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Enzyme > Harpers > Flashcards

Harpers Flashcards

1
Q

Biologic polymers that catalyze the chemical reactions

A

Enzymes

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2
Q

Characteristics of enzymes

A

Catalytic activity
Substrate specificity
Stereospecificity

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3
Q

Enzymes are classified by reaction type. Name the six classes of enzymes.

A 
Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerases
Ligases
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4
Q

Naming enzymes may use modifiers to indicate the:

A

Substrate
Source of the enzymes
Regulation
Feature of its mechanism of action

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5
Q

Enzymes that catalyze oxidations and reductions

A

Oxidoreductases

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6
Q

Enzymes that catalyze transfer of moieties such as glycosyl, methyl, or phosphoryl groups

A

Transferases

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7
Q

Enzymes that catalyze hydrolytic cleavage of C-C, C-O, C-N and other covalent bonds

A

Hydrolases

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8
Q

Enzymes that catalyze cleavage of C-C, C-O, C-N and other covalent bonds by atom elimination, generating double bonds

A

Lyases

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9
Q

Enzymes that catalyze geometric or structural changes within a molecule

A

Isomerases

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10
Q

Enzymes that catalyze the joining together of two molecules in reactions coupled to the hydrolysis of ATP

A

Ligases

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11
Q

Tightly and stably incorporated into a protein’s structure by covalent or noncovalent forces

A

Prosthetic group

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12
Q

Examples are pyridoxal phosphate, flavin mononucleotide, flavin adenine dinucleotide, thiamin pyrophosphate, biotin, metal ions of cobalt, copper, magnesium, manganese, zinc

A

Prosthetic group

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13
Q

Enzymes that contain tightly bound metal ions

A

Metalloenzymes

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14
Q

Serve functions similar to those of prosthetic groups but bind in transient, dissociable manner either to the enzyme or to a substrate such as ATP

A

Cofactors

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15
Q

Must be present in the medium surrounding the enzymes for catalysis to occur

A

Cofactors

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16
Q

Enzymes that require a metal ion cofactor

A

Metal-activated enzyme

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17
Q

Serve as recyclable shuttle-or group transfer agents-that transport many substrates from one point within the cell to another

A

Coenzymes

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18
Q

Stabilize species such as hydrogen atoms or hydride ions that are too reactive to persist for any significant time period in the presence of the water or organic molecules that permeate the cell interior

A

Coenzymes

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19
Q

Adaptor or handle that facilitates the recognition and binding of small chemical groups

A

Coenzymes

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20
Q

Many coenzymes, cofactors and prosthetic groups are derivatives of ____

A

B vitamins

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21
Q

Component of the redox coenzymes NAD and NADP

A

Nicotamide

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22
Q

Component of the redox coenzymes FMN and FAD

A

Riboflavin

23
Q

Component of the acyl group carrier coenzyme A

A

Pantothenic acid

24
Q

Participates in decarboxylation of alpha-keto acids

A

Thiamin

25
Q

Function in one-carbon metabolism

A

Folic acid

Cobamide

26
Q

Enzymes and substrates interact to form ES complex whose thermal stability was ___ than that of enzyme itself

A

Greater

27
Q

Recognition site for binding substrates

A

Active site

28
Q

The higher the concentration of enzyme and substrate, the ___ frequently they will encounter one another, and the ___ will be the rate of the reaction.

A

More

Greater

29
Q

True or false
In specific acid catalysis or specific base, the rate of reaction is sensitive to changes in the concentration of protons and dependent of the concentrations of other acids or bases present in the solution or at the active site.

A

False

Independent of the concentration of other acids or bases present in the solution

30
Q

Reactions whose rates are responsive to all the acids or bases present are said to be subject to ____

A

General acid/base catalysis

31
Q

Enzymes that catalyze ___ reactions that involve breaking a covalent bond typically bind their substrate in a conformation that is somewhat unfavorable for the bond that will undergo cleavage

A

Lytic

32
Q

A transient species that represents the transition state in the transformation of substrates to products

A

Transition state intermediates

33
Q

The process of ____ involves the formation of a covalent bond between the enzyme and one or more substrates

A

Covalent catalysis

34
Q

Covalent catalysis introduces a new reaction pathway whose activation energy is ___ than the reaction pathway in homogenous solution.

A

Lower

35
Q

When substrates approach and bind to an enzyme they induce a conformational change analogous to placing a hand into a glove

A

Induced fit model

36
Q

Exquisitely high specificity with which enzymes discriminate their substrates when forming an ES complex

A

Lock and key model

37
Q

Several physically distinct versions of a given enzyme, each of which catalyzes the same reaction

A

Isoenzyme

38
Q

Field of biochemistry concerned with the quantitative measurement of the rates of enzyme-catalyzed reactions and the systematic study of factors that affect these rates

A

Enzyme kinetics

39
Q

Anything that increases the frequency or energy of collision between substrates will ___ the rate of the reaction in which they participate

A

Increase

40
Q

Two factors that increase the frequency of collision between substrate

A

Temperature

Reactant concentration

41
Q

True or false

The presence of an enzyme alters the equilibrium constant of the reaction.

A

False
It only lowers the activation energy. Since they emerge unchanged at the completion of the reaction, they do not affect the free energy for the overall reaction.

42
Q

In Michaelis-Menten equation, when [S] is considerably below Km, v is proportionate to k[S]. Therefore, the initial reaction velocity is ____ to [S].

A

Directly proportional

43
Q

In Michaelis-Menten equation, when [S] = Km, the initial velocity is ___.

A

Half-maximal

44
Q

The linear form of Michaelis-Menten equation

A

Double reciprocal plot

Lineweaver-Burk plot

45
Q

When further increases in substrate concentration do not further increase velocity, the enzyme is said to be ___ with the substrate

A

Saturated

46
Q

An exclusive property of multimeric enzymes that bind substrate at multiple sites

A

Cooperative behavior

47
Q

Inhibitor binds to the substrate-binding portion of the active site thereby blocking access by the substrate

A

Competitive inhibition

48
Q

Can be overcome by raising the concentration of substrate

A

Competitive inhibition

49
Q

Acts by decreasing the number of free enzyme molecules available to bind the substrate to form ES and thus eventually to form product

A

Competitive inhibitor

50
Q

Competitive inhibitor has no effect on ____ but raises the ___

A

Vmax

Km apparent

51
Q

Binding of the inhibitor does not affect binding of the substrate

A

Noncompetitive inhibition

52
Q

Formation of both EI and EIS complexes is possible

A

Noncompetitive inhibition

53
Q

True or false
Competitive and noncompetitive inhibitors are reversible inhibitors, meaning the inhibitors form a dissociable, dynamic complex with the enzyme

A

True

54
Q

Modifications of enzyme involving making or breaking covalent bonds essential for substrate binding, catalysis or maintenance of the enzyme’s conformation

A

Irreversible inhibitors

Enzyme (2 decks)

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