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Clinical Chemistry 2 > Lecture: Enzymology > Flashcards

Lecture: Enzymology Flashcards

1
Q

Protein part of an enzyme without the cofactor necessary for catalysis

A

Apoenzyme

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2
Q

An effector molecule that increases the catalytic activity of an enzyme when it binds to a specific site

A

Activator

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3
Q

Substance that diminishes the rate of a chemical reaction

A

Inhibitor

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4
Q

Property of a catalyst that is measured by the catalyzed rate of conversion of a specified chemical reaction produced in a specified assay system

A

Catalytic Activity

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5
Q

When combined with an inactive protein called an apoenzyme, forms an active compound (complete enzyme) called a holoenzyme

A

Coenzyme

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6
Q

A protein molecule that catalyzes chemical reaction without itself being destroyed, altered, consumed

A

Enzyme

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7
Q

Group of related enzymes catalyzing the same reaction but having different molecular structures and physical, biochemical, and immunological properties

A

Isoenzyme

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8
Q

Amount of enzyme that catalyzes the conversion of one micromole of substrate per minute under the specified conditions of the assay method

A

International Unit

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9
Q

A reactant in a catalyzed reaction

A

Substrate

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10
Q

Substance produced by the enzyme-catalyzed conversion of a substrate

A

Product

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11
Q

Water-free cavity; specific portion of enzyme that binds on the substrate

A

Active Site

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12
Q

A cavity other than the active site which may bind with regulatory molecules

A

Allosteric Site

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13
Q

When bound tightly to the enzyme, the coenzyme is called

A

Prosthetic group

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14
Q

Digestive enzyme originally secreted from the organ of production is called a

A

Proenzyme
Zymogen

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15
Q

Apoenzyme and coenzyme forms a complete and active system known

A

Holoenzyme

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16
Q

Enzyme have a rigid active site; The shape of the key (substrate) must fit into the lock (enzyme)

A

Emil Fisher’s / Lock and Key Theory

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17
Q

Enzyme has a flexible active site; Based on the substrate binding to the active site of the enzyme

A

Kochland / Induced Fit Theory

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18
Q

The minimum energy input needed for a reaction to occur and convert the substrates into products

A

Activation Energy

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19
Q

A molecular intermediate between the substrate and its product, through which the reaction passes

A

Transition State

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20
Q

Enzymes work by _ activation energy

A

Lowering

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21
Q

An enzyme combines with only one substrate and catalyzes only one reaction

A

Absolute Specificity

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22
Q

Enzymes combine with all the substrates in a chemical group

A

Group Specificity

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23
Q

Enzymes reacting with specific chemical bonds

A

Bond Specificity

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24
Q

Isoenzymes/isoforms

A

Stereoisomers

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25
Q

If the reaction reached the maximum velocity, no reaction will happen.

A

Michaelis Menten Kinetics

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26
Q

Reaction rate depends only on enzyme concentration

A

Zero-Order Reaction

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27
Q

Reaction rate is directly proportional to the substrate concentration

A

First-Order Reaction

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28
Q

The rate of reaction depends on the doubled concentration of one reactant or on the product of concentration of two reactants

A

Second-Order Reaction

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29
Q

6 Enzyme Nomenclature

A

Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerases
Ligases

30
Q

Catalyzes the transfer of electrons from 1 molecule (oxidant) to another molecule (reductant)

A

Oxidoreductases

31
Q

Oxidoreductases often requires cofactors such as _

A

NADPH

32
Q

Add hydroxyl groups to a substrate

A

Hydroxylases

33
Q

Intramolecular oxygen is the hydrogen or electron acceptor

A

Oxidases

34
Q

Oxidize a substrate by transferring one or more hydride ion

A

Dehydrogenase

35
Q

Reduction of hydrogen peroxide and organic hydroperoxides

A

Peroxidase

36
Q

Catalyze reductions

A

Reductase

37
Q

Incorporate intramolecular oxygen into organic substrates

A

Oxygenase

38
Q

Enzymes that catalyze the movement of a functional group from one molecule to another

A

Transferases

39
Q

Enzymes are involved in catalyzing the transfer of phosphate groups in a process called phosphorylation

A

Kinase

40
Q

Enzymes that catalyzes the transfer an amine group

A

Deaminases

41
Q

Catalyzes hydrolysis (breaking of single bonds through the addition of water)

A

Hydrolase

42
Q

Catalyzes lysis reactions that generate a double bond; type of elimination reaction but not hydrolytic or oxidative; often referred to as synthase enzymes

A

Lyases

43
Q

Catalyzes addition reaction (substrate is added to a double bond)

A

Reverse Reaction

44
Q

Enzymes that catalyzes structural changes within a molecule

A

Isomerases

45
Q

Joining enzymes; responsible for catalyzing ligation of 2 molecules with the hydrolysis of a diphosphate bond in ATP or any triphosphate

A

Ligases

46
Q

Associated with a unique numerical code designation

A

Enzyme Commission Numerical Nomenclature

47
Q

First EC Digit of oxidoreductases

A

1

48
Q

First EC Digit of transferases

A

2

49
Q

First EC Digit of hydrolases

A

3

50
Q

First EC Digit of lyases

A

4

51
Q

First EC Digit of isomerases

A

5

52
Q

First EC Digit of ligases

A

6

53
Q

The temperature at which the enzyme is most active, catalyzing the largest number of reactions per second

A

Optimum Temperature

54
Q

Most enzymes in the human body function best at about _

A

37 degrees Celsius

55
Q

The rate of denaturation increases as the temperature increases and is usually significant at

A

40°C to 50°C

56
Q

Looser, more random structure, and become insoluble

A

Denatured proteins

57
Q

The process where the enzyme loses its shape and active site

A

Denaturation

58
Q

Low temperature or freezing does not usually destroy enzymes, except:

A

LD – freezing at -20 degrees C
CK – storing at 4 degrees C

59
Q

Enzymes that work best at acidic conditions

A

Renin and pepsin

60
Q

Enzymes that work best at alkaline conditions

A

Intestinal enzymes

61
Q

Enzymes that work best at neutral conditions

A

Amylase

62
Q

At pH slightly above or below the optimum, enzyme activity _

A

Reduces

63
Q

At extreme pH conditions, enzymes are _

A

Denatured

64
Q

Physically bind to the active site of an enzyme and compete with the substrate for the active site; reversible

A

Competitive inhibitors

65
Q

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

A

Noncompetitive inhibitor

66
Q

Another kind of inhibition in which the inhibitor binds to the ES complex

A

Uncompetitive inhibition

67
Q

Reaction takes place at a certain period; reactions are combined; reaction proceeds for a designated time; reaction is assumed to be linear over the reaction time; the larger the reaction, the more enzyme is present

A

Fixed-Time (Endpoint Method)

68
Q

Measured absorbance at a certain period; More advantageous than fixed time – allows monitoring of linearity

A

Continuous Monitoring (Kinetic Assay)

69
Q

Amount of enzyme that catalyzes 1 micromole of substrate per minute

A

International Unit (IU/U)

70
Q

1 mole of substrate per second

A

Katal Unit (KU)

Clinical Chemistry 2 (5 decks)

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