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CC 2 LEC > ENZYMES > Flashcards

ENZYMES Flashcards

1
Q

ENZYMES

Definition and function

A

• Biologic catalysts
Hasten chemical reactions

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2
Q

T or F

Enzymes are not consumed during the reactions

A

True

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3
Q

T or F

Enzymes do not undergo a chemical change after the reactions

A

True

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4
Q

MAIN ACTION OF ENZYMES

A

• Catalyze/interact with substrate to mediate/facilitate chemical reactions.

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5
Q

Where are enzymes found?

A

Enzymes are found in the cells and tissues.
They are present only in the circulation at a limited level (low
level)

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6
Q

T or F

TESTING FOR ENZYMES is NOT DIAGNOSTIC for a certain disease.

A

True

Purpose: For the doctors to be alerted as to which body part, cell/tissue has a problem.

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7
Q

• Study of enzymes

A

ENZYMOLOGY

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8
Q

Study of enzymes
We have to look for:

A

• Activity of Enzymes
• Chemical reactions they catalyze
• Clinical uses

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9
Q

T or F

Enzymes do not undergo change.

A

True

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10
Q

Enzvme + substrate =

A

enzyme-substrate complex

which produces a product and the enzyme

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11
Q

During________ reaction, the enzyme will not be consumed and the form will not be changed

The intact enzyme bound to the substrate is still the same enzyme that was expelled after______ were formed.

It retains the same appearance before binding.

A

enzyme+substrate

products

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12
Q

T or F

There will still be products formed even when there is no enzyme

A

True

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13
Q

Y axis =
X axis =

A

Energy usage

Time required to produce a product

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14
Q

Enzymes may recognize and catalyze:

A

a single substrate

a group of substrates that have specific functional groups

A group of substrates that have a particular type of bond

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15
Q

TYPES OF ENZYME SPECIFICITY

A

Absolute
Group
Linkage

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16
Q

Catalyze one type of reaction for a single substrate

A

Absolute

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17
Q

Catalyze one type of reaction for all similar substrates

A

Group

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18
Q

Looks for a specific functional group (amino group, carboxyl group, ester, etc. made into substrate)

A

Group

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19
Q

Urease catalyzes only the hydrolysis of urea

A

Absolute

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20
Q

Hexokinase adds a phosphate group to hexoses

A

Group

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21
Q

Catalyze one type reaction for a specific type of bond

A

Linkage

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22
Q

Chymotrypsin catalyzes the hydrolysis of peptide bonds (all types of protein) [not all, but they share the peptide bond]

A

Linkage

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23
Q

Lock and Key Model

A

Emil Fisher in 1894

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24
Q

= where the substrate binds to an
enzyme

A

ACTIVE SITE

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25
Q

The________is where the activators and the inhibitors bind (not the substrate)

A

Allosteric site

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26
Q

•______ promote the binding of the enzyme to the substrate.
•______ prevent the binding of the enzyme to the substrate

A

Activators

Inhibitors

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27
Q

________prevent, so they make sure the substrate doesn’t bind to the active site.

The shape of the enzyme is changed so they could not bind.

A

Inhibitors

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28
Q

An________ makes the enzyme better at binding the substrate

A

allosteric activator

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29
Q

• The substrate and the active site are not the same, so they could not bind

• What’s needed for them to bind is for the______ to bind to the allosteric site

A

activator

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30
Q

is an inhibitor of xanthine oxidase.

A

Allopurinol

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31
Q

In inflammation, as _______ act as inhibitors.

A

anti-inflammatory drugs

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32
Q

NOMENCLATURE OF ENZYMES

A
  1. Substrate + -ase (not true to all)
  2. Reaction it catalyzes
  3. Enzyme Commission Nomenclature (E.C.)
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33
Q

Substrate + -ase (not true to all)

Examples

A

a. Lipid = lipase
b. Ester = esterase
c. Protein = protease

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34
Q

Reaction it catalyzes

Nomenclature Examples

A

a. Oxidation = oxidase
b. Reduction = reductase
c. Hydrolysis = hydrolase
d. Dehydrogenase = remove hydrogen atoms
e. Decarboxylase = remove carboxyl groups

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35
Q

Enzyme Commission Nomenclature (E.C.)

E.C. 1.1.1.21

Meaning of each digit

A

• 1st digit = class
• 2nd digit = subclass
• 3rd and 4th = serial number

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36
Q

T or F

All enzymes end with an -ase

A

False

Examples: pepsin, trypsin
• Angiotensin-converting enzyme

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37
Q

CLASSIFICATION OF ENZYMES

HILLOT

A

Hydrolases
Isomerases
Ligases
Lyases
Oxidoreductases
Transferases

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38
Q

T or F

ENZYMATIC REACTIONS
Can occur in both ways. There is a forward and reverse reaction, thats why the arrow points both ways.

A

True

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39
Q

All enzymes in this class can perform oxidation and reduction forward and reverse.

A

OXIDOREDUCTASES

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40
Q

Oxidation
Reduction

A

O - removal of H ion
R - acceptance of H ion

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41
Q

(removal of hydrogen from lactate)

This enzyme has a lactate substrate.

A

Lactate Dehydrogenase

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42
Q

• Transfer of functional groups other than hydrogen from one substrate to another

A

TRANSFERASES

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43
Q

(transfers amino group)

Substrate is aspartate

A

Aspartate Aminotransferase

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44
Q

• Hydrolysis of various bonds
• Addition of water to a bond resulting in bond breakage

Loss of substrate

A

HYDROLASES

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45
Q

• Catalyze the removal of groups from Substrates without hydrolysis or oxidation; the product contains double bonds or a ring

A

LYASES

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46
Q

Which type of enzyme makes a product that contains double bonds or a ring

A

Lyases

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47
Q

It breaks down a big molecule, WITH NO WATER INVOLVED.

A

Lyases

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48
Q

• Rearrange the functional groups within a molecule and catalyze the conversion of one isomer into another

A

ISOMERASES

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49
Q

• Catalyze the joining of two large molecules by forming a new chemical bond

A

LIGASES

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50
Q

LIGASES
• Accompanied by an

A

ATP-ADP interconversion

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51
Q

Acted upon by the enzyme
• Specific

A

Substrate

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52
Q

• Different form, but with the same action

53
Q

Non-protein molecule

Helper of enzyme / promote enzymatic attachment to the substrate
Some enzymes require cofactor, some do not

54
Q

Polypeptide portion
Inactive enzyme

Enzyme that requires a cofactor BUT has not met a cofactor

55
Q

Apoenzyme + Coenzyme

Enzyme that has met a cofactor

A

Holoenzyme

56
Q

Holoenzyme

A

Apoenzyme + Coenzyme

57
Q

Some enzymes require cofactors
Without cofactors:
With cofactors:

A

inactive apoenzyme

active holoenzyme

58
Q

COFACTORS
TWO TYPES

A

Activators
Coenzymes

59
Q

-› inorganic substances
Does NOT contain carbon

-› organic substances
• Contains carbon

A

Activators

Coenzymes

60
Q

cofactors based on their binding tightness.

A

Prosthetic groups
Coenzymes

61
Q

: Tightly bound

: loosely bound

A

Prosthetic groups

Coenyzmes

62
Q

Metal ions (activators) or organic molecules

Change to the configuration of the enzyme/link substrate to the enzyme/ coenzyme

Copper is a member

Activators are members

A

Prosthetic groups

63
Q

Organic molecules

“Second substrate” for enzyme reactions

64
Q

Some enzymes require a_____ to facilitate the reaction.
The_______ binds the coenzyme and then the substrate.

The coenzyme is a part of the catalytic domain and will either donate or accept functional groups, allowing the reaction to occur.

Once the product is formed, both the_____ and _____ are released.

A

coenzyme

apoenzyme

product and the coenzyme

65
Q

• Role: enzyme precursor / immature enzyme

A

Proenzyme/ Zymogen

66
Q

There are certain enzymes, most especially digestive enzymes, they express as a ______

A

Proenzyme/ Zymogen

67
Q

Not all enzymes have_____ - there are enzymes where once they are created, they are good to go.

A

proenzymes

68
Q

is the proenzyme, whereas trypsin is the active enzyme.

A

Trypsinogen

69
Q

ENZYME KINETICS

A

MICHAELIS-MENTEN THEORY

70
Q

MICHAELIS-MENTEN THEORY

A

Leonor Michaelis
1875-1949

Maud Menten
1879-1960

71
Q

MICHAELIS-MENTEN THEORY how many steps?

72
Q

2 steps in MICHAELIS-MENTEN THEORY

A

First: forms non-covalent ES complex

Second: end in with a Product and Enzyme

73
Q

• A double-reciprocal plot of the Michaelis-Menten constant which yields a straight line

A

LINEWEAVER-BURK PLOT

74
Q

Presents the same thing as with the Michaelis-Menten Plot (MM Plot), the difference between the 2 is that the lineweaver-burk plot (LB Plot) presents a______ compared to the_____ of Michaelis-Menten’s plot.

A

STRAIGHT LINE

HYPERBOLA

75
Q

• Another difference is the unit of X and Y axis of the lineweaver-burk plot is the_____ of Michaelis-Menten which are the Velocity and Substrate concentration

A

RECIPROCAL

76
Q

FACTORS THAT INFLUENCE ENZYMATIC REACTIONS
These factors either INCREASE or DECREASE the rate of reaction

A

Substrate concentration
Enzyme concentration
pH
Temperature
Cofactors
Activators
Inhibitors

77
Q

Are those which proceed at a rate exactly proportional to the concentration of ONE
REACTANT

In enzymes, when the reaction rate is directly proportional to the substrate concentration

A

First-Order Reactions

78
Q

Are those in which the rate is proportional to the product of the concentration of TWO REACTANTS or THE SQUARE OF THE CONCENTRATION OF ONE REACTANT

A

• Second-Order Reactions

79
Q

Similarities between 1ST and 2ND order is that the relationship between SUBSTRATE conc. and VELOCITY is…

A

DIRECTLY PROPORTIONAL. (S = V | 1S ^V)

80
Q

The MORE substrates you add, the FASTER is the______.

Which is true because if there are substrates, there are products nga form.

81
Q

When the substrate concentration is high enough to saturate all available enzymes

A

• Zero-Order Reactions

82
Q

A higher concentration of substrate will no longer result in increased reaction rate
• 1S = No change in V

A

• Zero-Order Reactions

83
Q

• The HIGHER the enzyme level, the FASTER the reaction will proceed.

A

ENZYME CONCENTRATION

84
Q

Once the reaction has reached its Vmax it cannot anymore produce any reaction but when enzyme is added the reaction will proceed once again eliminating Vmax-

A

ENZYME CONCENTRATION

85
Q

Optimal pH

86
Q

Changes in pH may____ the enzyme.

87
Q

TEMPERATURE
•_____ is the OPTIMAL temp for enzymes

88
Q

• Denaturation @
• Inactivation @

A

40-50°C (HOT)

4-10°C (COLD)

89
Q

Assay temperatures:

A

25, 30, or 37°C

90
Q

(Activators or Coenzymes)
• Non-protein entities that must bind to particular enzymes before a reaction occurs

91
Q

Cofactors

: Metallic or Nonmetallic
: Nucleotide phosphate and
Vitamins

A

Activators

Coenzymes

92
Q

• Proper substrate binding
• Link substrate to the enzyme or coenzyme
• Undergo oxidation or reduction

A

ACTIVATORS

93
Q

• Interfere with enzyme reactions

A

INHIBITORS

94
Q

• 3 types of Inhibition

A

Competitive

Noncompetitive

Uncompetitive

95
Q

: The inhibitor will bind to the ACTIVE SITE

A

Competitive Inhibition

96
Q

: The inhibitor will bind to the ALLOSTERIC SITE.

A

Noncompetitive Inhibition

97
Q

: The inhibitor will bind to the ENZYME-SUBSTRATE COMPLEX.

A

Uncompetitive Inhibition

98
Q

The STRUCTURE of the substrate is
COMPLEMENTARY to the size and appearance of the active site.

So when they interact they will just merge as one perfectly.

A

LOCK AND KEY THEORY

99
Q

According to one journal, this theory is too perfect, too good to be true. They believe that our body is not THIS PERFECT.

A

Lock and Key theory

100
Q

There is a CLASH between the structure of the substrate and the active site of the enzyme.

If a substrate comes close to its target enzyme, the active site will CHANGE ITS STRUCTURE to accommodate the substrate

The fact the substrate is CLOSE TO THE ACTIVE SITE, is enough to change the structure of the active site to accommodate the substrate.

A

Induced fit theory

101
Q

In the laboratory we do not measure the enzymes directly, but we measure their________; By measuring that, we will now come up with their______.

A

ACTIVITY

concentration

102
Q

MEASUREMENT OF ENZYME ACTIVITY

A

• Increase in PRODUCT concentration.

• Decrease in SUBSTRATE concentration

• Decrease or increase in COENZYME concentration

• An increase in the concentration of the altered coenzyme

103
Q

ENZYMATIC ASSAYS

A
  1. Coupled- Enzyme Assay
  2. Fixed - Time Method (End point)
  3. Continuous - Monitoring Method (Kinetic Assay)
104
Q

• Coupling the activity of the enzyme being tested to another, more easily detectable, enzyme

A

Coupled- Enzyme Assay

105
Q

Measured here is the activity of
ANOTHER ENZYME.

This is because enzymes are difficult to catch or measure directly, so we need to examine another thing, in order to
represent our TARGET ENZYME.

A

Coupled- Enzyme Assay

106
Q

•______ meaning you are using
MANY ENZYMES.
• Indirect measurement

A

Coupled-Enzyme

107
Q

• Reactants are combined
• Reaction proceeds for a designated time
• Reaction is stopped
• Measurement is made of the amount of reaction that has occurred.

A

Fixed - Time Method (End point)

108
Q

We are given with only 1 RESULT; meaning the measurement will only come at the

A

Fixed - Time Method (End point)

109
Q

Multiple measurements of absorbance change

In order for us to know if there are
fluctuations in the absorbance while the machine is assessing your sample.

A

Continuous - Monitoring Method (Kinetic Assay)

110
Q

CALCULATION OF ENZYME ACTIVITY

A

IU
IU/L
KATAL UNIT (mole/s)

111
Q

• Amount of enzyme that will catalyze the reaction of 1 MICROMOLE OF SUBSTRATE PER MINUTE under specified conditions

A

INTERNATIONAL UNIT (IU)

112
Q

Enzyme concentration

Used MOSTLY in the hospitals in the laboratory.

A

INTERNATIONAL UNIT PER LITER (IU/L)

113
Q

• Amount of enzvme that will catalvze the reaction of 1 MOLE OF SUBSTRATE PER SECOND under specified conditions.

A

KATAL UNIT (mole/s): Sl unit

114
Q

Is it normal for enzymes to be at an increased numbers in the circulation?

115
Q

ALT (alanine transaminase) is found in the cells of the____.

116
Q

Enzyme + substrate = enzyme-substrate complex which produces a…

A

product and the enzyme

117
Q

The Allosteric site is where the ____ and _____bind

A

activators and the inhibitors

118
Q
  1. Lipase with water will break down TAG (triacylglycerol.)
  2. It will become…
A

Diacylglyercol with 1 Free Fatty Acid

119
Q

○ Enzyme is strained
○ Product should always contain either a double-bond or a ring.

120
Q

Phosphoglycerate mutase is what type of enzyme?

121
Q

Inactive enzyme

122
Q

It binds and changes the active site

123
Q

T or F

Copper is a coenzyme

A

False. It is inorganic therefore it is an activator

124
Q

There are certain enzymes, most especially_____ enzymes, they express as a proenzyme

125
Q

ALP → Has a pH:

126
Q

ALP → Has a pH:

127
Q

T or F

Each enzyme operates within a specific pH range

128
Q

How to ensure desired pH in reagents?

  • The Reagent box contains_____. It ensures desired pH is followed; NO MORE MANUAL measurement.
129
Q

End product of lyases contain

A

Double bonds

CC 2 LEC (13 decks)

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