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

25
Function in one-carbon metabolism
Folic acid | Cobamide
26
Enzymes and substrates interact to form ES complex whose thermal stability was ___ than that of enzyme itself
Greater
27
Recognition site for binding substrates
Active site
28
The higher the concentration of enzyme and substrate, the ___ frequently they will encounter one another, and the ___ will be the rate of the reaction.
More | Greater
29
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.
False | Independent of the concentration of other acids or bases present in the solution
30
Reactions whose rates are responsive to all the acids or bases present are said to be subject to ____
General acid/base catalysis
31
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
Lytic
32
A transient species that represents the transition state in the transformation of substrates to products
Transition state intermediates
33
The process of ____ involves the formation of a covalent bond between the enzyme and one or more substrates
Covalent catalysis
34
Covalent catalysis introduces a new reaction pathway whose activation energy is ___ than the reaction pathway in homogenous solution.
Lower
35
When substrates approach and bind to an enzyme they induce a conformational change analogous to placing a hand into a glove
Induced fit model
36
Exquisitely high specificity with which enzymes discriminate their substrates when forming an ES complex
Lock and key model
37
Several physically distinct versions of a given enzyme, each of which catalyzes the same reaction
Isoenzyme
38
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
Enzyme kinetics
39
Anything that increases the frequency or energy of collision between substrates will ___ the rate of the reaction in which they participate
Increase
40
Two factors that increase the frequency of collision between substrate
Temperature | Reactant concentration
41
True or false | The presence of an enzyme alters the equilibrium constant of the reaction.
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
In Michaelis-Menten equation, when [S] is considerably below Km, v is proportionate to k[S]. Therefore, the initial reaction velocity is ____ to [S].
Directly proportional
43
In Michaelis-Menten equation, when [S] = Km, the initial velocity is ___.
Half-maximal
44
The linear form of Michaelis-Menten equation
Double reciprocal plot | Lineweaver-Burk plot
45
When further increases in substrate concentration do not further increase velocity, the enzyme is said to be ___ with the substrate
Saturated
46
An exclusive property of multimeric enzymes that bind substrate at multiple sites
Cooperative behavior
47
Inhibitor binds to the substrate-binding portion of the active site thereby blocking access by the substrate
Competitive inhibition
48
Can be overcome by raising the concentration of substrate
Competitive inhibition
49
Acts by decreasing the number of free enzyme molecules available to bind the substrate to form ES and thus eventually to form product
Competitive inhibitor
50
Competitive inhibitor has no effect on ____ but raises the ___
Vmax | Km apparent
51
Binding of the inhibitor does not affect binding of the substrate
Noncompetitive inhibition
52
Formation of both EI and EIS complexes is possible
Noncompetitive inhibition
53
True or false Competitive and noncompetitive inhibitors are reversible inhibitors, meaning the inhibitors form a dissociable, dynamic complex with the enzyme
True
54
Modifications of enzyme involving making or breaking covalent bonds essential for substrate binding, catalysis or maintenance of the enzyme's conformation
Irreversible inhibitors