enzymes Flashcards

1
Q

enzymes

A

most are proteins. all are catalysts. not used up in reactions. highly specific. accelerate reactions

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2
Q

what are the 6 enzyme classes?

A

oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases

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3
Q

oxidoreductases

A

oxidation-reduction reactions

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4
Q

transferases

A

group transfer reactions

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5
Q

hydrolases

A

hydrolysis reactions

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6
Q

lyases

A

addition or removal of groups to form double bonds

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7
Q

isomerases

A

isomerization ( intramolecular group transfer)

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8
Q

ligases

A

ligation of two substrates at the expense of ATP hydrolysis

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9
Q

holoenzyme

A

the active enzyme with its non-protein component

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10
Q

apoenzyme

A

the enzyme without its non-protein moiety and is inactive

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11
Q

cofactor

A

non-protein moiety that is a metal ion (minerals)

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12
Q

coenzyme

A

small organic molecules (vitamins)

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13
Q

what do enzymes alter?

A

reaction speed

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14
Q

lock and key model

A

enzyme’s tertiary structure consists of a unique pocket or site which is tailor made to fit only its substrate

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15
Q

induced fit model

A

as enzymes interact with substrates they change their conformation so that the enzyme is snug around the substrate

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16
Q

factors affecting reaction rates

A

temperature, pH, enzyme concentration, and substrate concentration

17
Q

Vo

A

initial velocity of reaction

18
Q

[S]

A

concentration of substrate

19
Q

Vmax

A

the theoretical maximal rate of the reaction

20
Q

Km

A

substrate at which the reaction velocity is equal to 1/2 Vmax

21
Q

inhibitor

A

any substance that can diminish the velocity of an enzyme-catalyzed reaction

22
Q

irreversible inhibitors

A

bind to enzymes through covalent bonds

23
Q

reversible inhibitors

A

bind to enzymes through noncovalent bonds

24
Q

competitive inhibition

A

inhibitor binds reversibly to the same site as substrate

25
Q

noncompetitive inhibition

A

inhibitor binds to different sites than enzymes

26
Q

allosteric enzymes

A

have multiple subunits. can either inhibit or increase enzyme activity

27
Q

homotropic effectors

A

substrate serves as effector, enhancing other substrate-binding sites. binding to one site “helps” other sites

28
Q

heterotropic effectors

A

effector different from substrate, effector may be the product, + feeds back to cause inhibition

29
Q

homotropic positive

A

lots of A activates E1

30
Q

heterotropic positive

A

lots of A activates E3

31
Q

homotropic negative

A

lots of B inhibits E1

32
Q

heterotropic negative

A

lots of A inhibits E3

33
Q

Michaelis-Menten non-competitive

A

covalent, irreversible. decreases Vmax

34
Q

Michaelis-Menten competitive

A

non-covalent, reversible. increases substrate and Km