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Biochemistry > Unit 5 - Enzymes > Flashcards

Unit 5 - Enzymes Flashcards

1
Q

What structure are enzymes in to be functional?

A

Quaternary

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2
Q

What are enzymes composed of?

A

Subunits or protomers grouped together

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3
Q

How many subunits do enzymes need to be functional?

A

All of them

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4
Q

Isoenzymes

A

Different forms of enzymes that catalyze the same reaction

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5
Q

Subunits

A

AKA promoters
Grouped together to form a fully functional enzyme

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6
Q

Function of enzymes

A

Increase rate of a reaction

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7
Q

Enzymes only increase the rate of a reaction not…

A

create a reaction that wouldn’t normally occur

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8
Q

How do enzymes increase rate of reaction?

A

Lower activation energy

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9
Q

Where do enzymes get synthesized?

A

Intracellularly

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10
Q

Specific enzyme synthesis markers

A

PSA - prostate only
CK - heart and skeletal muscle

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11
Q

Wide variety synthesis markers

A

LD - Different tissues
ALP - Bone Liver Intestine Placenta (BLIP)

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12
Q

Why is half life important in measuring enzymes?

A

You know if cell damage was recent or not

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13
Q

Active site

A

Catalytic site of enzyme

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14
Q

Where do substrates bind

A

Active site

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15
Q

Law of mass action

A

Direction of reaction from high concentration to low concentration

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16
Q

Enzyme cofactors bind what

A

Bind allosteric site

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17
Q

What do enzymes need to work?

A

Cofactors

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18
Q

Apoenzyme

A

Protein part of enzyme WITHOUT cofactor

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19
Q

Holoenzyme

A

Functional enzyme with cofactors/all parts

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20
Q

Are cofactors consumed after the reaction?

A

No

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21
Q

Types of cofactors

A

Activators
Coenzymes
Prosthetic groups

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22
Q

Activator cofactors

A

Inorganic ions like ca or mg

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23
Q

Coenzyme cofactor

A

Non protein organic compound (NAD/NADH)

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24
Q

Prosthetic group cofactor

A

Cofactor bound so tightly it looks like its part of the enzyme

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25
Q

Stereoisomeric specificity

A

Enzymes that only work with a specific isomer (3d config)

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26
Q

Isomer

A

3D configuration

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27
Q

When would enzymes release?

A

When there’s damage to cells

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28
Q

Enzyme activity

A

Amount of substrate converted to a product in a given period of time

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29
Q

Standard International Unit of Enzyme Activity

A

Quantity of enzyme that catalyzes a rxn of one micromole of substrate per minute

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30
Q

Enzyme equilibrium (Michaelis-Menten)

A

Point where product is formed from substrate at a constant RATE

31
Q

Rate =

A

Velocity under constant conditions

32
Q

Constant rate of the enzyme run is proportional to

A

Amount of Substrate available
Amount of Enzyme available
How much enzyme-substrate complex made
How much product made

33
Q

What is the rate limiting factors of an enzyme reaction

A

Substrate

34
Q

Km

A

M-M constant (1/2 Vmax)
Substrate concentration at which enzyme catalyzes 1/2 as fast as it can

35
Q

Low substrate concentration

A

Enzyme makes product slowly

36
Q

First order kinetics

A

Product formation depends on substrate concentration
(low substrate)

37
Q

High Substrate concentration

A

Enzyme makes product faster

38
Q

Vmax

A

Maximum velocity

39
Q

Zero order kinetics

A

Substrate in excess relative to enzyme
(high substrate concentration)

40
Q

Mixed order kinetics

A

Center of the graph where its not predictable

41
Q

Which part of the MM curve shows zero order kinetics

A

The top where Vmax is

42
Q

Which part of the MM curve shows first order kinetics

A

The bottom where the initial velocity is slow because there less substrate

43
Q

When Km is determined, what do you have to do with the conditions that achieved that?

A

Keep them the same, they have to be exactly duplicated

44
Q

What should be in excess for expected enzyme concentration?

A

Substrate

45
Q

What should be in excess for expected substrate concentration?

A

Enzyme

46
Q

What does the Km have to be multiplied by for enzyme concentration?

A

Multiply Km by 10-100 fold

47
Q

What does the Km have to be substrate concentration?

A

Half of Km

48
Q

What does it mean if one substrate has a higher Km than the other?

A

Low affinity, requires more enzyme to do the job

49
Q

What does it mean if one substrate has a lower Km than the other?

A

High affinity, requires less enzyme to do the job

50
Q

Do you want a substrate with a low Km or high Km?

A

Low Km

51
Q

International standard temp

A

30C

52
Q

Frequently used temp for enzymes

A

37C

53
Q

Lag period

A

Little product formed, reaction getting started

54
Q

Linear period

A

Equilibrium attained
Product formed at a constant rate (Vmax)

55
Q

Nonlinear period

A

No additional product formed, substrate exhaustion

56
Q

The more product formed per minute…

A

The more enzyme activity, the more enzyme concentration

57
Q

When using enzyme to measure substrate, what do you want in excess?

A

Enzyme or co-factors

58
Q

When using enzyme to measure substrate, what controls the rate of the reaction

A

Substrate

59
Q

When using enzyme to measure substrate, what order kinetics must be observed?

A

First, you want low substrate to find the linearity point

60
Q

What is on the x and y axis of a line weaver burk plot

A

Y: 1/Vmax
X: -1/Km

61
Q

Which plot is used to study inhibitor activity?

A

Lineweaver burk plot

62
Q

If the X intercept moves to the left, what does that mean for the Km?

A

Km lower
Better enzyme activity

63
Q

If the X intercept moves to the right, what does that mean for the Km?

A

Km is higher
Worse enzyme activity

64
Q

If the Y intercept moves up, what does that mean for the reaction?

A

Slowing down

65
Q

IF the Y intercept moves down, what does that mean for the reaction?

A

Going faster

66
Q

How do competitive inhibitors affect Km?

A

Km increases because more normal substrate needed to perform the same amount of enzyme activity

67
Q

How do competitive inhibitors affect Vmax?

A

Vmax not affected because enough normal substrate can overcome inhibitor because of the large concentration

68
Q

moves to right and up

A

worse enzyme

69
Q

moves left and down

A

better enzyme

70
Q

How does noncompetitive inhibition affect Km

A

No effect because there are still normal enzymes that are doing the reaction at that linear speed

71
Q

Where do noncompetitive inhibitors bind

A

Allosteric site instead of active site

72
Q

How does noncompetitive inhibition affect Vmax

A

Decrease
More enzyme is required to produce a product because enzyme are having their conformation changed

73
Q

What is uncompetitive inhibition and hwo does it affect Km/Vmax

A

Binds enzyme-substrate complex
affects both

Biochemistry (26 decks)

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