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FINALS CC 2 > ENZYMOLOGY > Flashcards

ENZYMOLOGY Flashcards

1
Q

Biologic proteins that catalyze biochemical reactions

A

ENZYME

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2
Q

Enzymes are _________ proteins, produced by living cells

A

INTRACELLULAR

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3
Q

Enzymes affect the ________ or speed of a chemical rxn;
__________ its chemical reaction

A

VELOCITY, speeding up

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4
Q

In an enzymatic process, enzymes are not _______ , ________, ________ nor ________ in composition; it only affects the speed

A

consumed, modified, altered, changed

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5
Q

Enzyme action is specific with ________ substrates

A

ORGANIC

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6
Q

In the lab, enzymes are measured in terms of their ________ and not in their __________

A

ACTIVITY, absolute values (concentration)

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7
Q

Activity of enzyme to a substrate is _________ with its concentration

A

directly proportional

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8
Q

Greater Enzymatic Activity =

A

High Enzyme Concentration

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9
Q

in serum, enzyme concentration is normally low, if it is high, it is indicative of:

A

a. Cellular Injury/ Damage
b. Increase Membrane Permeability

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10
Q

Hastens respiration process

A

Hydration of CO2
(Carbonic Acid = buffers the pH)

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11
Q

Transmission of nerve impulses

A

Nerve Induction

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12
Q

Helps in movement & heat generation

A

Muscle Contraction

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13
Q

Digestive juices contain enzymes to facilitate the interconversion of complex molecules in the diet. Absorption of macromolecules in the small intestine

A

Nutrient Degradation/ Digestion

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14
Q

Assist in growth & metabolism of a person

A

Growth & Reproduction

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15
Q

Conversion of energy stores (in ADIPOSE)

A

Energy Storage & Use
(Creatine Phosphate = ATP for muscles)

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16
Q

Components of an Enzyme

A
  1. ACTIVE SITE
  2. ALLOSTERIC SITE
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17
Q

A waterless cavity of an enzyme where substrates bind and undergo chemical reaction

A

ACTIVE SITE

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18
Q

Binding site for SUBSTRATE

A

ACTIVE SITE

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19
Q

Specific substrate can only bind to the active site of the enzyme

A

Enzyme-Substrate Specificity

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20
Q

A waterless cavity other than the active site that binds regulatory or effector molecules.

A

ALLOSTERIC SITE

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21
Q

Activators of Enzymes

A

1- Substrate (lab)
2- Cofactor (in the body)

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22
Q

Substances acted upon by enzymes

A

SUBSTRATES

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23
Q

Nonprotein substances added in the enzyme substrate complex to manifest an enzyme activity (to allow enzyme reaction)

A

COFACTORS

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24
Q

To ENHANCE enzymatic activity

A

COFACTORS

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25
Q

Organic cofactor that hastens enzymatic reactions

A

COENZYME (2nd Substrate)

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26
Q

COENZYME examples

A

NAD & NADP

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27
Q

Facilitates enzyme-substrate binding by altering the spatial configuration of the enzyme active site

A

ACTIVATOR

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28
Q

ACTIVATOR EXAMPLES

A
  1. Metallic Type: Mg, Ca, Fe, Zn, Mn
  2. Non-metallic Type: Cl, Br
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29
Q

Enzymes with similar enzymatic activity/ reaction but differ in their physical, biochemical, and immunologic characteristics

A

ISOENZYME

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30
Q

One way of differentiating/ fractionating isoenzymes is with the use of _____________

A

electrophoresis.

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31
Q

In the lab, ___________ is more preferred than _________ measurement due to its _______ to target tissue

A

isoenzyme measurement, total enzyme activity, HIGH SPECIFICITY

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32
Q

ISOENZYME EXAMPLES

A
  1. Creatine Kinase (CK1, CK2, CK3)
  2. Lactate Dehydrogenase (LDH1 to LDH5)
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33
Q

Protein portion of the enzyme

A

APOENZYME (Inactive Enzyme)

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34
Q

If the apoenzyme is subjected to _________, enzyme activity is lost

A

denaturation

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35
Q

Denaturation promotes at ________, would promote destruction of ____________

A

56degC, tertiary proteins

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36
Q

When an apoenzyme is tightly bound/attached with a coenzyme, it is termed as a _____________

A

prosthetic group

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37
Q

An active substance formed by the combination of a coenzyme and an apoenzyme (the product)

A

HOLOENZYME (Active Enzyme)

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38
Q

The naming of enzymes and its classifications was recommended by the

A

Enzyme Commission or the International Union of Biochemistry

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39
Q

The LONGER name
Defines the substrate acted on, or the reaction catalyzed, and possibly the coenzyme involved

A

Systematic Name

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40
Q

The usable/ trivial name of the enzyme
Frequently used name

A

Recommended Name

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41
Q

Always starts with E.C. followed by the 4 digits
1st – class of enzyme
2nd – subclass of enzyme
3rd – sub-subclass of enzyme
4th – serial number specific to enzyme sub-subclass

A

EC (Enzyme Commission) Numerical Code

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42
Q

Always starts with E.C. followed by the 4 digits
1st –
2nd –
3rd –
4th –

A

EC (Enzyme Commission) Numerical Code
1st – class of enzyme
2nd – subclass of enzyme
3rd – sub-subclass of enzyme
4th – serial number specific to enzyme sub-subclass

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43
Q

6 1st DIGIT CLASSIFICATION OF ENZYME

A
  1. Oxidoreductases
  2. Transferases
  3. Hydrolases
  4. Lyases
  5. Isomerases
  6. Ligases
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44
Q

Catalyzes the reduction oxidation reaction between 2 substrates; loss or gain of electrons; these enzymes utilize NAD/ NADP coenzymes (redox reaction)

A

Oxidoreductases

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45
Q

A– + B → A + B–

A

Oxidoreductases

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46
Q

In Oxidoreductases, ___ is the commonly transferred atom

A

H+

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47
Q

The conversion of the coenzymes NAD and NADP is catalyzed by _______

A

oxidoreductase

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48
Q

Catalyzes the transfer of a chemical group such as phosphate, methyl, among others (other than hydrogen) between two substrates

A

Transferases

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49
Q

A-X + B → A + B-X

A

Transferases

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50
Q

Transferases examples

A

1.AST/ SGOT (aspartate serum transferase)
2.ALT/ SGPT (alanine aminotransferase)
3.Gamma-glutamyl transferase (GGT)

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51
Q

Dehydrogenase examples

A
  1. Lactate Dehydrogenase (LDH)
  2. Glucose-6 Phosphate Dehydrogenase (G-6-PD)
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52
Q

Kinases example/s

A

Creatine Kinase (CK)
- Transfers PHOSPHATE groups

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53
Q

A–B + H2O → A–OH + B–H

A

Hydrolases

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54
Q

Hydrolysis of ether and ester & various bonds

A

Hydrolases

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55
Q

In the presence of water, hydrolases can _______ on different chemical bonds; when water is introduced, the bond is _______ (separates substrate A from substrate B).

A

cleave, cleaved

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56
Q

There must always be _____ for hydrolases to function

A

water

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57
Q

targets glycosidic bond connecting complex sugars

A

.Amylase

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58
Q

fats

A

Lipase

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59
Q

organic phosphomonoester bond

A

Phosphatase

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60
Q

6 Hydrolases examples

A
  1. Amylase
  2. Lipase
  3. Phosphatase
  4. Cholinesterase
  5. 5-nucleotidase
  6. ACE (acetyl cholinesterase)
61
Q

ATP → cAMP + PPi

A

Lyases

62
Q

Removal of groups from substrate without hydrolysis/ presence of water. The product remains having double bonds

A

Lyases

63
Q

cAMP
PPi

A

cAMP - Cyclic Adenosine Monophosphate
PPi - Intermediate Diphosphate

64
Q

Lyases example/s

A

1.Glutamate Decarboxylase Aldolases
2. Fructose biphosphate aldolase (ALS)

65
Q

enzyme
that acts on carbohydrates

A

Fructose biphosphate aldolase (ALS)

66
Q

A → B

A

Isomerases

67
Q

The interconversion of geometric, optical, and positional isomers.

A

Isomerases

68
Q

It would catalyze the interconversion of substrate A to become substrate B

A

Isomerases

69
Q

Ab + C → A–C + b

A

Ligases

70
Q

Joining of two substrate molecules coupled with the breaking of pyrophosphate bond in ATP

A

Ligases

71
Q

Enzymes catalyze physiologic reactions by __________ that the reactants must reach

A

lowering the activation energy level

72
Q

energy required for chemical reactions to proceed; important for product formation

A

ACTIVATION ENERGY

73
Q

The _________ the activation energy required, the ________ the product formation

A

higher/greater

74
Q

The _________ the activation energy required, the ________ the product formation

A

higher/greater, longer

75
Q

The _______ the activation energy required, the ______ the product formation (in presence of enzymes)

A

lower, faster

76
Q

The enzyme reaction is always _______ with the substrate.

A

reversible

77
Q

Enzymes combined with only one substrate and catalyzes only one corresponding reaction

A

Absolute Specificity

78
Q

Enzymes combined with all substrates containing a particular chemical group

A

Group Specificity

79
Q

Enzymes attached to substrates with specific chemical bonds

A

Bond Specificity

80
Q

Enzymes combine with only one specific optical isomer

A

Stereoisometric Specificity

81
Q

Higher Substrate =

A

More Enzymatic Reaction

82
Q

Enzyme is greater than substrate

A

FIRST ORDER KINETICS (E > S)

83
Q

Reaction rate is proportional to substrate conc.

A

FIRST ORDER KINETICS (E > S)

84
Q

Rate depends on concentration of substrate

A

FIRST ORDER KINETICS (E > S)

85
Q

when substrate conc. reaches the maximal value, addition of more substrate could no longer increase the rate of reaction as enzymes are already exhausted

A

Saturation Kinetics

86
Q

Only a fixed/ constant number of substrate (in excess) is converted to product per second

A

ZERO ORDER KINETICS (S > E) → used in the lab

87
Q

In enzymatic reaction, we prefer that substrate is GREATER than enzyme → as long as substrate is in excess, there will be enzyme activity

A

ZERO ORDER KINETICS (S > E) → used in the lab

88
Q

If the enzyme activity or concentration is __________, it cannot be measured by the machine, thus, it must be _________ → retest

A

too HIGH, serially diluted

89
Q

lowers the conc. of enzyme

A

SERIAL DILUTION

90
Q

Reporting of diluted serum

A

result of diluted serum is not reported, rather multiply the dilution factor to diluted serum

91
Q

Higher Enzyme Concentration = More Substrate Binding = Faster Reaction

A

Enzyme Concentration

92
Q

Velocity of reaction is proportional to enzyme as long as there is zero order kinetics

A

Enzyme Concentration

93
Q

Normal except G-6-PD

A

LOW enzyme conc

94
Q

HIGH enzyme conc.

A

Clinically Significant

95
Q

Most physiologic reactions occur between a pH range of ________

A

7.0-8.0 (close to plasma pH of 7.35-7.45)

96
Q

If the pH is too high or too low (extreme pH), enzymes are usually __________ , because enzymes are __________.

A

denatured/ inactivated, ergo proteins which undergo denaturation when pH is too acidic or too basic

97
Q

can survive in extremely low and extremely high pH levels respectively

A

Acid phosphatase (pH 3-5) and Alkaline phosphatase (pH 9-10)

98
Q

Tests for enzymes are done at __________ to mimic the ________ happening in the body.

A

body temp. 37°C, in vivo reaction

99
Q

Assay temperature should be constant within ____ in which the enzyme is active at ____ , ____, and ____.

A

±0.1, 25°C, 30°C, 37°C

100
Q

2 Temperatures for Enzymatic Testing:

A
  1. Room Temperature (25°C) – longer incubation
  2. Warm/ Body Temperature (37°C) – shorter; optimum temperature
101
Q

Increased Temp.. =

A

Increased Rate of Chemical Rxn

102
Q

Q10
(Temp. Coefficient) = Increased incubation temperature by _____ will have a characteristic of ______ in enzyme activity

A

10°C, twofold increase

103
Q

Extreme Temp. =

A

Decreased Enzyme Activity

104
Q

When the temp. exceeds 37°C, the activity starts to _____; which is _____

A

decrease, irreversible

105
Q

significant decrease in enzyme activity (denaturation of tertiary structure)

A

40-50°C

106
Q

significant decrease in enzyme activity (denaturation of tertiary structure)

A

40-50°C

107
Q

significant denaturation/ inactivation

A

56°C

108
Q

proteins are completely inactivated

A

60-65°C

109
Q

Most enzymes are THERMOLABILE (inactive at high temperatures) except

A

The placental type of Alkaline phosphatase (Regan Alkaphose) which is thermoresistant/
thermostable

110
Q

At low/ cold temperatures, enzymes are _______ ; but are preserved and become activated when temperature is ________

A

reversibly inactive, increased to room/ body temp

111
Q

Non protein that enhances the reaction

A

Cofactors

112
Q

It must be present in excess

A

Cofactors

113
Q

when added to the enzyme structure could alter spatial configuration of the enzyme for proper substrate binding

A

Inorganic/ Activators

114
Q

serves as 2nd substrate for enzymatic reaction (NAD). When coenzymes are increased, the velocity of the enzyme activity could also increase

A

Organic/ Coenzyme (prosthetic groups):

115
Q

Agents that could interfere with the enzyme-substrate reaction

A

Inhibitors

116
Q

competes with the substrate on the active site of the enzyme (alters/ slows down velocity by preventing enzyme binding)

A

Competitive Inhibitors

117
Q

it binds on the site (allosteric site) other than the active site

A

Non-competitive Inhibitors

118
Q

binds to enzyme-substrate (ES) complex

A

Uncompetitive Inhibitors

119
Q

Increased Inhibitors =

A

Decreased Enzymatic Activity

120
Q

Storage for substrates & coenzymes (reagents)

A

2-8degC [refrigerated]

121
Q

Storage for storage of LDH (LD4 and LD5 are cold labile)

A

Room temp. (20-24 degC)

122
Q

Storage for longer preservation of enzyme found in samples (serum)

A

-20degC or colder [freezer]

123
Q

Why is thawing of frozen serum is only done for one time?

A

Multiple freeze thawing = can destroy enzyme
(denaturation) = falsely decreased

124
Q

Factors that Influence Enzymatic Reactions

A
  1. Substrate Concentration
  2. Enzyme Concentration
  3. pH
  4. Temperature
  5. Cofactors
  6. Inhibitors
  7. Storage
  8. Interferences
124
Q

It is the energy required to raise all molecules to the transition state in a chemical reaction so that products may be formed

A

Activation Energy

125
Q

Increase in product concentration

A

= ↑ Rate of Substrate Conversion = ↑ Enzyme Concentration

126
Q

Decrease in substrate concentration

A

= ↑ Products formed = ↓ Substrate Concentration

127
Q

Decrease in coenzyme concentration (NADH)

A

Oxidized NAD (decreased) → reduced NADH (increased absorbance)

128
Q

Always performed in zero-order kinetics (w/ fixed substrate)

A

Catalytic Activity

129
Q

Performed during the linear phase of reaction

A

Measurement of Catalytic Activity

130
Q

Simple outright procedure (only 1 measurement)

A

Fixed Time/Two-Point Assay

131
Q

The reagents are combined, the reaction proceeds, the reaction is stopped and the amount of reaction is measured

A

Fixed Time/Two-Point Assay

132
Q

Multiple enzyme activity is included in the procedure

A

Continuous Monitoring/ Kinetic Assays

133
Q

Multiple measurements at specific time intervals or continuous measurement as absorbance changes.

A

Continuous Monitoring/ Kinetic Assays

134
Q

Deviation from zero kinetics can be observed

A

Continuous Monitoring/ Kinetic Assays

135
Q

30-60s interval; then absorbance is noted

A

Continuous Monitoring/ Kinetic Assays

136
Q

2 Types of Enzymes Involved in Continuous Monitoring/ Kinetic Assays

A
  1. Primary Enzyme
  2. Secondary/ Coupling/ Indicator Enzyme
137
Q

target enzyme in serum

A

Primary Enzyme

138
Q

rely on primary enzyme activity for the reaction to proceed

A

Secondary/ Coupling/ Indicator Enzyme

139
Q

An expression of the relationship between the velocity of the enzymatic reaction and the substrate concentration.

A

Michaelis-Menten Equation

140
Q

The amount of enzyme that will catalyze the reaction of 1 μmol of substrate per minute (umol/ min)

A

IU; International Unit (EC) - [μmol/min]

141
Q

Used by the Enzyme Commission

A

IU; International Unit (EC) - [μmol/min]

142
Q

The amount of enzyme that will catalyze the reaction of 1 mol of substrate per second (mol/s)

A

Kat; Katal (SI) – [mol/s]

143
Q

Used by the Système international

A

Kat; Katal (SI) – [mol/s]

144
Q

The actual enzyme concentration

A

Enzyme Mass

145
Q

Enzyme mass can be quantified using _______; enzymes are proteins with charged differences depending on the ___ and the isoelectric point

A

electrophoresis, pH, isoelectric point

146
Q

2 enzyme theories

A
  1. Emil Fisher’s/ Lock & Key Theory
  2. Kochland’s Induced Fit Theory
147
Q

Based on the substrate binding to the active site of the enzyme

A

Kochland’s Induced Fit Theory

148
Q

The shape of the key (the substrate) must fit into the lock (the active site of the enzyme)

A

Emil Fisher’s/ Lock & Key Theory

FINALS CC 2 (7 decks)

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