Enzymes 1,2 and 3 Flashcards

1
Q

what happens inside the ATP synthase

A

the middle and lower parts rotate

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2
Q

how does the middle and lower part of ATP synthase rotate

A

this happens when protons are flowing back into the mitochondria

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3
Q

what does the top part of ATP synthase do

A

merge ATP and phosphate

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4
Q

what is a cofactor

A

a non-protein component that is required to help the enzyme to do its job

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5
Q

examples of some cofactors

A

K+, Mg2+ and Fe2+/Fe3+

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6
Q

what are coenzymes

A

complex organic molecules, usually produced from a vitamin

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7
Q

examples of coenzymes

A

FAD, NAD+ and Coenzyme A

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8
Q

what is a prosthetic group

A

cofactor covalently bound to the enzyme or very tightly associated with the enzyme

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9
Q

what is an apoenzyme

A

the protein component of an enzyme that contains a cofactor

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10
Q

what is a holoenzyme

A

“whole enzyme” - the apoenzyme plus the cofactor(s)

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11
Q

what is a substrate

A

molecule acted on by the enzyme

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12
Q

what is an active site

A

the very point the reaction takes place

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13
Q

what are the 6 types of class names for enzymes

A

oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases

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14
Q

what type of reaction does oxidoreductase involve

A

transfer e-

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15
Q

what type of reaction does transferase involve

A

group transfers

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16
Q

what type of reaction does hydrolase involve

A

hydrolysis (transfer chemical groups to water)

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17
Q

what type of reaction does lyases involve

A

form or add groups to double bonds

18
Q
A
19
Q

what is “useful” energy called

A

Gibs Free Energy (G)

19
Q

what type of reaction does ligase involve

A

formation of C-C, C-S, C-N or C-O bonds

19
Q

what type of reaction does isomerase involve

A

transfer groups within molecules (form isomer..)

20
Q

what is the energy barrier

A

the energy that is require to get to transition sate from ground state (S)

21
Q

a spontaneous reaction must have a (delta)G value of…

A

negative value (-)

22
Q

what are the 3 ways that enzymes reduce activation energy

A

entropy, desolvation and induced fit

23
Q

what types of techniques can you use to understand enzyme function

A

enzyme kinetics, mutagenesis (the ability to change individual amino acids and see how it affects the properties of the enzyme) and 3D structure

24
Q

what happens to initial rate of reaction if there is more substrate

A

there is a higher initial rate of reaction

25
Q

what can the Vmax tell us

A

it can tell us how fast a reaction is proceeding when the enzyme is saturated with substrate

26
Q

if there is two or more substrates, how do they react to the enzyme

A

random order or ordered with a ternary complex, and no ternary complex formation, order/random sequential mechanism, double displacement

27
Q

what is a ternary complex

A

a protein complex containing three different molecules that are bound together

28
Q

what do allosteric enzymes do

A

have no reaction speed at the very beginning of the [S]

29
Q

what does vmax indicate

A

how fast a reaction is proceeding when the enzyme is saturated with substrate

30
Q

what does Km depict

A

the stability of the enzyme-substrate complex (affinity)

31
Q

what does low and high Km mean

A

low Km has high substrate affinity and gets to Vmax faster
high Km is the opposite

32
Q

what is the rate limiting factor of the Michealis-Menten equation

A

the ES–>EP

33
Q

what are catalytic antibodies

A

antibodies that generated specific to a transition state molecule

34
Q

how does an inhibitor irreversibly bond to an inhibitor

A

binds to enzyme covalently and thus irreversibly

35
Q

what does the plateau demonstrates in the Michealis-Menten curve

A

demonstrates zero order kinetics

36
Q

what does the plateau on Michealis-Menten curve indicate

A

the systems or enzyme is saturated with substrate

37
Q

where is glucokinase found and what is their relation with Km and Vmax

A

mainly found in the liver and has high Km and Vmax

38
Q

where is hexokinase found and what is their relation with Km and Vmax

A

is found everywhere and has low Km and Vmax

39
Q

what happens when blood glucose goes up after a meal

A

glucokinase activity increases

40
Q

describe competitive inhibition binding and how it would appear on a michealis-meten plot

A

reaches Vmax but increases Km resulting in a right shift compared to normal binding