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Biochem > Enzyme kinetics > Flashcards

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
Q

Conversion of substrate into products via enzymatic pathways

A

Enzymatic reaction

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26
Q

Factors affecting enzyme kinetics

A

Substrate concentration
Enzyme concentration
pH
Temperature
Presence of co-factors
Presence of inhibitors

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27
Q

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

A

Substrate Concentration

28
Q

In normal biological conditions, substrate concentration is ____ than enzyme concentration.

A

Higher

29
Q

pH at activity of a particular enzyme is at max

A

Optimum pH

30
Q

Enzymes have optimum pH with the same location they operate. Example

A

PEPSIN (opt pH 1.5; pH of the stomach)

31
Q

If the reaction in activity is reversible, the enzyme has been

A

Denatured

32
Q

If the reaction in activity is not reversible, the enzyme has been

A

Digested

33
Q

T or F
Optimum temp of most human enzymes is about that of body temp (98.6F)

A

T

34
Q

Some enzymes need additional subs called ____ to induce reaction

A

Cofactors

35
Q

Cofactor which is an organic compound

A

Coenzyme

36
Q

Cofactor which is a metal ion

A

Metal ion activator

37
Q

Substances that reduce the rate of enzyme activity by binding with the enzyme and inteferring the formation of enzyme-substrate complex

A

Inhibitors

38
Q

Study of how enzymes bind with the substrate and convert them intro product

A

Enzyme kinetics

39
Q

Optimum temp of human enzymes

A

Same with body temp (98.6 F)

40
Q

Some enzymes are not capable of catalytic activity by themselves, other need addtl subs called ___ to induce reax

A

Cofactors

41
Q

Cofactor that is an organic compound

A

Coenzyme

42
Q

Cofactor that is a metal ion

A

metal ion activator

43
Q

When cofactor is not present, the activity of enzyme ____

A

dramatically reduced

44
Q

Substances that reduce the rate of enzyme activity by binding with the enzyme and interferring the formation of enzyme-substrate complex

A

Inhibitors

45
Q

Study of how enzymes bind with the substrate and convert them into product

A

Enzyme kinetics

46
Q

number of substrate mol converted into product per active site per second

A

Turnover number

47
Q

Conservation equation on enzyme

A

[E] = [Eo] - [ES]

48
Q

In Michaelis menten type kinetics, reaction rate is ____ at relatively low values of concentration

A

1st order

49
Q

In Michael-Menten Type Kinetics, when substrate concentration increases, reaction order _______

A

diminishes continuously from 1-0

50
Q

In Michael-Menten Type Kinetics, rate of reaction is proportional to the _____

A

amount of enzyme present

51
Q

Low substrate concentration equation of Michael Menten Kinetics

A

v = (Vmax/Km) ([S])

52
Q

In Michaelis menten type kinetics, reaction rate is ____ at high values of substrate concentration

A

Oth order

53
Q

High substrate concentration equation of Michael Menten Kinetics

A

v = Vmax

54
Q

The higher the substrate concentration, the higher the ____ until it reaches a ____

A

rate of reaction, plateau

55
Q

The higher the substrate concentration, the higher the

A
56
Q

Happens when enzyme is saturated

A

Reaches a plateau

57
Q

Substrate concentration equivaent to hafway to Vmax

A

Km (Michaelis Menten constant)

58
Q

Proposed rapid equilibrium assumption

A

Henri & Michaelis- Menten

59
Q

Dissociation constant in rapid equilibrium assumption

A

Km = k-1/k1

60
Q

In rapid eq assumption, Vmax changes as more ______

A

enzymes added

61
Q

In rapid eq assump, high substrate will ____ vmax

A

not affect

62
Q

In rapid eq assump, the value of Km _____

A

Decreases (enzyme has a high affnity with substrate)

63
Q

Proposed quasi steady state assumption

A

GE Briggs and JBS Haldane

64
Q

Used for reax in a well-mixed closed vessel provided that So&raquo_space; Eo

A

Quasi-steady state assumption

65
Q

Ability of enzyme to enhnace the rate of a chem

A

Catalytic power

Biochem (2 decks)

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