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BIOCHEM > Enzymology > Flashcards

Enzymology Flashcards

1
Q

Enzymes measures from?

A

12 kilo Daltons to 1,000 kilo Daltons

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2
Q

They are responsible for the different reactions in living matter necessary during digestion, metabolism, respiration, energy release and energy transfer in all metabolic reactions.

A

Enzymes

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3
Q

A specific region in enzyme which interacts with its substrate.

A

Active site

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4
Q

The substance acted upon by an enzyme.

A

Substrate

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5
Q

It is derived from a transformed substrate

A

Product

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6
Q

a cavity (other than the active site) that may bind regulator molecules
and thereby be significant to the basic enzyme structure

A

Allosteric site

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7
Q

Are invariably complex proteins

A

Enzymes

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8
Q

Enzymes are generally soluble in?

A

Water, glycerol and dilute alcohol

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9
Q

Enzymes are ____ in nature and are not _____

A

Colloidal; dialyzable

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10
Q

Enzymes function with a?

A

Cofactor

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11
Q

True or false: Enzymes are consumed and produced during the course of a reaction

A

Very very False

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12
Q

True or false: Enzymes do not cause reactions to take place but they expedite reactions.

A

Very very true

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13
Q

Are complex proteins

A

Enzymes

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14
Q

Means that they do not affect the acid-base balance of the body

A

Amphoteric

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15
Q

They are highly specific for the reaction they catalyze and only produce the expected produces from given reactants or substrates.

A

Enzymes

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16
Q

True or false: Enzymes are easily denatured

A

Very very true

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17
Q

Enzymes are synthesized in ___ state.

A

Inactive

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18
Q

It is a high energy state

A

Transition state

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19
Q

Is the Energy required to achieve or go to the transition state

A

Activation energy

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20
Q

What decreases the energy required to get a reaction started?

A

Enzyme

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21
Q

True or false: Enzymes lower energy barrier by forcing reacting molecules through different transition state.

A

true na true for you

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22
Q

True or false: the higher the free energy change for the transition barrier the slower the reaction rate is.

A

Very true ka diyan

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23
Q

Are non-protein molecule, necessary for enzyme activity

A

Cofactor

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24
Q

Are inorganic cofactors

A

Activators

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25
Q

Are organic cofactors

A

Coenzyme

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26
Q

Is a coenzyme bound tightly to the enzyme

A

Prosthetic group

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27
Q

It is secreted from the organ of production in an
inactive form (digestive enzymes)

A

Proenzyme/Zymogen

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28
Q

Is the enzyme portion without cofactor

A

Apoenzyme

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29
Q

Combination of Apoenzyme + coenzyme

A

Holoenzyme

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30
Q

Holoenzyme is the combination of?

A

Apoenzyme + coenzyme

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31
Q

Are inorganic activators existing as part of the enzyme
molecule usually consist of earth metals

A

Metalloenzyme

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32
Q

Examples of earth metals found in metalloenzymes

A

Iron, calcium, magnesium

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33
Q

Enzyme structure that is the specific amino acid sequence

A

Primary structure

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34
Q

Are the most important configurations in enzyme structure because it is responsible for characteristics like coiling and folding which results to formation of active site

A

Secondary and Tertiary structure

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35
Q

It is the twisting of the polypeptide chains

A

Secondary structure

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36
Q

The folding of the chains (interactions among the side
chains/groups of chains)

A

Tertiary structure

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37
Q

The spatial relationship between
the subunits

A

Quaternary structure

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38
Q

Where final adjustments happens to molecules before it becomes active

A

Quaternary structure

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39
Q

Are different molecular forms of enzymes that may be isolated from the same or different tissues but are of similar activity.

A

Isoemzymes

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40
Q

LD2 - H3M is found in?
(clue: H, R, R)

A

heart, RBC & renal tissues

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41
Q

LD3 - H2M2 is found in?
(Clue: L, L, S, P)

A

Lungs, lymphocytes, spleen, pancreas

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42
Q

LD1 - H4 is found in?
(Clue: H, R, R)

A

heart, RBC & renal tissues

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43
Q

LD4 - HM3 is found in?
(Clue: L, S)

A

liver, skeletal muscles

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44
Q

LD5 - M4 is found in?
(Clue: L, S)

A

liver, skeletal muscles

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45
Q

CK-MB found in?
(Clue: H, S)

A

Heart and skeletal muscle

46
Q

CK-MM found in?
(Clue: H, S)

A

Heart and Skeletal muscle

47
Q

CK-BB found in?
(Clue: B, B, L, P)

A

Brain, Bladder, Lung, Prostate…

48
Q

same enzymatic activity which are specie specific for different biological species

A

Heteroenzyme

49
Q

Are Genetically transmitted enzymes important in defining the biochemical characteristics of an individual

A

Alloenzyme

50
Q

Present only in some selected individuals of the same species

A

Alloenzyme

51
Q

Has practical value in forensic medicine and genetics

A

Alloenzyme

52
Q

Origin of enzymes that is secreted in the liver and released in the plasma. Exert function in plasma

A

Plasma Specific Enzymes

53
Q

Origin of enzymes that has no specific function in plasma

A

Non-Plasma Enzymes

54
Q

The two classes of Non-Plasma Enzymes

A

Enzymes of secretion
Enzymes associated with cellular metabolism

55
Q

Based on distribution:
Can be seen in Cell sap or one location only

A

Unilocular

56
Q

Based on distribution:
Can be seen in mitochondria and cell sap

A

Bilocular

57
Q

Nomenclature based on organ/ observation/experiences

A

Empirical names

58
Q

First digit:______

A

class of the enzyme (1 - 6)

59
Q

Nomenclature: With 4 digits separated by decimal points

A

EC numerical code

60
Q

Nomenclature suitable for everyday use

A

Trivial or Practical Name

61
Q

Fourth digit:______

A

serial number that is specific to each enzyme in a sub-subclass

62
Q

Second and Third digits: _______

A

subclass and sub- subclass

63
Q

Simplification of naming by using acronyms and Uppercase abbreviation of enzymes

A

Trivial or Practical Name

64
Q

Nomenclature Associated unique numerical code designation

A

Systematic name

65
Q

Nomenclature: define the substrate acted upon and describe the nature of the reaction catalyzed

A

Systematic name

66
Q

Catalyze oxidation and reduction reactionsbetween 2 substrates

A

OXIDOREDUCTASES

67
Q

Catalyze the joining of 2 substrate molecules usually with energy supplied by the cleavage of an ATP

A

LIGASES

68
Q

Catalyze the interconversion of one isomer to another by molecular rearrangements

A

ISOMERASES

69
Q

Catalyze hydrolysis of variety of bonds

A

HYDROLASES

70
Q

Catalyze removal of groups from substrates without hydrolysis

A

LYASES

71
Q

Catalyze the transfer of an intact group of atoms (amine or phosphate group) from one substrate to another

A

TRANSFERASES

72
Q

Most of these enzymes are important in assessing heart attacks and liver problems

A

OXIDOREDUCTASES

73
Q

Most are assayed in skeletal muscle disorders

A

LYASES

74
Q

Most of these enzymes are important in assessing liver damage and myocardial infarction

A

TRANSFERASES

75
Q

the particular enzyme catalyzing a specific substrate

A

Specificity

76
Q

the active site of the enzyme is complementary in conformation to the substrate, so that the enzyme and the substrate recognize one another

A

Lock and Key Theory

77
Q

number of enzymes or substrates that can be reacted

A

Space availability

78
Q

commonness /sameness of enzyme and substrate

A

Molecular compatibility

79
Q

The enzyme changes shape upon binding the substrate, so that the conformation of substrate and enzyme protein are only complementary upon the binding reaction.

A

Induced fit theory

80
Q

activation energy

A

Energy

81
Q

Enzyme concentration is fixed and the substrate concentration is varied

A

FIRST ORDER KINETICS

82
Q

At low substrate, the rate is directly
proportional to substrate concentration

A

SUBSTRATE CONCENTRATION

83
Q

Reaction rate is dependent on substrate concentration

A

FIRST ORDER KINETICS

84
Q

With excess substrate, the rate is a direct measure to the amount of enzyme present

A

SUBSTRATE CONCENTRATION

85
Q

Im Substrate concentration At high substrate, the rate is _____

A

constant

86
Q

condition where the enzymatic reaction is allowed to take place

A

TIME

87
Q

Reaction rate is dependent on enzyme concentration

A

ZERO ORDER KINETICS

88
Q

Direct Relationship

A

ENZYME CONCENTRATION

89
Q

When maximum velocity is reached, the rate of increase in velocity is “0”

A

ZERO ORDER KINETICS

90
Q

Increase of 10 degree C doubles the rate of enzyme activity

A

TEMPERATURE

91
Q

Form ionic bridges to help bind the substrate to the active site

A

Activators

92
Q

bind to the ES complex

A

Uncompetitive Inhibitors

93
Q

bind to the active site of the enzyme

A

Competitive Inhibitors

94
Q

bind at place other than the active site = change in shape

A

Non-Competitive Inhibitors

95
Q

Can be separated via physical dialysis, gel filtration

A

Reversible Inhibition

96
Q

Inhibitors combine covalently with the enzyme

A

Irreversible Inhibition

97
Q

may itself be an inhibitor of the forward reaction

A

Product of Reaction

98
Q

causes competition between substrate molecules for a single binding site

A

Excess substrate

99
Q

These are essentially coenzymes that firmly bind with enzymes

A

Prosthetic Group

100
Q

These must be present at the proper concentration for many enzyme reactions to take place

A

COENZYME Concentration

101
Q

enzyme combines with only 1 substrate and catalyzes only the one corresponding reaction

A

ABSOLUTE SPECIFICITY

102
Q

It refers to the disruption of the structure of enzyme molecule (3-dimensional structure) that leads to the loss of enzyme activity

A

ENZYME DENATURATION

103
Q

Denaturation may be reversed if the reaction process ______ too far and if ________

A

has not gone; the denaturing agent is removed

104
Q

when an enzyme acts only on the specific isomer of a certain compound

A

STEREOISOMERIC

105
Q

when some enzymes act on all substrates containing a particular chemical group

A

GROUP SPECIFICITY

106
Q

Multiple measurements (absorbance change), At specific time interval , Continuous-recording, spectrophotometer

A

CONTINUOUS-MONITORING

107
Q

Enzymes cause antibody production when injected to animals to which they are foreign

A

IMMUNOASSAYS

108
Q

The reactants are combined, the reaction proceeds for a designated time, Measure amount of reaction

A

FIXED-TIME

109
Q

least preferred specimen, inhibitorytoenzymeactivity

A

USE OF PLASMA

110
Q

presence of intracellular enzyme causes an increase in enzyme concentration

A

HEMOLYSIS

111
Q

In timing, prolonged time of reaction increases ________

A

product formation

112
Q

Prolonged time of incubation leads to _____ and _______

A

denaturation; inhibition of enzyme reaction

BIOCHEM (10 decks)

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