Enzyme kinetics Flashcards

1
Q

Speeds up reaction

A

Catalyst

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2
Q

Lowers temp or pressure w/o being consumed

A

Catalyst

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3
Q

Lowers activation energy

A

Catalyst

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4
Q

Energy barrier that must be surmounted for a chemical reaction to occur

A

Activation energy

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5
Q

Lowers activation energy by forming enzyme-substrate complex

A

Enzymes

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6
Q

structure is highly specific to the reaction they catalyze

A

Enzymes

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7
Q

Responsible for making or building of chemical bonds

A

Enzymes

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8
Q

Held together by weak bonds to allow dissociation of the complex when the reaction is finished

A

Enzyme-substrate complex (ES)

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9
Q

3 types of enzymes

A

Medical
Industrial
Analytical

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10
Q

Examples of medical enzymes

A

Asparaginase, proteases, lipases, streptokinase

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11
Q

Examples of industrial enzymes

A

Lipase, proteases, glocose isomerase

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12
Q

Examples of analytical enzymes

A

Glucose oxidase, alcohol dehydrogenase

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13
Q

Globular proteins with an active site that acts as catalyst in living organisms, regulating the rate at which the chemical reaction proceed without itself being altered

A

Enzymes

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14
Q

Lowers activation energy, where the catalysis takes place or where cjem reac occurs

A

Active site

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15
Q

Specific region of an enzyme where the substrate binds

A

Active site

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16
Q

Structural element of protein

A

Active site

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17
Q

Small cleft within an enzyme with a specific wmino acid structure allowing the substrate to bind

A

Active site

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18
Q

Complementary to its specific substrate shape

A

Active site

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19
Q

2 models for active sites

A
  • Lock and key model
  • Induced fit model
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20
Q

Model where active sites perfect for the substrate, does not require any changes to bind

A

Lock and key model

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21
Q

Model where active sites is almost complementary to the substrate but when it binds, the enzyme undergoes changes to make the shape better

A

Induced fit model

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22
Q

More accepted model in interaction of active sites

A

Induced fit model

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23
Q

Reaction rate of an enzyme reaction and factors associated with it

A

Enzyme kinetics

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24
Q

Developed to estimate the product yield, selectivity, and reaction time

A

Enzyme kinetics

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25
Conversion of substrate into products via enzymatic pathways
Enzymatic reaction
26
Factors affecting enzyme kinetics
Substrate concentration Enzyme concentration pH Temperature Presence of co-factors Presence of inhibitors
27
As this increases, each enzyme can locate and react more substrate mol and if low conc, each enzyme is reacting with fewer subs mol than suggested turnover number
Substrate Concentration
28
In normal biological conditions, substrate concentration is ____ than enzyme concentration.
Higher
29
pH at activity of a particular enzyme is at max
Optimum pH
30
Enzymes have optimum pH with the same location they operate. Example
PEPSIN (opt pH 1.5; pH of the stomach)
31
If the reaction in activity is reversible, the enzyme has been
Denatured
32
If the reaction in activity is not reversible, the enzyme has been
Digested
33
T or F Optimum temp of most human enzymes is about that of body temp (98.6F)
T
34
Some enzymes need additional subs called ____ to induce reaction
Cofactors
35
Cofactor which is an organic compound
Coenzyme
36
Cofactor which is a metal ion
Metal ion activator
37
Substances that reduce the rate of enzyme activity by binding with the enzyme and inteferring the formation of enzyme-substrate complex
Inhibitors
38
Study of how enzymes bind with the substrate and convert them intro product
Enzyme kinetics
39
Optimum temp of human enzymes
Same with body temp (98.6 F)
40
Some enzymes are not capable of catalytic activity by themselves, other need addtl subs called ___ to induce reax
Cofactors
41
Cofactor that is an organic compound
Coenzyme
42
Cofactor that is a metal ion
metal ion activator
43
When cofactor is not present, the activity of enzyme ____
dramatically reduced
44
Substances that reduce the rate of enzyme activity by binding with the enzyme and interferring the formation of enzyme-substrate complex
Inhibitors
45
Study of how enzymes bind with the substrate and convert them into product
Enzyme kinetics
46
number of substrate mol converted into product per active site per second
Turnover number
47
Conservation equation on enzyme
[E] = [Eo] - [ES]
48
In Michaelis menten type kinetics, reaction rate is ____ at relatively low values of concentration
1st order
49
In Michael-Menten Type Kinetics, when substrate concentration increases, reaction order _______
diminishes continuously from 1-0
50
In Michael-Menten Type Kinetics, rate of reaction is proportional to the _____
amount of enzyme present
51
Low substrate concentration equation of Michael Menten Kinetics
v = (Vmax/Km) ([S])
52
In Michaelis menten type kinetics, reaction rate is ____ at high values of substrate concentration
Oth order
53
High substrate concentration equation of Michael Menten Kinetics
v = Vmax
54
The higher the substrate concentration, the higher the ____ until it reaches a ____
rate of reaction, plateau
55
The higher the substrate concentration, the higher the
56
Happens when enzyme is saturated
Reaches a plateau
57
Substrate concentration equivaent to hafway to Vmax
Km (Michaelis Menten constant)
58
Proposed rapid equilibrium assumption
Henri & Michaelis- Menten
59
Dissociation constant in rapid equilibrium assumption
Km = k-1/k1
60
In rapid eq assumption, Vmax changes as more ______
enzymes added
61
In rapid eq assump, high substrate will ____ vmax
not affect
62
In rapid eq assump, the value of Km _____
Decreases (enzyme has a high affnity with substrate)
63
Proposed quasi steady state assumption
GE Briggs and JBS Haldane
64
Used for reax in a well-mixed closed vessel provided that So >> Eo
Quasi-steady state assumption
65
Ability of enzyme to enhnace the rate of a chem
Catalytic power