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My MCAT Biology > Enzymes & Inhibition > Flashcards

Enzymes & Inhibition Flashcards

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1
Q

Allosteric effector

A

Binds at the allosteric site and induces a change in the conformation of the enzyme so the substrate can no longer bind to the active site. Displays cooperativity, so it does not obey MichaelisMenten kinetics.

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2
Q

Hill coefficient = 1

A

No cooperativity (normal MM kinetics); Substrate binding doesn’t affect affinity

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3
Q

this enzyme Moves a functional group from one molecule to another

A

transferase

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4
Q
A

competitive inhibition

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5
Q

Hill coefficient

A

measure of cooperatively (ie Hb, where you see sigmoidal kinetic curves that don’t follow Michaelis-Menten)

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6
Q

hydrolysis of fats is included in this class of enzymes

A

lyases

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7
Q

in uncompetitive inhibition, Vmax…

A

decreases

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8
Q

catalyzes cleavage without H2O or the transfer of electrons

A

lyases

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9
Q

On the LWBP, competitive inhibition effects the X-intercept by…

A

increases it (moves toward the origin)

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10
Q

Prosthetic groups

A

tightly bound cofactors or coenzymes that are necessary for enzyme function

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11
Q

Hill coefficient > 1

A

positive cooperativity; Substrate binding increases affinity

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12
Q

dehydrogenase, oxidase, and peroxidase are all ____ enzymes

A

oxidoreductases

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13
Q

this type of enzyme is known for addition/synthesis reactions and usually requires ATP

A

ligases

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14
Q

Glycosylation

A

covalent modification w/ carbohydrate (adding sugar)

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15
Q

phosphotransferases that add a phosphate group, usually with ATP as a donor

A

kinases

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16
Q

On the LWBP, competitive inhibition effects the Y-intercept by…

A

no change

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17
Q

Enzyme-catalyzed reactions w/ high enzyme-substrate affinity will reach the ½Vmax benchmark at a (lower/higher) [substrate] aka have a (lower/higher) Km; lower enzyme-substrate affinities → needing a (lower/higher) [substrate] to reach ½Vmax (have a (lower/higher) Km).

A

Enzyme-catalyzed reactions w/ high enzyme-substrate affinity will reach the ½Vmax benchmark at a lower [substrate] aka have a lower Km; lower enzyme-substrate affinities → needing a higher [substrate] to reach ½Vmax (have a higher Km).

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18
Q

in noncompetitive inhibition, Km…

A

doesn’t change

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19
Q

these enzymes introduce a phosphate group into an organic molecule (glucose)

A

phosphorylase

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20
Q

this type of enzyme joins two large biomolecules, often of the same type

A

ligases

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21
Q

cofactor

A

Inorganic ions and metal cation; like Fe²⁺ and Mg²⁺; directly involved in the enzyme’s catalytic mechanism

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22
Q

If Vmax increases, the paramater values ______. The intercept _____ and moves ______ the origin.

A

If Vmax increases, the paramater values doubles. The intercept decreases (becomes less +) and moves towards the origin.

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23
Q

this type of enzyme is used to create bonds b/t Okazaki fragments

A

ligases

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24
Q

In this type of inhibition, the inhibitor is similar to the substrate and binds @ the active site

A

competitive inhibitor

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25
Q

In enzyme kinetics, calculate v0

A
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26
Q

this class of enzymes includes the interconversion of isomers, constitutional & stereoisomers

A

isomerases

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27
Q

in this type of inhibition, the inhibitor binds w/ unequal affinity to the enzyme and the enzyme-substrate complex

A

mixed inhibition

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28
Q

a synthase could also be a ______ but a synthetase must be a _____

A

a synthase could also be a synthase but a synthetase must be a ligase

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29
Q

Coenzyme

A

Organic molecule; like heme, NAD⁺ & Coenzyme A. Many are derived from vitamins

30
Q

heterotrophic effector

A
31
Q

where is the binding site in noncompetitive inhibition

A
32
Q

In this type of inhibition, the inhibitor binds with equal affinity to the enzyme and the enzyme-substrate complex

A

noncompetitive inhibition

33
Q

Irreversible inhibition:

A

alters the enzyme so that the active site is unavailable for a prolonged duration or permanently; new enzymes molecules must be synthesized for the rxn to occur again

34
Q

On the LWBP, uncompetitive inhibition effects the X-intercept by…

A

decreases it (moves away from the origin)

35
Q

If the mixed inhibitor ends up binding more readily to the _____ Km is lower

A

If the mixed inhibitor ends up binding more readily to the enzyme-substrate complex Km is lower

36
Q

Enzyme kinetics equaiton, what does v = ?

A
37
Q

On the LWBP, uncompetitive inhibition effects the Y-intercept by…

A

increases (moves away from the origin)

38
Q

where is the binding site in competitive inhibition?

A

active site

39
Q

these remove a phosphate group

A

phosphatase

40
Q

in mixed inhibition, Km…

A

increases or decreases

41
Q

in competitive inhibition, Km…

A

increases

42
Q

Km

A

The [S] at which an enzyme runs at half its Vmax.

43
Q

transaminase is an example of a ______ enzyme

A

transferase

44
Q

nucleic acid synthesis uses these kind of enzymes

A

ligases

45
Q

On the LWBP, mixed inhibition effects the X-intercept by…

A

increases or decreases it (moces towards or away from the origin)

46
Q

how does increasing the amount of substrate affect Vmax

A

increasing substrate = increases Vmax

47
Q

On the LWBP, mixed inhibition effects the Y-intercept by…

A

increases (moves away from the origin)

48
Q

isomerases include

A

oxidoreductases, transferases, lyases

49
Q

Hill coefficient n < 1

A

negative cooperativity; Substrate binding decreases affinity for subsequent substrate

50
Q

these generates either a double bound or ring structure

A

lyases

51
Q

Cleavage with H₂O = ____ enzyme

A

hydrolases

52
Q
A

Noncompetitive inhibition

53
Q

aminotransferase is an example of a _____ enzyme

A

transferase

54
Q

On the LWBP, noncompetitive inhibition effects the X-intercept by…

A

no change

55
Q

In this type of inhibition, the the inhibitor binds only with the enzyme-substrate complex

A

uncompetitive inhibition

56
Q

On the LWBP, noncompetitive inhibition effects the Y-intercept by…

A

increases (moves away from the origin)

57
Q

If the mixed inhibitor ends up binding more readily to the _____ Km is higher

A

If the mixed inhibitor ends up binding more readily to the enzyme Km is higher

58
Q

in mixed inhibition, Vmax…

A

decreases

59
Q

where is the binding site in mixed inhibition

A

allosteric site

60
Q

These only require 1 substrate when cleaving but 2 for the reverse

A

lyases

61
Q

Vmax

A

The max rate (enzyme velocity) at which an enzyme can catalyze a reaction; when all enzyme active sites are saturated with substrate

62
Q

in uncompetitive inhibition, Km…

A

decreases

63
Q

in competitive inhibition, Vmax…

A

doesn’t change

64
Q

If Km increases, the paramater values ______. The intercept _____ and moves ______ the origin.

A

If Km increases, the paramater values doubles. The intercept increases (becomes less negative) and moves towards the origin.

65
Q

Suicide inhibitor:

A

A substrate analogue that binds irreversibly to the active site via a covalent bond.

66
Q

homotrophic effector

A

An allosteric regulator that is also the substrate.

67
Q
A

uncompetitive inhibition

68
Q

in noncompetitive inhibition, Vmax…

A

decreases

69
Q

phosphatase, peptidase, nuclease, lipase = all are ____ enzymes

A

hydrolases

70
Q

methyltransferase is an example of a _____ enzyme

A

transferase

71
Q

where is the binding site in uncompetitive inhibition

A

enzyme-substrate complex

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