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CLINICAL CHEMISTRY 2 > Enzymology > Flashcards

Enzymology Flashcards

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1
Q

study of Enzymes

A

ENZYMOLOGY

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2
Q

catalyzed reactions are specific and essential to physiologic functions like

A
  • hydration of CO2
  • nerve conduction
  • nutrient degradation
  • energy use
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3
Q

Enzymes that facilitate **coagulation **are specific to

A

PLASMA

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4
Q

Biological catalyst (enzyme) mostly inhibit

A

Homogenous catalysis

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5
Q

Catalytic site; water free cavity

A

Active site

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6
Q

Allosteric site may bind

A

regulator molecules

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7
Q

How do these molecules inhibit or enhance substrate binding?

A

conformational change is introduced in the active site

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8
Q

Reaction rate is reduced when

A

there is conformational change due to allosteric inhibitor, unable to bind to enzyme and prevents it from lowering the activation energy

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9
Q

Cofactor and coenzyme bind temporarily and permanently through?

A

T: ionic and hydrogen bond
P: strong covalent bond

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10
Q

alters the spatial configuration of an enzyme for proper substrate binding

A

COFACTOR OR COENZYME

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11
Q

____ IS A TYPE OF COFACTOR

A

COENZYME

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12
Q

____ are covalently bound and can be removed by ________ the enzyme

A

some cofactors, denaturing

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13
Q

thermostable and form the active site of enzyme

A

Cofactor

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14
Q

true or false: coenzyme can catalyze a reaction by itself

A

false; coenzyme cannot catalyze by itself but has to bind to apoenzyme

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15
Q

Holoenzyme

A

coenzyme + apoenzyme;
comple and active form of enzyme

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16
Q

protein part of the enzyme; inactive form

A

apoenzyme

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17
Q

Catalytic components of DNA polymerase enzyme

A

apoenzyme

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18
Q

multi-subunit complex of DNA polymerase

A

holoenzyme

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19
Q

true or false: catalytic activity of enzymes depends on the **integrity of the enzymes’ 3D structure **

A

true

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20
Q

factors that act as denaturing agents

A
  • temperature
  • pH
  • chemicals
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21
Q

denaturation disrupts the ___ bonds

A

hydrogen bonds (that stabilize the 3D structure)

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22
Q

Enzymes like polymerases resume their activity at temperatures higher than

A

90 degrees Celsius

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23
Q

causes the unfolding of the enzyme

A

extremes of pH

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24
Q

In extremes of pH, unfolding can lead to loss of structural integrity then

A

loss of function

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25
Q

____ bonding: secondary structure
____ bonding: tertiary structure

A

hydrogen; covalent

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26
Q

EC-IUB

A

Enzyme Commission of the International Union of Biochemistry

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27
Q

EC-IUB adopted a classification in ___, and was revised in ____ & ____

A

1961, 1972, 1978

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28
Q

EC CLASS 4

A

Lyases

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29
Q

EC Class 2

A

Transferases

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30
Q

reduction

A

gain of electrons

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31
Q

EC class of Lactate Dehydrogenase

A

Oxidoreductase

Class 1

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32
Q

conversion of ethanol to acetaldehyde in liver

A

Alcohol dehydrogenase

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33
Q

EC of Creatine Kinase

A

Transferase

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34
Q

In CK, a phosphate group from ATP is transfered to the _ atom of creatine phosphate

A

nitrogen

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35
Q

End products of CK

A

ADP and creatine phosphate

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36
Q

Cleavage of bonds with the addition of H2O

A

Hydrolases

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37
Q

EC of esterases

ACP, ALP

A

Hydrolases

38
Q

group elimination to form double bonds (product)

A

LYASES

39
Q

In Aldolases, it cleaves the 6-carbon molecule (fructose-1,6-diphosphate) to produce 2 3-carbon compounds:

A

glyceraldehyde-3-phosphate and dihydroxyacetone phosphate

40
Q

True or false: Isomeric reactions are reversible

A

true

41
Q

responsible for the conversion of carbohydrate, glucose, to toher compounds

A

Glycolytic pathway

42
Q

EC class of mutases

A

Isomerase

43
Q

triacylglycerol acylhydrolase

A

lipase

44
Q

1,4-a-D-glucan glucanohydrolase

A

Amylase

45
Q

In activation energy, reactants possessing enough energy to overcome the enrgy barrier participate in

A

product formation

46
Q

Enzyme ___ free energy required to activate the reaction

A

reduces

47
Q

true of false: transition state of the ES complex has a lower activation energy than transition state of the substrate aloe

A

true

48
Q

Who are the two people who hypothesized the role ofsubstrate cocnentration in the formation of ES complex in 1913?

A

Michaelis and Mentern

49
Q

Substrate readily binds to free enzymes at ____ concentration

A

low

50
Q

FIRST ORDER: reaction rate is directly proportional to the ___________ concentration

A

substrate

51
Q

further increase in substrate concentration no longer accelerates reaction due to

A

saturated enzyme with the susbtrate (no enzyme left to react)

52
Q

Maximum velocity is achieved when

A

substrate concentration is high enough to saturate all available enzymes

53
Q

Km

A

specifically the substrate concentration (enzyme yields 1/2 of the possible Vmax)
amount of susbtrate needed for a particular enzyme reaction

54
Q

double reciprocal plot (yields a straight line)

A

Lineweaver-Burk plot

55
Q

higher the enzyme level

A

faster the reaction

56
Q

pH is carefully controlled at an optimal pH by

A

buffer solutions

57
Q

low temperatures render enzymes

A

reversibly inactive

58
Q

Common Activators (Inorganic Cofactors)

A

Metallic: Ca2+, Fe2+, Mg2+, Mn2+, Zn2+, K+
Non-metallic: Br-, Cl-

59
Q

Common Coenzymes (Organic factors)

A

Nucleotide phosphates, Vitamins

60
Q

true or false: Km is constant for each enzyme and can be altered

A

false: cannot be altered

61
Q

presence of compettive inhibitors will ___ the maximum velocity

A

lower

62
Q

bind to enzyme at a place other than the active site; metallic

A

noncompetitive inhibitors

63
Q

true or false: both inhibitor and susbtrate bind to enzyme simultaneously

A

true

64
Q

binds to the Enzyme-Substrate (ES) complex

A

Uncompetitive Inhibitors

65
Q

example of antienzyme

A

Trypsin inhibitors

66
Q

In rate of reaction, velocity constant o the reaction of the inhibitor with enzyme is

A

measure of the effectiveness of the inhibitor

67
Q

convenient method of enzyme quantitation

A

measurement of enzyme activity (not directly the enzyme)

68
Q

amount f susbtrate exceeds that of enzyme, rate of reaction will depend on the

A

ENZYME CONCENTRATION

69
Q

Period for Analysis sequence

A
  1. Enzyme is initially introduced
  2. Excess substrate steadily combine with available enzyme
  3. Reaction rate increases
  4. Enzyme is saturated
  5. Rate of product formation, release of enzyme, and recombination proceed linearly
70
Q

In fixed time, reaction is stopped, by inactivating enzyme with

A

weak acid

71
Q

also known as Kinetic Assays

A

Continuous-Monitoring

72
Q

Causes of deviation from linearity

A
  • enzyme is elevated: substrate is used up too early
  • coenzyme conc. is low
73
Q

variables that may alter results

A

pH, temperature, substrate

74
Q

Enzyme conc is usually expressed as

A

Units per Liter (IU/L)

75
Q

alternativeof measurement of enzyme activity

A

measurement of enzyme mass

76
Q

example of digestive enzyme where inactive precursors and inhibtors of catalysis are present in plasma

A

trypsin

77
Q

enzyme activties in serum are due to

A

mixtures of immunologically distinct isoenzymes

78
Q

enzymes can be used as

A

reagents

79
Q

used for uric acid determination

A

uricase (urate oxidase)

80
Q

In glucose determination, this enzyme reaction converts sugar other than glucose to their 6 phosphate esters

A

Hexokinase reaction

81
Q

In glucose determination, this is used to monitor the change in reaction (catalyzed by G6PD)

A

Indicator reaction

82
Q

equilibrium methods are also called

A

End point methods

83
Q

Enzymes with high affinities for their substrate

A
  • have low Km values
  • most suitable for equilibrium analysis
84
Q

general property of first order reaction

A

change in substrate concentration over a fixed time interval is directly proportional to its ratio of concentration

85
Q

most accurate for enzymatic determination of substrates; more demanding than equilibrium methods

A

two-point kinetic methods

86
Q

example of enzyme labels

A

ALP, Horeradish, peroxidase, G6PD, B-galactosidase

87
Q

ENZYME-LABELED ANTIBODIES OR ANTIGENS

A
  1. react with ligand
  2. enzyme substrate is added
  3. washing then 2nd enzyme-labeled antibody is added
  4. Ag-Ab-enzyme complex is formed
  5. 2nd washing then substrate is added
88
Q

conversion of susbtrate is proportional to

A

quantity of antigen

89
Q

example of adsorbents

where immobilized enzymes are chemically bonded to

A

Microcrystalline cellulose, Diethylaminothyl (DEAE) cellulose, Carboxymethyl cellulose, Agarose

90
Q

enzyme electrodes

enzymes incorporated into membranes

A

Ion-sensitive electrodes

91
Q

when immersed in a solution of appropriate substrate, action of enzymes

A

produces ions to which electrode is sensitive

CLINICAL CHEMISTRY 2 (2 decks)

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