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CC2 > Enzymology > Flashcards

Enzymology Flashcards

0
Q

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

A

Transferase

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1
Q

Catalyze the removal or addition of electrons

A

Oxidoreductases

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2
Q

Catalyzes hydrolysis or splitting of a bond by addition of water

A

Hydrolases

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3
Q

Catalyze removal of groups from substrate w/o hydrolysis. Product contains double bonds

A

Lyases

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4
Q

Catalyze the intramolecular arrangement of the substrate

A

Isomerases

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5
Q

Catalyze the joining of two substrate molecules coupled with breaking of the pyrophosphate bond in ATP or similar compound

A

Ligases

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6
Q

Enzyme Nomenclature of Acid Phosphatase

A

E.C. 3.1.3.2

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7
Q

Enzyme Nomenclature of Alkaline Phosphatase

A

E.C. 3.1.3.1

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8
Q

Enzyme Nomenclature of Amylase

A

E.C. 3.2.1.1

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9
Q

Enzyme Nomenclature of Alanine Aminotransferase

A

E.C.2.6.1.2

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10
Q

Enzyme Nomenclature of Aspartate Aminotransferase

A

E.C.2.6.1.1

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11
Q

Enzyme Nomenclature of Aldolases

A

E.C.4.1.2.13

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12
Q

Enzyme Nomenclature of Angiotensin Converting Enzyme

A

E.C. 3.4.15.1

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13
Q

Enzyme Nomenclature of Creatine Kinase

A

E.C. 2.7.3.2

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14
Q

E.C. 3.1.1.7

A

Enzyme Nomenclature of True/Acetyl Cholinesterase

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15
Q

Enzyme Nomenclature of Pseudocholinesterase

A

E.C. 3.1.1.8

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16
Q

Enzyme Nomenclature of Gamma Glutamly Transferase

A

E.C. 2.3.2.2

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17
Q

Enzyme Nomenclature of G-6-PD

A

E.C. 1.1.1.49

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18
Q

Enzyme Nomenclature if Lipase

A

E.C. 3.1.1.3

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19
Q

Enzyme Nomenclature of Lactic Dehydrogenase

A

E.C. 1.1.1.27

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20
Q

Enzyme Nomenclature of 5’Nucleotidase

A

E.C. 3.1.3.5

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21
Q

Higher the enzyme the higher the reaction

A

Enzyme Conc.

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22
Q

Amount of enzyme exceeding the amount of substance

A

Substrate Conc.

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23
Q

Needed in the enzyme in order to have its activity

A

Cofactors

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24
Q

Organic compound
Increase the velocity of an enzymatic reaction
NAD

A

Coenzymes

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25
Q

Coenzymes if bound tightly

A

Prosthetic group

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26
Q

Addition if apoenzyme

A

Holoenzymes

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27
Q

Inorganic ions
Alters spatial configuration of the enzyme
Ca, Zn, Cl, Mg

A

Activators

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28
Q

Inorganic ion attached to a molecule

A

Metallonenzyme

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29
Q

Physically bind to the active site of an enzyme

A

Competitive inhibitor

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30
Q

Both the substrate and inhibitor compete for the same active site of the enzyme

A

Competitive inhibitor

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31
Q

The effect of the Competitive inhibitor can be counterattack by what to bind the enzyme?

A

Adding excess substrate

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32
Q

Binds an enzyme at a place other than the active site

A

Non-Competitive inhibitor

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33
Q

Inhibitor binds the enzyme independently from the substrate

A

Non-Competitive inhibitor

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34
Q

Substrate and inhibitor may bind an enzyme simultaneously

A

Non-Competitive inhibitor

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35
Q

The inhibitor binds to the enzyme-substrate complex

A

Uncompetitive inhibitor

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36
Q

Increasing substrate concentration, increases inhibition

A

Uncompetitive inhibitor

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37
Q

Enzymes having the same catalytic reactions but slightly different molecular structures

A

Isoenzymes

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38
Q

Temp where enzymes are active

A

25, 30, 37

39
Q

Temp where enzymes are denaturated

A

40-50

40
Q

Temp where enzymes are inactived

A

60-65

41
Q

For every 10’C inc in temp, there will be a two-fold increase in enzyme activity

A

Temperature Coefficient Q10

42
Q

Most physiologic reaction occur

A

pH range of 7-8

43
Q

Storage of preservation for longer period of time

A

20 degrees C

44
Q

Storage for temp ideal for substrate and coenzymes

A

2-8 degrees C

45
Q

Ideal storage for LDH (LD4 and LD5)

A

Room temp

46
Q

Substrate interacts with particular charge amino acid residues

A

Active site

47
Q

Cavity other than the active site; may bind regulator molecules

A

Allosteric site

48
Q

The shape of the key must fit into the lock (substrate is specific to one enzyme)

A

Emil Fisher’s/Lock and Key Theory

49
Q

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

A

Kochland’s/Induced Fit Theory

50
Q

Combines with only one substrate and catalyzes only one reaction

A

Absolute specificity

51
Q

Enzymes combine with all the substrate in a chemical group

A

Group specificity

52
Q

Enzymes reacting with specific chemical bonds

A

Bonds specificity

53
Q

Reaction rate depends only enzyme conc.

A

Zero-order reaction

54
Q

Reaction rate is directly proportional to substrate conc.

A

First-order reaction

55
Q

The reactants are combined; the reaction proceeds for a designated time
The reaction is stopped and measurement is made

A

Fixed-Time

56
Q

Multiple measurements of absorbance changed are made during the reaction; more adventurous than fixed-time

A

Continuous monitoring/Kinetic assay

57
Q

Predominant physiologic functions occurs in muscle cells.

A

Creatine Kinase

58
Q

Catalyzes the transfer of a phosphate group bet creatine phosphate and adenosine diphosphate

A

Creatine Kinase

59
Q

Sensitive indicator of AMI and muscular dystrophy-Duchenne type (50-100x)

A

Creatine Kinase

60
Q

Highest tissue source of CK

A

Heart, skeletal, smooth muscle, brain tissue

61
Q

Smallest tissue source found in the CK

A

Bladder, placenta, uterus, kidney, GiT, thyroid, lungs, prostate, spleen, liver, pancreas

62
Q

Size of CK

A

Dimeric molecules

63
Q

Composed of two different monomers

A

M and B

64
Q

Major isoenzyme in the serum of the healthy people

A

CK-MM( muscle type) / CK3

65
Q

Major activity of CK-MM are found where?

A

In the heart

66
Q

Undetectable/trace

Hybrid type

A

CK-MB

67
Q

Migrates in the middle of CKMM and CKMB

A

Macro CK

68
Q

Migrates cathodal to CK MM; Indicator of severe illness

A

Mitochondrial CK

69
Q

Methods used in Creatine Kinase: it requires a pH of 9.0-10.0; 340nm

A

Tanzer-Gilbarg Assay (forward/direct method)

70
Q

Methods used in Creatine Kinase: most commonly used method; faster reaction; pH 6.8; 340 nm

A

Oliver-Rosalki(reverse/indirect method)

71
Q

Specimen considerations: added to the reverse method to inhibit AK which may be present in the serum from hemolysis

A

Adenosine monophosphate (AMP)

72
Q

Specimen considerations: serves as buffer; component also of CK rgt

A

Imidazole

73
Q

Specimen considerations: partially restore lost activity of CK

A

Cleland’s reagent and gluthatione

74
Q

Specimen considerations: added to CK rgt to activate the enzyme

A

N-acetylcysteine

75
Q

Specimen considerations for Creatine Kinase:

A

Urate and cysteine are potent inhibitors
Liver cells and RBC do not contain CK
CK is light and pH sensitive; it is also lost with excessive storage

76
Q

Catalyzes the interconversion of lactic and pyruvic acids

A

Lactate Dehydrogenase

77
Q

Molecular form of Lactate Dehydrogenase

A

Tetrametric molecule

78
Q

Highest tissue source of Lactate Dehydrogenase

A

Heart, liver, skeletal muscle, kidney, erythrocytes

79
Q

Lesser amount of tissue source in Lactate Dehydrogenase

A

Lung, smooth muscle, brain

80
Q

Isoenzymes of Lactate Dehydrogenase: Heart and RBC (higher than LD2), kidney

A

LD1

81
Q

Isoenzymes of Lactate Dehydrogenase: same as LD1, major isoenzymes

A

LD2

82
Q

Isoenzymes of Lactate Dehydrogenase: in lungs, pancreas, spleen

A

LD3

83
Q

Isoenzymes of Lactate Dehydrogenase: in skeletal muscle, liver, intestine

A

LD4

84
Q

Isoenzymes of Lactate Dehydrogenase: significant in hepatic disorder; liver, skeletal(higher than Ld4), intestine

A

LD5

85
Q

Isoenzymes of Lactate Dehydrogenase: arteriosclerotic cardiovascular failure

A

LD6

86
Q

Onset for AMI:

A

12-24 hrs

87
Q

Peak for AMI

A

48-72 hrs

88
Q

Remain elevated for AMI

A

10 days

89
Q

Highest level are seen where in Lactate Dehyrdogenase

A

Pernicious anemia and hemolytic disorders

90
Q

It has a 10 fold increased in Lactate Dehydrogenase

A

Hepatic Carcinoma and toxic hepatitis

91
Q

Transudate from exudates

A

Pleural fluids

92
Q

Specimen consideration for Lactate Dehydrogenase: substrate; high affinity in H subunits

A

Alpha-hydroxybutyrate

93
Q

Methods for Lactate Dehydrogenase: most commonly used method
pH 8.8
Preferred for LD1

A

Wacker Method (forward/direct reaction)

94
Q

Methods for Lactate Dehydrogenase:
2x faster as the forward reaction
pH 7.2
Preferred for LD5

A

Wrobleuski La Due (reverse/indirect reaction)

CC2 (2 decks)

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