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MTAP 2 FINALS - CC2 > Introduction to Enzymes > Flashcards

Introduction to Enzymes Flashcards

1
Q

Biologic protein that catalyze biochemical reaction

A

Enzyme

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2
Q

Enzyme decreases or increases velocity in the reaction?

A

Increases

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3
Q

Enzyme only acts as ______; since it ______

A

participant; not consumed, nor change reaction

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4
Q

Majority of the enzymes are located ____

A

Intracellularly

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5
Q

Functions of Enzyme

A
  • Hydration of Carbon Dioxide (respiration)
  • Nerve Induction
  • Muscle contraction (locomotion)
  • Growth and Reproduction
  • Energy storage and use
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6
Q

it is readily available in the presence of enzyme

A

Heat

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7
Q

Components of Enzyme

A

Active Site
Allosteric Site

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8
Q

binding site of substrate

A

Active site

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9
Q

binds regulatory/effector molecules

A

Allosteric Site

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10
Q

binding of active and substrate is

A

HIGHLY SPECIFIC

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11
Q

Substance that ACTED UPON enzymes

A

Substrate

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12
Q

Lactose metabolism is accelerated due to

A

Lactase

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13
Q

Nonprotein portion of enzyme

A

Cofactor

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14
Q

3 types of Cofactor

A
  • Coenzyme
  • Activator
  • Isoenzyme
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15
Q

Acts as second substrate

A

Coenzyme

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16
Q

Coenzyme is ORGANIC OR INORGANIC cofactor?

A

Organic

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17
Q

Example of Coenzymes

A

NAD

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18
Q

Nonmetallic or Metallic cofactor

A

Activator

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19
Q

Non metallic Activator are

A

Bromide
Chloride

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20
Q

Metallic Activator are

A

MICZ

Magnesium
Iron
Calcium
Zinc

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21
Q

Cofactor that has same enzymatic activity but differs in PHYSICAL, BIOCHEMICAL, IMMUNOLOGIC characteristics

A

Isoenzyme

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22
Q

Example of Isoenzyme

A

CK Isoenzyme

CK-MM
CK-MB
CK-BB

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23
Q

Protein portion of enzyme

A

Apoenzyme

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24
Q

Susceptible for protein denaturation

A

Apoenzyme

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25
Q

Protein denaturation happens under what temp

A

56 deg cel.

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26
Q

Coenzyme + apoenzyme

A

Holoenzyme

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27
Q

coenzyme is tightly bound to the apoenzyme; coenzyme belongs to

A

Prosthetic group

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28
Q

Enzyme classification and name is based on

A

Enzyme Commission of IUB (International Union of Biochemistry)

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29
Q

Long name; Involves the:

Substrate
catalyzed reaction
Coenzyme

A

Systemic name

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30
Q

Usable name; commonly used

A

Recommended name/Trivial name

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31
Q

consist of four digits

A

Enzyme Commission Numerical Code

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32
Q

Enzyme Commission: First Digit

A

Enzyme Class

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33
Q

Enzyme Commission: Second Digit

A

Subclass

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34
Q

Enzyme Commission: Third Digit

A

Enzyme Sub Subclass

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35
Q

Enzyme Commission: Fourth Digit

A

Specific serial number of Enzyme

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36
Q

Enzyme Classes are the ff:

A

Oxidoreductase
Transferase
Hydrolase
Lyases
Isomerase
Ligases

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37
Q

Enzyme class that catalyzes the transfer of charged ions

A

Oxidoreductase

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38
Q

Redox reaction between 2 substrate

A

Oxidoreductase

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39
Q

Examples of Oxidoreductase enzyme:

A

Lactate Dehydrogenase (LDH)
Glucose Phosphate Dehydrogenase (G-6-PD)

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40
Q

Transfer of specific particular group other than hydrogen ion

A

Transferase

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41
Q

A- + B = A + B-

A

Oxidoreductase

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42
Q

A-X + B = A + B-X

A

Transferase

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43
Q

Transferase Enzymes are

A

Alanine Amino Transferase
Aspartate Amino Transferase
Gamma Glutamyl Transferase
Kinase (Creatine Kinase, Phosphokinase)

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44
Q

catalyze hydrolysis of various chemical bonds

A

Hydrolase

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45
Q

Hydrolase enzymes are

A

Amylase (glycosidic)
Lipase (Ester bond)
Phosphatase (monophosphoester bond)
- Acid Phosphatase
- Alkaline Phosphatase

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46
Q

catalyzes the removal of a particular chemical group from substrate w/o hydrolysis/water

A

Lyases

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47
Q

does lyases retain the double bond of an enzyme

A

Yes

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48
Q

A-B + H2O = A-OH + B-H

A

Hydrolysis

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49
Q

ATP –> cAMP + PPi

A

Lyases

50
Q

Lyases enzymes are

A

Fructose biphosphate aldolase

51
Q

catalyze interconversion of geometric, optical, and positional enzyme

A

Isomerase

52
Q

A –> B

A

Isomerase

53
Q

Isomerase enzymes are

A

Triphosphate isomerase

54
Q

catalyze the joining of 2 substrate

A

Ligases

55
Q

Example of Ligase enzyme

A

Glutathione synthetase

56
Q

Ab + C = AC + b

A

Ligase

57
Q

2 substrates joined together with

A

breaking of pyrophosphate bond in ATP

58
Q

lower the activation energy needed by enzymes results to

A

fast chemical reaction

59
Q

catalytic mechanism of enzyme

A

E + S = ES&raquo_space;> E + P

60
Q

Enzyme combined with only one substrate

A

Absolute specificity

61
Q

Enzymes combined with all substrate of a particular chemical group

A

Group Specificity

62
Q

Group Specificity example

A

Kinases (binds with phosphate group)

63
Q

enzymes bind with the chemical bond

A

Bond specificity

64
Q

Example of Bond specificity

A

Amylase (glycosidic)
Lipase (Ester)
Phosphatase (monophosphoester)

65
Q

Enzymes bind with one specific optical isomer

A

Stereoisometric specificity

66
Q

Factors that Influence Enzymatic Reactions

A

Substrate Concentration
Enzyme Concentration
Cofactor
Inhibitor
Storage
Hemolysis
Lactesence/Lipemic

67
Q

Increase substrate concentration results to

A

Increase enzymatic reaction

68
Q

Condition by which excessive increase of substrate no longer affects the enzymatic reaction

A

Saturation Kinetics

69
Q

Measurement of Enzyme activity that uses an increasing amount of substrate concentration

A

First-Order Kinetics

70
Q

Rate of Reaction is DIRECTLY PROPORTIONAL substrate concentration

A

First-Order Kinetics

71
Q

Increasing substrate concentration is used in

A

First-Order Kinetics

72
Q

FIXED number of substrates is converted to product

A

Zero Order Kinetics

73
Q

Increased enzyme concentration

A

Faster chemical Reaction

74
Q

TRUE / FALSE
All increased enzymes are clinically significant

A

false

75
Q

Example of an enzyme that is normally increased

A

G-6-PD

76
Q

Most physiologic reaction occurs @ what pH

A

7.0-8.0

76
Q

Most physiologic reaction occurs @ what pH

A

7.0-8.0

77
Q

Enzymes that can react with extremely low and high pH

A

Phosphatases

78
Q

Acid Phosphatase pH

A

3-5

79
Q

Alkaline Phosphatase pH

A

10

80
Q

Plays a vital role in reaction

A

Temperature

81
Q

enzyme is active at what temp

A

25, 30, 37 deg cel

82
Q

room temperature

A

25 deg cel

83
Q

optimum temperature for enzymatic activity

A

Body temperature (37 deg cel)

84
Q

Denaturation starts at what temperature

A

40-50

85
Q

Protein is denatured at what temp

A

56

86
Q

Temperature by which enzyme is inactivated

A

60-65

87
Q

Temperature coefficient/ Q10

A

for every 10 deg cel increase temperature = 2 fold increase in enzymatic activity

88
Q

Enhances spacial configuration of the enzyme

A

Activator

89
Q

3 kinds of Inhibitor

A

Competitive Inhibitor
Uncompetitive Inhibitor
Noncompetitive inhibitor

90
Q

prevents substrate conversion to a product

A

Inhibitor

91
Q

competes with substrate to the active site

A

Competitive inhibitor

92
Q

Kind of inhibitor that binds with the allosteric site

A

Noncompetitive inhibitor

93
Q

slow down or affect velocity of enzyme reaction; decreases substrate reaction

A

Competetive inhibitor

94
Q

slow down or affect velocity of enzyme reaction; decreases substrate reaction

A

Competitive inhibitor

95
Q

inhibitor that binds with Enzyme-Substrate Complex

A

Uncompetitive Inhibitor

96
Q

Preferred temperature for storage that maintains the enzymatic activity for long period of time

A

-20 deg cel.

97
Q

Substrate and Coenzyme temperature storage

A

2 - 8 deg. cel.

98
Q

Temperature storage for LDH

A

Room temperature (25 deg cel)

99
Q

Thawing of serum sample can be done ___

A

Once

100
Q

Hemolysis can cause false INCREASED / DECREASED enzyme activity

A

INCREASED

RBC contains enzymes; hemolysis causes to release these enzymes causing false elevation of enzyme concentration

101
Q

Lipemic, Lactescence, Milky specimen causes false INCREASED / DECREASE enzyme activity

A

Decrease

102
Q

Increase product concentration

A

Decrease substrate concentration (substrate –> product)

103
Q

Decrease in Coenzyme concentration (NADH)

A
  • Coenzyme (second substrate, indicator)
  • Commonly used in Oxidoreductase reaction
104
Q

Redox Reaction happens in the presence of

A

Coenzyme

105
Q

There is an INCREASED/DECREASED on altered coenzyme concentration during enzyme activity

A

Increased

106
Q

Enzyme catalytic activity uses what substrate kinetics

A

Zero-order kinetics

107
Q

Measurement of catalytic activity is done at what phase of reaction

A

LINEAR

108
Q

General Method for Measuring Enzymatic activity

A

Fixed Time (2-point) Assay
Continuous Monitoring Assay / Kinetic Assay

109
Q

mix reagents (substrate/coenzyme) and sample (enzymes)
incubate
measure

A

Fixed Time Assay

110
Q

multiple measurement at specific time interval

A

Continuous Monitoring Assay

111
Q

Commonly used interval

A

60 secs

112
Q

Kinetic Assay uses what type of substrate kinetics

A

Zero-order kinetics

113
Q

expression of the relationship between the velocity of the enzyme reaction and substrate concentration

A

Michaelis-Menten Equation

114
Q

IU (EC) unit

A

1 substrate umol/min (umol/min)

115
Q

SI unit

A

Katal (mol/sec)

116
Q

measurement of enzymatic mass is used for

A

isoenzymes

117
Q

Isoenzymes are measured through their

A

Electrophoretic migration

118
Q

Theory that is based on binding of substrate (key) to the active site (lock)

A

Emil Fishers (Lock and Key theory)

119
Q

Theory by which the configuration of the substrate would be manipulated so that it will fit to active site

A

Kochland’s Induced fit Theory

MTAP 2 FINALS - CC2 (11 decks)

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