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Biochemistry > Unit 5 - Enzymes > Flashcards

Unit 5 - Enzymes Flashcards

(73 cards)

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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
Stereoisomeric specificity
Enzymes that only work with a specific isomer (3d config)
26
Isomer
3D configuration
27
When would enzymes release?
When there's damage to cells
28
Enzyme activity
Amount of substrate converted to a product in a given period of time
29
Standard International Unit of Enzyme Activity
Quantity of enzyme that catalyzes a rxn of one micromole of substrate per minute
30
Enzyme equilibrium (Michaelis-Menten)
Point where product is formed from substrate at a constant RATE
31
Rate =
Velocity under constant conditions
32
Constant rate of the enzyme run is proportional to
Amount of Substrate available Amount of Enzyme available How much enzyme-substrate complex made How much product made
33
What is the rate limiting factors of an enzyme reaction
Substrate
34
Km
M-M constant (1/2 Vmax) Substrate concentration at which enzyme catalyzes 1/2 as fast as it can
35
Low substrate concentration
Enzyme makes product slowly
36
First order kinetics
Product formation depends on substrate concentration (low substrate)
37
High Substrate concentration
Enzyme makes product faster
38
Vmax
Maximum velocity
39
Zero order kinetics
Substrate in excess relative to enzyme (high substrate concentration)
40
Mixed order kinetics
Center of the graph where its not predictable
41
Which part of the MM curve shows zero order kinetics
The top where Vmax is
42
Which part of the MM curve shows first order kinetics
The bottom where the initial velocity is slow because there less substrate
43
When Km is determined, what do you have to do with the conditions that achieved that?
Keep them the same, they have to be exactly duplicated
44
What should be in excess for expected enzyme concentration?
Substrate
45
What should be in excess for expected substrate concentration?
Enzyme
46
What does the Km have to be multiplied by for enzyme concentration?
Multiply Km by 10-100 fold
47
What does the Km have to be substrate concentration?
Half of Km
48
What does it mean if one substrate has a higher Km than the other?
Low affinity, requires more enzyme to do the job
49
What does it mean if one substrate has a lower Km than the other?
High affinity, requires less enzyme to do the job
50
Do you want a substrate with a low Km or high Km?
Low Km
51
International standard temp
30C
52
Frequently used temp for enzymes
37C
53
Lag period
Little product formed, reaction getting started
54
Linear period
Equilibrium attained Product formed at a constant rate (Vmax)
55
Nonlinear period
No additional product formed, substrate exhaustion
56
The more product formed per minute...
The more enzyme activity, the more enzyme concentration
57
When using enzyme to measure substrate, what do you want in excess?
Enzyme or co-factors
58
When using enzyme to measure substrate, what controls the rate of the reaction
Substrate
59
When using enzyme to measure substrate, what order kinetics must be observed?
First, you want low substrate to find the linearity point
60
What is on the x and y axis of a line weaver burk plot
Y: 1/Vmax X: -1/Km
61
Which plot is used to study inhibitor activity?
Lineweaver burk plot
62
If the X intercept moves to the left, what does that mean for the Km?
Km lower Better enzyme activity
63
If the X intercept moves to the right, what does that mean for the Km?
Km is higher Worse enzyme activity
64
If the Y intercept moves up, what does that mean for the reaction?
Slowing down
65
IF the Y intercept moves down, what does that mean for the reaction?
Going faster
66
How do competitive inhibitors affect Km?
Km increases because more normal substrate needed to perform the same amount of enzyme activity
67
How do competitive inhibitors affect Vmax?
Vmax not affected because enough normal substrate can overcome inhibitor because of the large concentration
68
moves to right and up
worse enzyme
69
moves left and down
better enzyme
70
How does noncompetitive inhibition affect Km
No effect because there are still normal enzymes that are doing the reaction at that linear speed
71
Where do noncompetitive inhibitors bind
Allosteric site instead of active site
72
How does noncompetitive inhibition affect Vmax
Decrease More enzyme is required to produce a product because enzyme are having their conformation changed
73
What is uncompetitive inhibition and hwo does it affect Km/Vmax
Binds enzyme-substrate complex affects both

Biochemistry (26 decks)

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