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MT6324 > 1S [LEC]: Enzymes (intro + CK + LDH) > Flashcards

1S [LEC]: Enzymes (intro + CK + LDH) Flashcards

1
Q

Biological molecules that act as catalysts, facilitating and accelerating chemical reactions within living organisms

A

Enzymes

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2
Q

Specific proteins that catalyze biochemical reaction without altering the equilibrium point of the reaction or being consumed or changed in composition

A

Enzymes

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3
Q

Refers to the number, type, and sequence of amino acids in the polypeptide chain

A

Primary structure

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4
Q

Refers to the commonly formed arrangements stabilized by hydrogen bonds between nearby amino acids within the protein molecule

A

Secondary structure

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5
Q

Refers to the overall shape of the protein molecule

A

Tertiary structure

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6
Q

The structure that results from the interaction of more than one protein molecule, or protein subunits

A

Quaternary structure

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7
Q

The substance acted upon by the enzyme

A

Substrate

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8
Q

A water free cavity, where the substrate interacts with particular charged amino acid residues

A

Active site

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9
Q

A cavity other than the active site

A

Allosteric site

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10
Q

Binds the regulator molecules

A

Allosteric site

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11
Q

T/F: Regulator molecules change enzyme conformation

A

True

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12
Q

Enzymes with the same function but exist in different forms

A

Isoenzyme

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13
Q

Forms of enzymes that were post-transcriptionally modified

A

Isoforms

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14
Q

Non-protein molecule necessary for enzyme activity such as activators and coenzymes

A

Cofactors

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15
Q

A coenzyme bound tightly to the enzyme

A

Prosthetic group

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16
Q

The enzyme portion that is activated by the prosthetic group

A

Apoenzyme

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17
Q

Prosthetic group + apoenzyme

A

Holoenzyme

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18
Q

Inactive precursor of an enzyme

A

Zymogen/ Proenzyme

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19
Q

Classify the enzyme:

Catalyze an oxidation-reduction reaction between two substrated

A

Oxidoreductase

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20
Q

Classify the enzyme:

Catalyze the transfer of a group other than hydrogen from one substrate to another

A

Transferase

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21
Q

Classify the enzyme:

Catalyze hydrolysis of various chemical bonds

A

Hydrolase

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22
Q

Classify the enzyme:

Catalyze removal of groups from substrates without hydrolysis

A

Lyases

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23
Q

Classify the enzyme:

Catalyze the interconversion of geometric, optical, or positional isomers

A

Isomerase

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24
Q

Classify the enzyme:

Catalyze the joining of two substrate molecules

A

Ligase

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25
Q

Classify the enzyme:

Lactate dehydrogenase

A

Oxidoreductase

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26
Q

Classify the enzyme:

Glucose-6-phosphate dehydrogenase

A

Oxidoreductase

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27
Q

Classify the enzyme:

Glutamate dehydrogenase

A

Oxidoreductase

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28
Q

Classify the enzyme:

Creatine kinase

A

Transferase

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29
Q

Classify the enzyme:

Alkaline phosphatase

A

Hydrolase

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30
Q

Classify the enzyme:

Acid phosphattase

A

Hydrolase

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31
Q

Classify the enzyme:

a-Amylase

A

Hydrolase

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32
Q

Classify the enzyme:

Cholinesterase

A

Hydrolase

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33
Q

Classify the enzyme:

Chymotrypsin

A

Hydrolase

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34
Q

Classify the enzyme:

Elastase-1

A

Hydrolase

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35
Q

Classify the enzyme:

5’ nucleotidase

A

Hydrolase

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36
Q

Classify the enzyme:

Aldolase

A

Lyase

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37
Q

Classify the enzyme:

Triosephosphate isomerase

A

Isomerase

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38
Q

Classify the enzyme:

Glutathione synthetase

A

Ligase

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39
Q

If the reaction is substrate dependent, it is ___-order kinetics

A

first

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40
Q

If the reaction is enzyme dependent, it is ___-order kinetics

A

zero

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41
Q

If the reaction is substrate independent, it is ___-order kinetics

A

zero

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42
Q

If the reaction is enzyme independent, it is ___-order kinetics

A

first

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43
Q

Curve of velocity versus substrate concentration for enzymatic reaction

A

Michaelis-Menten curve

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44
Q

Curve that is a transformation of Michaelis-Menten curve

A

Lineweaver Burk

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45
Q

A compound that shares some structural feature found in the substrate will typically physically bind to the same form of the enzyme that the substrate binds

A

Competitive inhibitory

46
Q

Inhibitors associated with enzymes showing allosteric inhibition

A

Noncompetitive inhibitor

47
Q

Identify the type of inhibition based on Lineweaver Burk curve change:

Same Vmax
Increased Km

A

Competitive

48
Q

Identify the type of inhibition based on Lineweaver Burk curve change:

Vmax not achieved & decreased
Same Km

A

Noncompetitive

49
Q

Identify the type of inhibition based on Lineweaver Burk curve change:

Vmax not achieved
Decreased Km

A

Uncompetitive

50
Q

Size of CK

A

82 000 Daltons

51
Q

CK isoenzyme:

Most cathodal

52
Q

CK isoenzyme:

Least anodal

53
Q

CK isoenzyme:

Most anodal

54
Q

CK isoenzyme:

Least cathodal

55
Q

CK isoenzyme:

Most numerous

56
Q

CK isoenzyme:

Bound to the exterior surface of the inner mitochondrial membranes of muscle, brain, and liber

A

Mitochondrial CK

57
Q

CK isoenzyme:

Migrate cathodal to CK-MM

A

Mitochondrial CK

58
Q

Macro-CK migrate midway ___ and ___

A

CK-MM
CK-MB

59
Q

Method of isoenzyme measurement:

May visualize adenylase kinase

A

Electrophoresis

60
Q

Adenylase kinase is cathodal to ___

61
Q

Method of isoenzyme measurement:

Reference method

A

Electrophoresis

62
Q

Method of isoenzyme measurement:

More sensitive and precise if done properly

A

Ion exchange chromatography

63
Q

Method of isoenzyme measurement:

Measure enzyme concentration rather than activity

A

Immunoassays

64
Q

Method of isoenzyme measurement:

Double Ab immunoinhibition

A

Immunoassay

65
Q

Immunoassays measure Abs against which subunits?

66
Q

Forward CK method with an optimum pH of 9

A

Tanzer Gilvarg

67
Q

Reverse CK method that is 2-6x faster and has an optimum pH of 6.8

A

Oliver Rosalki

68
Q

Analyte that is markedly increased in RBC disorder

69
Q

Catalyzes the interconversion of lactic and pyruvic acids by transferring hydrogen using the coenzyme NAD+

70
Q

LD forward method

A

Wacker method

71
Q

LD reverse method that is 3x faster

A

Wroklewski La Due method

72
Q

A phenomenon where LD 1 has a higher amount than LD 2

A

Flipped pattern

73
Q

Flipped pattern is most commonly observed in what condition?

A

Heart (AMI) & RBC disease

74
Q

LD isoenzyme that is cathodal to LD5 and is a hallmark of arteriosclerotic CVD

A

Alcohol dehydrogenase (LD6)

75
Q

Macro-LD is found between ___ and ___

76
Q

Classify the enzyme:

Glycogen phosphorylase

A

Transferase

77
Q

Classify the enzyme:

Pyruvate kinase

A

Transferase

78
Q

Classify the enzyme:

Trypsin

79
Q

The intermediate state formed after the reactants exist

A

Transition state

80
Q

The excess energy needed to induce the transition state

A

Activation energy

81
Q

Specificity where the enzyme combines only one substrate and catalyzes only the one corresponding reaction

A

Absolute specificity

82
Q

Specificity where the enzyme combine with all substrates containing a particular functional group, such as a phosphate ester

A

Group specificity

83
Q

Specificity where the enzyme predominantly combine with only one optical isomer of a certain compound

A

Stereoisomeric specificity

84
Q

Hypothesized the role of substrate concentration in formation of the enzyme-substrate complex

A

Michaelis and Maud Menten

85
Q

A constant for a specific enzyme and substrate under defined reaction conditions an can provide an expression of the relationship between the velocity of an enzymatic reaction and substrate concentration

A

Michaelis-Menten constant

86
Q

The ___ is specifically the substrate concentration at which the enzyme yield half the possible maximum velocity

A

Michaelis-Menten constant (Km)

87
Q

A temperature increase of ___ will approximately double the enzymatic reaction

88
Q

The rate of denaturation increases as the temperature increase s and usually is significant at what range of temperature?

A

40-50C (but some may denature at body temp, 37C)

89
Q

T/F: Low temperatures render enzymes irreversibly inactive

A

False (reversibly inactive)

90
Q

Serve as secondary substrate for enzymatic reactions

91
Q

The method of enzyme determination where the reactants are combined, the reaction proceeds for a designated time, the reaction is stopped, and a measurement is made of the amount of reaction that has occurred

A

Fixed-time method

92
Q

The method of enzyme determination where multiple measurements, usually of absorbance change, are made during the reaction, at specific time intervals

A

Continuous monitoring/ Kinetic assays

93
Q

T/F: Kinetic methods are more advantageous than fixed-time methods

94
Q

Conventional unit for enzymatic activity

A

IU (International Unit)

95
Q

SI unit for enzymatic activity

96
Q

Conversion factor from IU to nano katal

A

1 IU = 17 nano katal

97
Q

Increased CK isoenzyme in Duchenne Muscular Dystrophy

98
Q

Predominant CK isoenzyme in the heart

99
Q

CK isoenzyme that is an indicator of severe illness, malignant tumor, and cardiac abnormalities

A

Mitochrondrial CK

100
Q

The Macro CK is comprised of which CK isoenzyme?

101
Q

The Macro CK is complexed with immunoglobulins, namely ___

A

IgG and IgA

102
Q

In CK forward method, the enzyme is measured through the ___ in absorbance

A

Decrease (since the reaction will be NADH&raquo_space;> NAD)

103
Q

In CK reverse method, the enzyme is measured through the ___ in absorbance

A

Increase (since the reaction will be NAD&raquo_space;> NADH)

104
Q

Effect of hemolysis in CK measurement

A

False increase

105
Q

Reference range for total CK

A

Male: 46-171 U/L
Female: 34-145 U/L

106
Q

Reference range for CK-MB

A

<5% total CK

107
Q

LD isoenzyme increased in RBC disorders

108
Q

LD isoenzyme increased in lung, spleen, and pancreatic problems

109
Q

LD isoenzyme increased in liver and skeletal muscle conditions

110
Q

In LD forward method, the enzyme is measured through the ___ in absorbance

A

Decrease (NADH&raquo_space;> NAD rxn.)

111
Q

In LD reverse method, the enzyme is measured through the ___ in absorbance

A

Increase (NAD&raquo_space;> NADH)

MT6324 (12 decks)

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