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Clinical Chemistry 2 > Enzymes > Flashcards

Enzymes Flashcards

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1
Q

are specific biologic proteins that catalyze biochemical reactions without altering the equilibrium point of the reaction or being consumed or changed in composition.

A

Enzymes

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2
Q

Found in all body tissues, frequently appear in the serum following cellular injury or, sometimes, in smaller amounts, from degraded cells.

A

Enzymes

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3
Q

Are often useful in the diagnosis of particular diseases or physiologic abnormalities.

A

Plasma/Serum Enzyme Levels

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4
Q

specific amino acid sequence

A

Primary structure

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5
Q

polypeptide chains twisting

A

secondary structure

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6
Q

structure with folding or bend

A

tertiary structure

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7
Q

If an enzyme contains more than one polypeptide unit

A

Quaternary structure

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8
Q

refers to the spatial relationships between the subunits.

A

Quaternary structure

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9
Q

interacts with particular charged amino acid residues.

A

Active site

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10
Q

may bond regulator molecules and, thereby, be significant to the basic enzyme structure.

A

Allosteric site

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11
Q

Different forms may be differentiated from each other based on certain physical properties:

A
  1. Electrophoretic mobility
  2. Solubility
  3. Resistance to inactivation.
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12
Q

results when an enzyme is subject to posttranslational modifications

A

Isoform

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13
Q

a nonprotein molecule; not an enzyme

A

Cofactor

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14
Q

Cofactor + Enzyme =?

A

Reaction

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15
Q

Nonprotein entities that must bind to particular enzymes ______ a reaction occurs

A

Before

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16
Q

is an organic compound (second substrates)

A

coenzymes

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17
Q

increasing its concentration will increases the velocity of an enzymatic reaction

A

Coenzymes

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18
Q

Example of coenzymes

A

NAD and NADP

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19
Q

are inorganic ions which alters the spatial configuration of the enzyme for proper substrate binding

A

Activators

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20
Q

Example of Activators

A

Calcium, Zinc, Chloride, Magnesium, and Potassium

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21
Q

are inorganic ion attached to a molecule

A

Metalloenzymes

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22
Q

Example of Metalloenzymes

A

Catalase and Cytochrome oxidase

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23
Q

Pancreas specific enzyme

A

Lipasa

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24
Q

A non-specific saliva and pancreas

A

Amylase

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25
Q

This enzyme is elevated in alcoholic individual

A

Gamma Glutamyl Transferase (GGT)

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26
Q

This enzyme is associated with cellular injury

A

cytochrome P450

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27
Q

is an organic cofactor. Such as nicotinamide adenine dinucleotide (NAD)

A

Coenzyme

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28
Q

When bound tightly to the enzyme, the coenzyme is called a ______________

A

Prosthetic group

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29
Q

Another term for Prosthetic group

A

Apoenzyme

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30
Q

When a bound tightly to the enzyme, the coenzyme is a called a prosthetic group which forms a complete and active system

A

Holoenzyme

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31
Q

are originally secreted from the organ of production is a structurally inactive form.

A

Zymogen

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32
Q

Another term for Zymogen

A

Proenzyme

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33
Q

CoEnzyme + ApoE =?

A

HoloE

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34
Q

Cause of interference/stop/ prevent

A

Inhibitors

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35
Q

Binds to the active site of an enzyme and is reversible (Substrate >
Inhibitor)

A

Competitive Inhibitor

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36
Q

Bind to the allosteric site (cofactor site) and is Irreversible

A

Noncompetitive Inhibitor

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37
Q

Binds to the enzyme-substrate complex (increased substrate is equal
to increased enzyme-substrate complex is equal increased inhibition)

A

Uncompetitive Inhibitor

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38
Q

Same catalyctic reactions but slightly different molecular structures and involve in Fractionation of
isoenzymes

A

Isoenzymes

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39
Q

Optimum temperature for enzymatic activity

A

37°C / body temp

40
Q

increased temperature is equal to?

A

increased reaction

rate or increased movement of molecules

41
Q

Denaturation of enzymes

A

40-50°C

42
Q

Inactivation of enzymes

A

60-65°C

43
Q

For every 10⁰C increase in temperature, there will be a two-fold increase in enzyme
activity.

A

Temperature Coefficient

44
Q

Most physiologic reactions occur in?

A

pH range of 7-8 (neutral to slightly alkaline)

45
Q

Temperature for the storage of enzymes for longer periods of time

A

20°C

46
Q

Temperature for storage for coenzymes

A

2-8°C

47
Q

Temperature for storage for LDH (LDH 4 and 5)

A

Room Temp

48
Q

Mostly increases enzyme concentration.

A

Hemolysis

49
Q

Decreases enzyme concentration

A

Lactescence or milky specimen (CHYLE)

50
Q

Test for rape victims

A

Acid Phosphatase (ACP)

51
Q

In which body fluid is ACP found

A

Semen or in prostate (fluid)

52
Q

Adopted classification system in

A

1961

53
Q

Revision years

A

1972, 1978

54
Q

Defines the substrate acted on.

A

Systemic ANme

55
Q

are lengthy, a more usable and trivial.

A

Systemic Name

56
Q

Assign by the IUB system

A

Recommended Name

57
Q

System associated with ACE

A

Renin-Angiotensine-Aldosterone System

58
Q

Catalyze an oxidation-reduction reaction between two substrates

A

Oxidoreductase

59
Q

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

A

Transferases

60
Q

Catalyze hydrolysis of various bonds

A

Hydrolases

61
Q

Catalyze removal of groups from substrates without hydrolysis; the product contains double bonds

A

Lyases

62
Q

Catalyze the interconversion of geometric, optical, or positional isomers

A

Isomerase

63
Q

Catalyze the joining of two substrate molecules, coupled with breaking of the pyrophosphate bond in adenosine triphosphate (ATP) or a similar compound

A

Ligases

64
Q

Enzymes included in Oxidoreductase

A

LDH, G-6-PDH, Glumate Dehydrogenase

HYDROGENASES

65
Q

Enzymes included in Transferases

A

AST, ALT, GGT, Glutathione-S-Tranferase, Phosphorylase, Pyruvate kinase1 (PK)

[TRANSFERASES, PHOSPHORYLASE, KINASE)

66
Q

Enzymes in Hydrolases

A

Alkaline Phosphatase (ALP), ACP, α-Amylase (AMY), Cholinesterase (CHE, PCHE), Chymotrypsin (CHY), ELastase-1 (E1), 5-Nucleotidase (NTP), Triacyglyerol lipase (LPS), Trypsin (TRY)

67
Q

Enzymes in Lyases

A

Aldolase (ALD)

68
Q

Enzymes in Isomerases

A

Triphosphate isomerase (TPI)

69
Q

Ligase

A

Glutathione Synthetase (GSH-S)

70
Q

may occur spontaneously if the free energy or available kinetic energy is higher for the reactants than for the products

A

Chemical Reaction

71
Q

also called excess energy

A

Activation Energy

72
Q

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

A

Activation Energy

73
Q

The general relationship among the enzyme, substrate, and product may be represented as follows:

A

E + S → ES → E + P

74
Q

is a physical binding of a substrate to the active site of an enzyme.

A

Enzyme-Substrate Complex

75
Q

combined with all substrates containing a particular chemical group, such as phosphate ester.

A

Group Specific

76
Q

Enzymes that are specific to chemical bonds exhibits _________________.

A

Bond Specificity

77
Q

refers to enzymes that predominantly combine with only one optical isomer of a certain compound

A

Stereoisometric Specificity

78
Q

The rate at which an enzymatic reaction proceeds and whether the forward or reverse reaction occurs depend on several reaction conditions.

A

Substrate Concentration

79
Q

One major influence on enzymatic reactions is________________.

A

Substrate Concentration

80
Q

The reaction rate is directly proportional to substrate concentration

A

First-Order Kinetics

81
Q

The reaction rate depends only on enzyme concentration

A

Zero-Order Kinetics

82
Q

Shape of the key (substrate) must fit into the lock (enzyme)

A

Emil Fisher’s/ Lock and Key Theory

83
Q

Base on the substrate binding to the active site of the enzyme; Acceptable theory

A

Kochland/ Induced Fit Theory

84
Q

Measurement of Enzyme Activity in terms of:

A
  • Change in substrate concentration
  • Change in product concentration
  • Change in coenzyme concentration
85
Q

Absorbance is made at 10-second intervals for 100 seconds

A

Nonkinetic Assay

86
Q

To measure the extent of enzymatic reactions, 2 general methods may be used

A
  1. Fixed-Time Assay

2. Continuous monitoring/ Kinetic Assay

87
Q

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

A

Fixed Time Assay

88
Q

Multiple measurements of changed in absorbance are made during the reaction; It is preferred than fixed-time

A

Continuous monitoring/ Kinetic assay

89
Q

1 micromole of substrate/minute (MI-MI-U)

A

International Unit ( IU o U)

90
Q

1 mole of substrate/second (MO-SE-KU)

A

Katal Unit (KU)

91
Q

Quantified base one their activity rather than absolute values

A

Katal unit

92
Q

The units used to report enzyme levels in kinetic assay are

A

activity units

93
Q

The definition for activity unit must consider change in pH, temperature, substrate, etc.

A

Katal unit (KU)

94
Q

Causes of Elevated Plasma Enzyme Levels:

A
  1. Impaired removal of enzyme form plasma
  2. Increased permeability of cell membrane
  3. Increased in the number of cells or production of cells
  4. Increased in the normal cell turnover
  5. Decreased clearance of enzymes
  6. Tissue necrosis and degradation
95
Q

Catalyst, speeds up rnx, responsible for break down

A

Enzymes

Clinical Chemistry 2 (2 decks)

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