

Used to control the amount of product

A

Regulation of metabolism

44
Q

Helps maintain homeostasis

A

Regulation of metabolism

45
Q

Controls pathways by slowing down production of END-PRODUCT

A

Inhibitor (they block or slow down the enzyme activity)

46
Q

End-product resembles closely an earlier substrate in the pathway and can bind to the final enzyme in the pathway

A

End-product inhibition

47
Q

When the pathways product is temporarily not needed by the cell, it begins to accumulate

A

Principle of feedback inhibition

48
Q

Higher concentration of product accumulates thus end-product begins to out-compete with the initial substrate concentration.

A

Principle of feedback inhibition

49
Q

Since end-product resembles the initial substrate, product will bind reversibly to the initial enzyme

A

Principle of feedback inhibition

50
Q

The normal substrate can no longer bind to this inhibited enzyme, as long as the inhibitor stays bound to the enzyme

A

Principle of feedback inhibition

51
Q

Pathway is blocked until the product is used by the cell, thus decreasing its concentration

A

Principle of feedback inhibition

52
Q

the end-product and initial substrate have a similar structure thus both recognize the enzyme (E1)

A

negative feedback control

53
Q

Compete with the substrate for binding to the same active site

A

competitive inhibitors

54
Q

bind to the allosteric site (site other than the enzyme’s active site)

A

noncompetitive inhibitors

55
Q

Interferes with active sites of enzyme so substrate cannot bind

A

Competitive inhibition

56
Q

Changes shape of enzyme so the active site does not bind the enzyme as well

A

Noncompetitive inhibition

57
Q

Possess an allosteric site different from the active site

A

Allosteric enzymes

58
Q

Can be inactivated or activated by the molecule binding

A

Allosteric enzymes

59
Q

Bind to the allosteric site to inactivate the enzyme

A

Allosteric inhibitors

60
Q

Bind to the allosteric site to activate the enzyme

A

Allosteric activators

61
Q

Important in cell signalling

A

Allosteric activation

62
Q

Controls many pathways

A

Allosteric inhibition

63
Q

Measures how much the substrate and enzyme like each other and meet to convert substrate to product

A

Affinity = Km

64
Q

A function of concentration and reaction rate

A

Affinity = Km

65
Q

The lower the [substrate]

A

the higher the affinity for the enzyme

66
Q

Due to low number of substrate encountering active site of enzymes

A

Initial reaction rates are slow

67
Q

If a substrate has a high attraction to the active site then________

A

the affinity is high.

68
Q

Represents the maximum rate the enzyme is capable of working to convert substrate to product, and represents enzyme saturation

A

Maximum velocity (Vmax)

69
Q

Concentration of substrate at ½ Vmax

A

Km

70
Q

Km (affinity) does not change, but max velocity is decreased.

A

Effect of noncompetitive inhibition on Km

71
Q

Result is the Km (affinity) changes, but max velocity is the same.

A

Effect of competitive inhibition on Km

Bio 2 (Let's go Chagnon) (13 decks)

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