Enzymes Flashcards

(101 cards)

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
Prosthetic groups are tightly bound ___ or ____
cofactors or coenzymes
26
Holoenzyme are _____ ___ complex of ___ and _____
catalytically active, protein and coenzyme
27
Apoenzyme are ___ without the ___ ___
proteins, prosthetic group
28
Holoenzyme are made of ___ and ____
protein and coenzyme
29
Coenzymes are ___ ___
organic molecules
30
Cofactors are ___ or ____
metal ions or organic molecules
31
Prosthetic groups are ____ or ____
cofactors or coenzymes
32
Apoenzymes are ____
proteins
33
Understanding the rates and processes of chemical reactions is ____
chemical kinetics
34
velocity (v) or the ____ ___ ____, is the amount of ___ formed or the amount of __ consumed per unit of time
rate of the reaction, P, A
35
The velocity (or rate) is ______ to the concentration of __
proportional, A
36
What is the proportionality constant or rate constant?
k
37
v=k[A] is the equation for what?
first order reaction
38
The Michaelis-Menten Equations is a
kinetics of enzyme-catalyzed reaction
39
v=k[A][B] is the equation for what?
second order reaction
40
In a __ ___ ___, there is a directly proportionate relationship between substrate concentration and the amount of produce produced per unit time
first order reaction
41
The Michaelis-Menton equation __ is no longer dependent on __ and the equation is obeying __ __ __
v, [S], zero-order kinetics
42
The Michaelis-Menton equation is __ ___ ____
zero order reaction
43
What equation is used for the kinetics of enzyme catalyzed reactions?
Michaelis-Menton equation
44
The M/M equation gives the rate of an enzyme reaction (v) in terms of what?
substrate concentration
45
What are the two constants in the M/M equation?
Vmax, Km
46
When substrate concentration is high, v=_____
v=Vmax
47
When substrate concentration is high, v is no longer dependent on what?
substrate concentration
48
When substrate concentration is high, the reaction is following what order kinetics?
zero
49
When substrate concentration is low, the reaction is following what order kinetics?
first
50
What variables are fixed in the M/M equation?
temp, pH, and ionic strength
51
v=(vmax/Km)*[S] is the equation for when the substrate concentration is __
low (first order)
52
The M/M equation for an enzyme-catalyzed reaction describes a ___ ___
hyperbolic curve
53
What is the shape of the curve of the M/M equation?
hyperbolic curve
54
A __ __ is a curve that approaches but never reaches the max value
hyperbolic curve
55
v=
product produced/unit time
56
Km is the ___ ___ at which the rate of the reaction, v, is ___ ____ since v=1/2Vmax when [S]=Km
substrate concentration, half maximal
57
At Vmax/2, what is equal to what?
substrate, enzyme
58
Km is a measure of what?
amount of substrate/unit volume
59
Kcat is the value for what?
catalytic constant/turnover number
60
Kcat measures the __ amount of product produced per second when the enzyme is ___ with the substrate
maximum, saturated
61
Kcat ___ greatly for different enzymes
varies
62
What is the pH that most enzymes have peak activity?
7.4
63
Kcat must be determined and compared under what type of conditions?
the same
64
Kcat is similar to what other value?
Vmax of the M/M equation
65
Kcat is determined under ___, standard conditions
fixed
66
The activity most enzymes have a peak at around __
40 degrees C
67
Kcat values are high/low because of what two things?
1. efficiency of the enzyme 2. nature of substrate (large, complex vs small, simple)
68
Staphylococcal nuclease has a __ Kcat
low (95)
69
Carbonic anhydrase has a __ Kcat
high (1,000,000)
70
[S] large =
zero order kinetics
71
[s] very small =
first order kinetics
72
What does enzyme staphylococcal nuclease do?
attack DNA, RNA, and other molecules
73
Why does carbonic anhydrase have such a high kcat?
CO2 and H2O are simple and small molcules
74
There's no activity at too low or too high of pH because of the interaction of what part of the amino acid?
positively or negatively charged side chains
75
___ is an enzyme that breaks down food in the stomach, and is therefore at peak activity at a ___ pH of ___
pepsin, low, 1.5
76
___ is an enzyme that breaks down food in the intestines and has peak activity at pH 7.7
trypsin, 7.7
77
What in the stomach makes it acidic?
HCl
78
At low temps, enzyme activity is ___ due to lack of energy
slowed
79
At high temps, enzyme activity might undergo irreversible ____
denaturing (unfolding)
80
denaturing of enzymes causes lack of ___
activity
81
What are the two reversible enzyme inhibitors?
1. Competitive Inhibitors 2. Noncompetitive inhibitors
82
Competitive inhibitors are _____ _____ ____
reversible enzyme inhibitors
83
Noncompetitive inhibitors are ___ ____ ___
reversible enzyme inhibitors
84
the ____ and _____ bind to the same site (the active site) on the enzyme in a ____ ____
substrate (S) and inhibitor (I), competitive inhibitor
85
the inhibitor binds to a site different from the active site and brings about a _____ ____ that _____ enzyme activity in a _______ _____
conformational change, reduces, noncompetitive inhibitor
86
What are the two types of noncompetitive inhibitors?
Mixed & pure
87
Mixed inhibitors ____ kcat and ___ substrate binding (Km)
decrease, change
88
Pure inhibitors are _____
uncommon
89
Pure inhibitors _____ kcat, but ____ affect substrate binding (Km)
decrease, don't
90
A competitive inhibitor is similar in ___ and __ to the normal substrate.
size, shape
91
A competitive inhibitor cannot undergo a ___ ____
chemical reaction
92
The inhibitor and substrate compete for a binding site to the active site of the enzyme in ___ ___
competitive inhibition
93
The inhibitor and substrate bind to different sites in __ ____
noncompetitive inhibition
94
Binding of the inhibitor ____ the activity of the enzyme and therefore decreases Kcat and Vmax in noncompetitive inhibition
decreases
95
Inhibitors might make it so the substrate is ___ bound to the enzyme.
loosely
96
Inhibitors decrease the ____ of the subsrate/reaction
Vmax
97
Inhibitos increase ____ of the substrate/reaction
Km
98
Irreversible inhibitors binds ____ to the enzyme, usually by ___ ___
irreversibly, covalent bonds
99
____ substrates generate a reactive group that forms a covalent bond during binding the active site.
suicide
100
Penicillin is an example of ___ substrate
suicide
101
Penicillin forms a covalent bond with an enzyme involved in the synthesis of what?
bacterial cell walls.