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Clinical Chemistry 2 > Ch. 13 Enzymes - Clinical Enzymology Lecture > Flashcards

Ch. 13 Enzymes - Clinical Enzymology Lecture Flashcards

1
Q

Specific biologic proteins that catalyze biochemical reactions w/o altering the equilibrium point of the rxn or being consumed or changed in composition

A

Enzymes

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2
Q

Enzymes are frequently found in _____ following cellular injury

A

Serum

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3
Q

A cavity of an enzyme where substrates bind and undergo a chemical reaction.

A

Active Site

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4
Q

A water-free cavity, where the substance on which the enzymes acts interacts with particular charged amino acid residues.

A

Active Site

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5
Q

The substance on which the enzyme acts.

A

Substrate

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6
Q

A cavity other than the active site that binds regulatory (effector) molecules.

A

Allosteric Site

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7
Q

Substances acted upon by enzymes

A

Substrate

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8
Q

Enzymes that have similar enzymatic activity but differ in physical, biochemical and immunologic characteristics

A

Isoenzymes

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9
Q

Enzymes with the same catalytic function throughout the body but exists in different forms within the same individual

A

Isoenzymes

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10
Q

Results when an enzyme is subject to posttranslational modifications.

A

Isoform

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11
Q

Non protein substances added in the enzyme substrate complex to manifest the enzyme activity

A

Cofactor

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12
Q

Non protein molecule that may be necessary for enzyme activity

A

Cofactor

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13
Q

Inorganic cofactors

A

Activators

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14
Q

Organic cofactor

A

Coenzyme

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15
Q

A coenzyme that is bound tightly to the enzyme

A

Prosthetic group

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16
Q 
Which is/are not an activator:
Vitamins
Chloride ion
Nicotinamide adenine dinucleotide
Magnesium ion
Nicotinamide adenine dinucleotide phosphate
Copper ion
A

NAD
Vitamins
Nicotinamide adenine dinucleotide phosphate

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17
Q 
Which is/are not a coenzyme:
Vitamins
Chloride ion
Nicotinamide adenine dinucleotide
Magnesium ion
Nicotinamide adenine dinucleotide phosphate
Copper ion
A

Chloride ion
Magnesium ion
Copper ion

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18
Q

The protein portion of the enzyme that is also subject to denaturation, in enzyme losses activity

A

Apoenzyme

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19
Q

An active substance formed by combination of a co-enzyme and an apoenzyme.

A

Holoenzyme

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20
Q

Enzymes originally secreted from the organ of production in a structurally inactive form

A

Proenzyme or Zymogen

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21
Q

Catalyze redox reaction between two substrates (A- + B → A + B-)

A

Oxidoreductases 1

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22
Q

Catalyze the transfer of a group other than hydrogen (Phosphate, methyl, etc.) between two substrates (A-X + B → A + B-X)

A

Transferases 2

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23
Q

Catalyze hydrolysis of various bonds

A–B + H2O → A–OH + B–H

A

Hydrolases 3

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24
Q

Catalyze the removal of groups from substrates without hydrolysis; the product contains double bonds
ATP → cAMP + PPi

A

Lyases 4

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25
Q

Catalyze the interconversion of geometric, optical or positional isomers
A → B

A

Isomerases 5

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26
Q

Catalyze the joining of two substrate molecules, coupled with breaking of pyrophosphate bond in ATP or a similar compound
Ab + C → A–C + b

A

Ligases 6

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27
Q 
Which among the given is/are Hydrolases:
Phosphatase (ALP, ACP)
Glutathione Synthetase (GSH-S)
Triphosphate isomerase (TPI)
Lipase (LPS)
Fructose biphosphate aldolase (ALS)
Amylase (AMS)
Transferase (ALT, AST, GGT)
Dehydrogenase (Lactate Dehydrogenase)
Kinase (CK)
A

Amylase (AMS), Lipase (LPS), Phosphatase (ALP, ACP)

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28
Q 
Which among the given is/are Oxidoreductases:
Phosphatase (ALP, ACP)
Glutathione Synthetase (GSH-S)
Triphosphate isomerase (TPI)
Lipase (LPS)
Fructose biphosphate aldolase (ALS)
Amylase (AMS)
Transferase (ALT, AST, GGT)
Dehydrogenase (Lactate Dehydrogenase)
Kinase (CK)
A

Dehydrogenase (Lactate Dehydrogenase)

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29
Q 
Which among the given is/are Transferases:	
Phosphatase (ALP, ACP)
Glutathione Synthetase (GSH-S)
Triphosphate isomerase (TPI)
Lipase (LPS)
Fructose biphosphate aldolase (ALS)
Amylase (AMS)
ALT
AST
GGT
Dehydrogenase (Lactate Dehydrogenase)
Kinase (CK)
A

ALT, AST, GGT, CK

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30
Q 
Which among the given is/are Lyases:
Phosphatase (ALP, ACP)
Glutathione Synthetase (GSH-S)
Triphosphate isomerase (TPI)
Lipase (LPS)
Fructose biphosphate aldolase (ALS)
Amylase (AMS)
ALT
AST
GGT
Dehydrogenase (Lactate Dehydrogenase)
Kinase (CK)
A

Fructose biphosphate aldolase (ALS)

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31
Q 
Which among the given is/are Isomerases:
Phosphatase (ALP, ACP)
Glutathione Synthetase (GSH-S)
Triphosphate isomerase (TPI)
Lipase (LPS)
Fructose biphosphate aldolase (ALS)
Amylase (AMS)
ALT
AST
GGT
Dehydrogenase (Lactate Dehydrogenase)
Kinase (CK)
A

Triphosphate isomerase (TPI)

32
Q 
Which among the given is/are Ligases:
Phosphatase (ALP, ACP)
Glutathione Synthetase (GSH-S)
Triphosphate isomerase (TPI)
Lipase (LPS)
Fructose biphosphate aldolase (ALS)
Amylase (AMS)
ALT
AST
GGT
Dehydrogenase (Lactate Dehydrogenase)
Kinase (CK)
A

Glutathione Synthetase (GSH-S)

33
Q 
Which of the following is/are not Transferases:
Phosphatase (ALP, ACP)
Glutathione Synthetase (GSH-S)
Triphosphate isomerase (TPI)
Lipase (LPS)
Fructose biphosphate aldolase (ALS)
Amylase (AMS)
A

All of the above

34
Q 
Which of the following is/are not Hydrolases:
Glutathione Synthetase (GSH-S)
Triphosphate isomerase (TPI)
Fructose biphosphate aldolase (ALS)
ALT
GGT
Dehydrogenase (Lactate Dehydrogenase)
Kinase (CK)
A

All of the above

35
Q 
Which of the following is/are not Lyases:
Glutathione Synthetase (GSH-S)
Triphosphate isomerase (TPI)
Fructose biphosphate aldolase
ALS
A 
Glutathione Synthetase (GSH-S)
Triphosphate isomerase (TPI)
36
Q

The energy required to raise all molecules in 1 mol of a compound at a certain temperature to the transition state t the peak of the energy barrier.

A

Activation Energy

37
Q

Catayze physiologic reactions by lowering the activation energy level that the reactants (substrates) must reach for the reaction to occur

A

Enzymes

38
Q

The physical binding of a substrate to the active site of an enzyme

A

Enzyme-substrate complex

39
Q

Refers to an enzyme combining with only one substrate and catalyzes only the one corresponding reaction.
E.g. CK, LD

A

Absolute Specificity

40
Q

Refers to enzymes that combine with all substrates containing a particular chemical group, such as phosphate ester.
E.g. ACP, ALP

A

Group Specific

41
Q

Refers to enzymes that are specific to chemical bonds

A

Bond Specificity

42
Q

Refers to enzymes that predominantly combine with only one optical isomer of a certain compound.
E.g. LDH, G6PD

A

Sterioisometric specificity

43
Q 
The following are Group specific enzymes except:
CK
LDH
ALP
G6PD
A

CK
LDH
G6PD

44
Q 
Which of the following enzymes exhibit Absolute Specificity?
CK
LDH
ACP
LDH
A

CK

45
Q

Enumerate the factors that influence enzymatic reactions

A 
Substrate Concentration
Enzyme Concentration
pH
Temperature
Cofactors
Inhibitors
46
Q

Hypothesized that the substrate readily binds to free enzyme at a low substrate concentration.

A

Michaelis and Menten

47
Q

It follows that the reaction rate is directly proportional to the substrate concentration.

A

First-order kinetics

48
Q

A reaction wherein only a fixed number of substrate (in excess) is converted to product per second; the reaction rate depends only on enzyme concentration

A

Zero-order kinetics

49
Q

Changes in _____ may denature an enzyme or influence its ionic state, resulting in structural changes or a change in the charge of an amino acid residue in the active site.

A

pH

50
Q

Used to carefully control and maintain the optimal pH in a reaction.

A

Buffer solutions

51
Q

Common pH range; most physiologic reactions occur in this range.

A

7.0 - 8.0

52
Q

Increasing _____ usually increases the rate of a chemical reaction by increasing the movement of molecules, the rate at which intermolecular collisions occur, and the energy available for the reaction

A

Temperture

53
Q

Incubation of enzymes should be accurate within what temperature

A

(+/-) 0.1 C

54
Q

Non protein entities that must bind to particular enzymes before a reaction occurs.

A

Cofactors

55
Q 
The following are some metallic activators except:
Ca2+
Fe2+
Zn2+
K+
Br-
Mg2+
Mn2+
Cl-
A

Br-

Cl-

56
Q 
The following are some nonmetallic activators except:
Cl-
Ca2+
Fe2+
Br-
Mg2+
Mn2+
Zn2+
K+
A 
Ca2+
Fe2+
Mg2+
Mn2+
Zn2+
K+
57
Q

Serve as second substrates for enzymatic reactions

A

Coenzymes

58
Q

Increasing _____ concentration will increase the velocity of an enzymatic reaction in a manner synonymous with increasing substrate concentration.

A

Coenzyme

59
Q

A particular substance that interferes with enzymatic reactions

A

Inhibitor

60
Q

A type of inhibitor that physically binds to the active site of an enzyme and compete with the substrate for the active site.

A

Competitive inhibitor

61
Q

In competitive inhibition, the inhibition is reversible when the inhibitor is (greater/less than) the substrate. Explain.

A

Less than. The inhibition is reversible because the substrate is more likely than the inhibitor to bind to the active site.

62
Q

Inhibition wherein the inhibitor binds to the ES complex

A

Uncompetitive inhibition

63
Q

An inhibitor that binds an enzyme at a place other than the active site and may be reversible in that some naturally present metabolic substances combine reversibly with certain enzymes

A

Noncompetitive inhibitor

64
Q

Explain why noncompetitive inhibtion may be irreversible and why increasing substrate concentration will not reverse the inhibition.

A

Noncompetitve inhibition may be irreversible when the inhibitor destroys part of the enzymes involved in catalytic activity. Increasing substrate concentration will not reverse the inhibition because the inhibitor binds directly to the enzyme.

65
Q

Km stands for

A

Michaelis-Menten constant

66
Q

It is an expression of the relationship between the velocity of an enzymatic reaction and substrate concentration

A

Km

67
Q

Indicates the amount of substrate needed for a particular enzymatic reaction

A

Km

68
Q

In Competitive inhibition, Km (increased/decreased/was unchanged)

A

Increased

69
Q

In Noncompetitive inhibition, Km (increased/decreased/was unchanged)

A

Unchanged

70
Q

In Uncompetitive inhibition, Km (increased/decreased/was unchanged)

A

Decreased

71
Q

This type of inhibition can be counteracted by adding excess substrate to bind the enzyme.

A

Competitive inhibition. Reaction will proceed at a slower rate but to the same maximum velocity (Vmax) as an uninhibited reaction.

72
Q

In this type of inhibition, maximum velocity cannot be achieved.

A

Noncompetitive inhibition

73
Q

When substrate concentration is increased, inhibition is also increased in this type of inhibition. Also, maximum velocity equal to that of an uninhibited reaction cannot be achieved.

A

Uncompetitive inhibition.

74
Q

A type of inhibition where:
Km increased
Vmax same with uninhibited reaction

A

Competitive inhibition

75
Q

A type of inhibition where:
Km is unchanged
Vmax cannot be achieved

A

Noncompetitive inhibition

76
Q

A type of inhibition where:
Km is decreased
Vmax equal to that of an uninhibited reaction cannot be achieved

A

Uncompetitive inhibition

77
Q

What are the functions of Enzymes?

A 
Hydration of Carbon Dioxide (respiration)
Nerve Induction
Muscle Contraction
Nutrient Degradation (Digestion)
Growth and Reproduction
Energy Storage and Use

Clinical Chemistry 2 (5 decks)

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