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biochem > (M) Enzymes > Flashcards

(M) Enzymes Flashcards

1
Q

Largely ‘protein’ in nature produced by living cells

A

Enzymes

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2
Q

Specific biological proteins involved in the catalysis of biochemical reactions.

A

yaurrr Enzymes

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3
Q

TOF. Enzymes alter the equilibrium point, resulting in the formation of products

A

F

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4
Q

Plays an important role in Metabolism, Diagnosis, and Therapeutics

A

Enzymes

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5
Q

What does an increase of serum or plasma enzyme indicate?

A

Bacterial infection

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6
Q

TOF. Inhibition of some enzyme also have therapeutic values

A

Tru

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7
Q

Group of enzymes catalyze an oxidation rxn between two substrates?

A

Oxidoreductases

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8
Q

Catalyze the transfer of a group other than Hydrogen fr one substrate to another

A

Transferases

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9
Q

Catalyzes the hydrolysis of a different bond

A

Hydrolases

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10
Q

Catalyzes the removal of groups from a substrate without hydrolysis (*prod. formed contains double bonds)

A

Lyases

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11
Q

Catalyze the interconversion of geometric optical/ positional isomers

A

Isomerases

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12
Q

Catalyze the joining of two substrate molecules

A

Ligases

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13
Q

Enzymes are classified into how many functional classes (EC number classification) ?

A

6

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14
Q

Types of Reactions that EC.1 enzymes catalyze

A

Oxidoreductases

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15
Q

Types of Reactions that EC.2 enzymes catalyze

A

Transferases

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16
Q

Types of Reactions that EC.3 enzymes catalyze

A

Hydrolases

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17
Q

Types of Reactions that EC.4 enzymes catalyze

A

Lyases

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18
Q

Types of Reactions that EC.5 enzymes catalyze

A

Isomerases

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19
Q

Types of Reactions that EC.6 enzymes catalyze

A

Ligases

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20
Q

According to the IUB, the 1st no. in the nomenclature of enzymes indicates what?

A

Class

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21
Q

According to the IUB, the 2nd no. in the nomenclature of enzymes indicates what?

A

Sub-class

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22
Q

According to the IUB, the 3rd no. in the nomenclature of enzymes indicates what?

A

Sub-sub-class

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23
Q

According to the IUB, the 4th no. in the nomenclature of enzymes indicates what?

A

Enzyme Serial No.

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24
Q

Greatly increase the rate of chemical reactions

A

Enzymes

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25
Q

TOF. Without enzymes, there will still be a formation of products

A

True (but slower)

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26
Q

TOF. Enzymes typically disrupt the transformation of one energy form into a more usable form

A

F (help)

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27
Q

TOF. Enzymes require helper molecules

A

True

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28
Q

TOF. Enzymes bind to specific reactants

A

True

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29
Q

Type of enzyme specificity that catalyzes one type of reaction for a single substrate

A

Absolute

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30
Q

Type of enzyme specificity that catalyzes one type of reaction for similar substrates

A

Group

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31
Q

Type of enzyme specificity that catalyzes one type of reaction for a specific type of bond

A

Linkage

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32
Q

TOF. Nearly all enzymes are proteins

A

True (with le exception of ribozymes)

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33
Q

TOF: Enzymes are used up and changed at the end of the reaction

A

F (not used up and remain unchanged)

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34
Q

TOF. Enzymes are free to attach to another substrate after releasing the product

A

True

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35
Q

Difference between the energies of the reactions and the energies of the products of a reaction

A

Standard free energy change or DG°

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36
Q

Energy input required to initiate a reaction

A

Free Energy of Activation or Activation Energy

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37
Q

TOF. Activation Energy for a catalyzed reaction is higher than an uncatalyzed reaction.

A

False (baliktad sizt)

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38
Q

TOF. Spontaneous = Instantaneous

A

False (spontaneity of a rxn depends on the concentration but it will never be instant)

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39
Q

Stable in the air with an unlimited supply of oxygen

A

Glucose

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40
Q

Relationship between Activation Energy and Rate of Reaction

A

Indirectly proportional

41
Q

The apex of the curve (from activation energy profile) is the energy that drives the

A

Transition state

42
Q

Enzymes lower the Activation Energy by

A

Stabilizing the Transition State

43
Q

TOF. The same amount of reactants and products are produced with or w/o enzymes

A

True (they only differ in the rate of reaction to form the products)

44
Q

The Site that has an important role in stabilizing the Transition State

A

Google eme,, Active Site

45
Q

Specific Region of the Enzyme that binds to the substate

A

Active Site

46
Q

Attachment point of substrates in an enzyme

A

Active Site (Binding Site Cleft)

47
Q

Substrates bind usually thru what interaction?

A

Noncovalent interaction

48
Q

Components of the Active Site:

A
  1. Contact Residues
  2. Catalytic Residues
  3. Structural Residues
  4. Non-essential Residues
49
Q

Makes up only a small portion of the overall enzyme

A

Active Site

50
Q

Have complementary structures corresponding to their substrates

A

Active Site

51
Q

2 Models developed to describe the binding process of substrates

A
  1. Lock and Key Model
  2. Induced Fit Model
52
Q

Model that assumes a high-level of similarity between substrate and geometry of the enzyme

A

Lock and Key Model

53
Q

TOF. In Lock and Key Model the active site has a flexible shape

A

F (rigid shape)

54
Q

Model; Only substrates with the matching shape can fit

A

Lock and Key Model

55
Q

Is a key that fits the lock of the active site

A

Substrate

56
Q

TOF. The lock and key model works for all enzymes

A

False

57
Q

Binding of the substrate induces a conformation change in the enzyme that result in a complementary fit

A

Induced-Fit Model

58
Q

Has a greater range of substrate specificity

A

Induced-Fit Model

59
Q

This model is more consistent with a wider range of enzymes

A

Induced Fit Model

60
Q

In Induced fit model the active site is

A

Flexible, not rigid

61
Q

TOF. The shape of the enzyme, active site, and substrate improve catalysis

A

True

62
Q

In the Michaelis-Menten Approach to Enzyme Kinetics, what does k1 represent?

A

Rate constant for the formation of the Enzyme-Substrate Complex (ES)

63
Q

In the Michaelis-Menten Approach to Enzyme Kinetics, what does k-1 represent?

A

Rate constant for the reverse reaction (dissociation of ES)

64
Q

In the Michaelis-Menten Approach to Enzyme Kinetics, what does k2 represent?

A

Rate constant of ES to form products

65
Q

When was the Michaelis-Menten Equation developed?

A

late 1913

66
Q

Order of Reaction where the rate depends on concentration of substrate

A

First order

67
Q

Order of Reaction where the rate does not depend on concentration of substrate

A

Zeroth order

68
Q

Order of Reaction where the rate depends on concentration of enzyme

A

First order

69
Q

Amount of enzyme which will catalyze the transformation of 1μmol of substrate per minute

A

Enzyme unit

70
Q

Catalytic activity which will raise the rate of a reaction by 1 mole per second in a specified system

A

katal

71
Q

List the ways on how an inhibitor can affect enzymatic reaction

A
  1. Reversible
  2. Irreversible
72
Q

Enzyme inhibition where inhibitors permanently bind to the enzyme through the formation of a covalent bond

A

Irreversible inhibition

73
Q

TOF. In an irreversible inhibition, the enzymes can still be regenerated

A

False (the inhibitors permanently bind to the active site = not enzymatically active)

74
Q

Inhibitors that easily dissociate

A

Reversible Inhibition

75
Q

Types of Reversible Inhibition

A
  1. Competitive
  2. Uncompetitive
  3. Noncompetitve
76
Q

Type of Enzyme Inhibition where the inhibitor resembles the shape of the actual substrate and prevents the substrate from binding to the active site

A

Competitive

77
Q

Increases Km, Vmax is unaffected

A

Competitive

78
Q

Can be resolved by increasing the S

A

Competitive

79
Q

Type of Enzyme Inhibition where an allosteric site is already present before the substrate binds to the active site

A

Noncompetitive

80
Q

Decreases Vmax, does not affect Km

A

Noncompetitive

81
Q

Slows down enzyme efficiency (turnover number=how fast the enzyme can catalyze reaction)

A

Noncompetitive

82
Q

TOF. Catalysis can still occur even in the presence of an inhibitor

A

False (it does not)

83
Q

The binding of the Substrate (S) to the active site
creates a crevice/pocket called
Allosteric site.

A

Uncompetitive

84
Q

If it is in close proximity with the ES complex, then this will prevent the S from dissociating from the active site

A

Uncompetitive

85
Q

Cannot be overcome by increasing S

A

Uncompetitive

86
Q

Decreases both Km and Vmax=parallel

A

Uncompetitive

87
Q

Equation that helps in exacting the value for Vmax because it is simply the reciprocal of the constant values in the equation.

A

Lineweaver Burke Eqn

88
Q

List down the 3 factors that influence enzyme activity

A
  1. Environmental Conditions
  2. Cofactors and Coenzymes
  3. Enzyme Inhibitors
89
Q

Extreme temperatures are the most dangerous

A

Environmental Conditions

90
Q

Significant temperature range where denaturation of enzyme occur

A

40° - 50°

91
Q

TOF. High temperatures may denature (unfold) the enzyme

A

True

92
Q

TOF. Rate of a chemical reaction
increases with temperature.

A

True (each 10° inc. in temp will double the rate of reaction until the protein is denatured)

93
Q

The temp at which enzymatic reaction occurs fastest

A

Optimum Temperature

94
Q

Ideal temperature for an enzymatic reaction

A

37°

95
Q

TOF. Rate of reaction increases as substrate concentration decreases

A

False (substrate concentration increases)

96
Q

TOF. Maximum activity occurs when the enzyme is saturated (when all enzymes are binding to the substrate)

A

True

97
Q

Inorganic substances (zinc, iron, Cu) and vitamins (respectively) are sometimes needed for proper enzymatic activity.

A

Cofactors and Coenzymes

98
Q

Once coenzymes are bound to enzymes they are called

A

Prosthetic groups

biochem (31 decks)

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