Enzymes Flashcards

1
Q

Enzymes are proteins that ___ the rates of biochemical reactions; ___

A

increase, biological catalysts

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2
Q

Enzymes make up ____ ____ such as those that synthesize new molecules and generate __ ____

A

metabolic pathways, cellular energy

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3
Q

Three distinct features of enzymes

A
  1. Catalytic power
  2. Specificity
  3. Regulation
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4
Q

Increases the rates of biochemical reactions as much as 10^16

A

Catalytic power

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5
Q

Selectively act upon a substrate to carry out a particular reaction

A

Specificity

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6
Q

Enzyme activity is regulated by a variety of mechanisms

A

Regulation

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7
Q

____ ____ increase the rates of biochemical reactions as much as __

A

catalytic power, 10^16

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8
Q

_____ selectively act upon a ____ to carry out a ____ reaction

A

specificity, substrate, particular

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9
Q

____ enzyme activity is regulated by a ___ of mechanisms

A

regulation, variety

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10
Q

How many fundamental categories can enzymes be classified in?

A

6 fundamental categories

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11
Q

Fundamental Enzyme Category:
Oxidoreductases

A

Transfer electrons from one molecule to another

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12
Q

Fundamental Enzyme Category:
Transferases

A

Transfer chemical groups

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13
Q

Fundamental Enzyme Category:
Hydrolases

A

Break covalent bonds by hydrolysis

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14
Q

Fundamental Enzyme Category:
Lyases

A

Cleave various bonds, or add groups to double bonds

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15
Q

Fundamental Enzyme Category:
Isomerases

A

Produce isomers

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16
Q

Fundamental Enzyme Category:
Ligases

A

Join large molecules by forming covalent bonds

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17
Q

Oxidoreductases ____ ____ from one molecule to another

A

transfer electrons

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18
Q

Transferases transfer ___ ___

A

chemical groups

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19
Q

Hydrolases break ____ ____ by hydrolysis

A

covalent bonds

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20
Q

Lyases ____ various bonds, or ___ groups to ___ ____

A

cleave, add double bonds

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21
Q

Isomerases _____ isomers

A

produce

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22
Q

Ligases join ____ ____ by forming ___ ____

A

large molecules, covalent bonds

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23
Q

Cofactors are ___ ___ or ___ ____ that bond to enzymes and are required for ___ ____

A

metal ions, organic molecules, enzyme activity

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24
Q

Coenzymes are ___ ___ (B-vitamin derivatives) that act as ___ ____

A

organic molecules, enzyme cofactors

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25
Q

Prosthetic groups are tightly bound ___ or ____

A

cofactors or coenzymes

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26
Q

Holoenzyme are _____ ___ complex of ___ and _____

A

catalytically active, protein and coenzyme

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27
Q

Apoenzyme are ___ without the ___ ___

A

proteins, prosthetic group

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28
Q

Holoenzyme are made of ___ and ____

A

protein and coenzyme

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29
Q

Coenzymes are ___ ___

A

organic molecules

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30
Q

Cofactors are ___ or ____

A

metal ions or organic molecules

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31
Q

Prosthetic groups are ____ or ____

A

cofactors or coenzymes

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32
Q

Apoenzymes are ____

A

proteins

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33
Q

Understanding the rates and processes of chemical reactions is ____

A

chemical kinetics

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34
Q

velocity (v) or the ____ ___ ____, is the amount of ___ formed or the amount of __ consumed per unit of time

A

rate of the reaction, P, A

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35
Q

The velocity (or rate) is ______ to the concentration of __

A

proportional, A

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36
Q

What is the proportionality constant or rate constant?

A

k

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37
Q

v=k[A] is the equation for what?

A

first order reaction

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38
Q

The Michaelis-Menten Equations is a

A

kinetics of enzyme-catalyzed reaction

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39
Q

v=k[A][B] is the equation for what?

A

second order reaction

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40
Q

In a __ ___ ___, there is a directly proportionate relationship between substrate concentration and the amount of produce produced per unit time

A

first order reaction

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41
Q

The Michaelis-Menton equation __ is no longer dependent on __ and the equation is obeying __ __ __

A

v, [S], zero-order kinetics

42
Q

The Michaelis-Menton equation is __ ___ ____

A

zero order reaction

43
Q

What equation is used for the kinetics of enzyme catalyzed reactions?

A

Michaelis-Menton equation

44
Q

The M/M equation gives the rate of an enzyme reaction (v) in terms of what?

A

substrate concentration

45
Q

What are the two constants in the M/M equation?

A

Vmax, Km

46
Q

When substrate concentration is high, v=_____

A

v=Vmax

47
Q

When substrate concentration is high, v is no longer dependent on what?

A

substrate concentration

48
Q

When substrate concentration is high, the reaction is following what order kinetics?

A

zero

49
Q

When substrate concentration is low, the reaction is following what order kinetics?

A

first

50
Q

What variables are fixed in the M/M equation?

A

temp, pH, and ionic strength

51
Q

v=(vmax/Km)*[S] is the equation for when the substrate concentration is __

A

low (first order)

52
Q

The M/M equation for an enzyme-catalyzed reaction describes a ___ ___

A

hyperbolic curve

53
Q

What is the shape of the curve of the M/M equation?

A

hyperbolic curve

54
Q

A __ __ is a curve that approaches but never reaches the max value

A

hyperbolic curve

55
Q

v=

A

product produced/unit time

56
Q

Km is the ___ ___ at which the rate of the reaction, v, is ___ ____ since v=1/2Vmax when [S]=Km

A

substrate concentration, half maximal

57
Q

At Vmax/2, what is equal to what?

A

substrate, enzyme

58
Q

Km is a measure of what?

A

amount of substrate/unit volume

59
Q

Kcat is the value for what?

A

catalytic constant/turnover number

60
Q

Kcat measures the __ amount of product produced per second when the enzyme is ___ with the substrate

A

maximum, saturated

61
Q

Kcat ___ greatly for different enzymes

A

varies

62
Q

What is the pH that most enzymes have peak activity?

A

7.4

63
Q

Kcat must be determined and compared under what type of conditions?

A

the same

64
Q

Kcat is similar to what other value?

A

Vmax of the M/M equation

65
Q

Kcat is determined under ___, standard conditions

A

fixed

66
Q

The activity most enzymes have a peak at around __

A

40 degrees C

67
Q

Kcat values are high/low because of what two things?

A
  1. efficiency of the enzyme
  2. nature of substrate (large, complex vs small, simple)
68
Q

Staphylococcal nuclease has a __ Kcat

A

low (95)

69
Q

Carbonic anhydrase has a __ Kcat

A

high (1,000,000)

70
Q

[S] large =

A

zero order kinetics

71
Q

[s] very small =

A

first order kinetics

72
Q

What does enzyme staphylococcal nuclease do?

A

attack DNA, RNA, and other molecules

73
Q

Why does carbonic anhydrase have such a high kcat?

A

CO2 and H2O are simple and small molcules

74
Q

There’s no activity at too low or too high of pH because of the interaction of what part of the amino acid?

A

positively or negatively charged side chains

75
Q

___ is an enzyme that breaks down food in the stomach, and is therefore at peak activity at a ___ pH of ___

A

pepsin, low, 1.5

76
Q

___ is an enzyme that breaks down food in the intestines and has peak activity at pH 7.7

A

trypsin, 7.7

77
Q

What in the stomach makes it acidic?

A

HCl

78
Q

At low temps, enzyme activity is ___ due to lack of energy

A

slowed

79
Q

At high temps, enzyme activity might undergo irreversible ____

A

denaturing (unfolding)

80
Q

denaturing of enzymes causes lack of ___

A

activity

81
Q

What are the two reversible enzyme inhibitors?

A
  1. Competitive Inhibitors
  2. Noncompetitive inhibitors
82
Q

Competitive inhibitors are _____ _____ ____

A

reversible enzyme inhibitors

83
Q

Noncompetitive inhibitors are ___ ____ ___

A

reversible enzyme inhibitors

84
Q

the ____ and _____ bind to the same site (the active site) on the enzyme in a ____ ____

A

substrate (S) and inhibitor (I), competitive inhibitor

85
Q

the inhibitor binds to a site different from the active site and brings about a _____ ____ that _____ enzyme activity in a _______ _____

A

conformational change, reduces, noncompetitive inhibitor

86
Q

What are the two types of noncompetitive inhibitors?

A

Mixed & pure

87
Q

Mixed inhibitors ____ kcat and ___ substrate binding (Km)

A

decrease, change

88
Q

Pure inhibitors are _____

A

uncommon

89
Q

Pure inhibitors _____ kcat, but ____ affect substrate binding (Km)

A

decrease, don’t

90
Q

A competitive inhibitor is similar in ___ and __ to the normal substrate.

A

size, shape

91
Q

A competitive inhibitor cannot undergo a ___ ____

A

chemical reaction

92
Q

The inhibitor and substrate compete for a binding site to the active site of the enzyme in ___ ___

A

competitive inhibition

93
Q

The inhibitor and substrate bind to different sites in __ ____

A

noncompetitive inhibition

94
Q

Binding of the inhibitor ____ the activity of the enzyme and therefore decreases Kcat and Vmax in noncompetitive inhibition

A

decreases

95
Q

Inhibitors might make it so the substrate is ___ bound to the enzyme.

A

loosely

96
Q

Inhibitors decrease the ____ of the subsrate/reaction

A

Vmax

97
Q

Inhibitos increase ____ of the substrate/reaction

A

Km

98
Q

Irreversible inhibitors binds ____ to the enzyme, usually by ___ ___

A

irreversibly, covalent bonds

99
Q

____ substrates generate a reactive group that forms a covalent bond during binding the active site.

A

suicide

100
Q

Penicillin is an example of ___ substrate

A

suicide

101
Q

Penicillin forms a covalent bond with an enzyme involved in the synthesis of what?

A

bacterial cell walls.