protein function 1 Flashcards

1
Q

what are enzymes?

A

they are biological catalysts that speed up chemical reaction.

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2
Q

what are cofactors?

A

they are basically required for enzymes catalyse, speed up the chemical reaction.

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3
Q

what is lock-key model?

A

this is when the active site has to be the same shape as the substrate to fit in as in this model the substrate fits in the active site perfectly with having to make any major atomic rearrangements.

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4
Q

what is the induced fit model?

A

This is when the substrate presents with a conformational change so that the substrate can fit and then the substrate fits well after the reshape.

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5
Q

what is an activation energy?

A

it is the minimum energy needed to start a chemical reaction.

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6
Q

what are the optimal conditions

A

temperature
PH
ionic strength
substrate concentration

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7
Q

what are the 4 types of catalysis?

A

acid-base
covalent
metal ion
approximation

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8
Q

what are cofactors?

A

molecules that aid enzyme function

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9
Q

what is an acid-base catalysis?

A

it is a enzyme that acts a a partial proton donor or acceptor

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10
Q

what is an example of acid-base catalyst?

A

motor protein-ATPase

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11
Q

what is an covalent catalysis?

A

it is when the active site is temporarily covalently modified

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12
Q

what is the example of a covalent catalysis?

A

chymotrypsin

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13
Q

what does a metal-ion catalysis do?

A

stabilise the negative charge

generate a nucleophile- this increases the acidity of the nearby molecule

allows the metal ion to bind to the substrate.

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14
Q

what is an example of a metal-ion catalysis?

A

carbonic anhydrase

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15
Q

what does approximation catalysis do?

A

bring two substrates together.

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16
Q

what is an example of a approximation catalysis?

A

nucleoside-monophosphate (NMP) kinase

17
Q

what are coenzyme?

A

small organic cofactors

18
Q

what are the examples of coenzymes?

A

prosthetic groups

cosubstrates

19
Q

what are prosthetic groups?

A

they are tightly bound coenzymes

20
Q

what are cosubstartes?

A

they are loosely associated coenzymes

21
Q

what happens in the downward shift in ES curve?

A

decreases Vmax

22
Q

what happens in the upward shift in ES curve?

A

increases Vmax

23
Q

What happens in the right shift in curve?

A

increases Km - lower binding

24
Q

what happens in the left shift curve?

A

decreases Km - higher binding.

25
Q

what does Vmax depend on?

A

the concentration of the enzyme.

26
Q

what does the glucokinase do in relation to michalis mention kinetics?

A

high Vmax

high Km

responds to large glucose.

27
Q

what does the hexokinase do in relation to michalis mention kinetics?

A

lower Vmax

lower Km

not specific too glucose.

28
Q

what is happens in the rate-limiting step?

A

it is the slowest step meaning that it takes time to reach to the end of the path and complete its duties

it has the highest activation energy

this pathway is limited by S

29
Q

what is the committed step?

A

it is the first irreversible enzymatic reaction that is specific to a product.

30
Q
A
31
Q

what happens in the competitive?

A

Vmax remains the same

Km increases so more S is needed

slope is steeper

32
Q

what happens in the uncompetitive?

A

Vmax is lower

Km is lower

they is no change in the slope.

33
Q

what happens in the non-competitive?

A

the Vmax is lower

Km remains the same

the slope is steeper

34
Q

what does allosteric protein contain?

A

distinct regulatory sites

multiple functional sites

35
Q

what are the examples of allosteric regulation?

A

haemoglobin tetramer
ATcase

36
Q

what are zymogens and proenzymes

A

they are enzymes that need activating by another enzyme in order to function.