topic 1 - factors affecting enzyme activity Flashcards

cgp (topic 1A) 12 -13

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1
Q

what are four factors that affect enzyme activity

A

temperature, pH, enzyme concentration, substrate concentration

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2
Q

why does the rate of an enzyme controlled reaction increase when the temperature increases

A

when heat is increased, kinetic energy is also increased so molecules move faster - making enzymes more likely to collide with the substrate molecules - the energy of these collisions also increases meaning each collision is more likely to result in a reaction

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3
Q

what happens to the enzyme’s molecules when the temperature rises

A

they vibrate more

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4
Q

what happens when the temperature goes above a certain level

A

the vibration of the enzyme’s molecules breaks some of the bonds that hold the enzyme in shape - therefore the active site changes and the enzymes and substrate no longer fit together

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5
Q

what does denatured mean

A

a protein that has lost its tertiary structure /its tertiary structure has been modified - it no longer functions as a catalyst

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6
Q

what is the normal shape of a protein called

A

native conformation

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7
Q

what is the reversal of denaturation called

A

renaturation

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8
Q

what are human enzymes optimum temperature

A

around 37 C

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9
Q

what are human enzymes optimum pH value

A

pH 7

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10
Q

what is pepsins optimum pH value

A

pH 2

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11
Q

what happens if the pH value is above or below the optimum

A

the H+ and OH- ions found in acids and alkalis can mess up the ionic bonds and hydrogen bonds that hold the enzyme’s tertiary structure in place - making the active site change shape so the enzyme is denatured

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12
Q

why does an increased enzyme concentration increase the rate of reaction

A

the more enzyme molecules there are in a solution, the more likely a substrate molecule is to collide with one and form an enzyme substrate complex - therefore increased concentration of enzyme increases the rate of reaction

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13
Q

when does adding more enzymes have no further effect

A

when there’s more than enough enzyme molecules to deal with all the available substrate - if the amount of substrate is limited

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14
Q

why does an increased saturation concentration increase the rate of reaction

A

the higher the substrate concentration, the faster the reaction - more substrate molecules means a collision between substrate and enzyme is more likely and so more active sites will be used

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15
Q

why does substrate concentration only affect the rate of reaction up to a point

A

eventually there are so many substrate molecules that all the active sites are full - so adding more makes no difference

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16
Q

what is the saturation point in enzymes

A

when all enzymes are occupied and are not searching for substrates

17
Q

why is the initial rate of reaction the highest rate of reaction

A

because substrate concentration decreases with time during a reaction so if no other variables are changed the rate of reaction will decrease over time too

18
Q

what can enzyme activity be prevented by

A

enzyme inhibitors

19
Q

what are enzyme inhibitors

A

molecules that bind to the enzyme that they inhibit

20
Q

what are the two types of inhibition

A

competitive inhibition and non competitive inhibition

21
Q

what do competitive inhibitor molecules have a similar shape to

A

substrate molecules

22
Q

what do competitive inhibitors compete with and what for

A

the substrate molecules to bind to the active site but no reaction takes place as they block the active site so no substrate molecules can fit in it

23
Q

what does how much the enzyme is inhibited depends on

A

the relative concentrations of the inhibitor and the substrate

24
Q

what happens if there’s a high concentration of the inhibitor

A

it will take up nearly all the active sites and hardly any of the substrate will get to the enzyme

25
Q

what happens if there’s a high concentration of the substrate

A

the substrate’s chances of getting to an active site before the inhibitor increase - so increasing the concentration of substrate will increase the rate of reaction

26
Q

what do non competitive inhibitor molecules bond to

A

the allosteric site

27
Q

what does the non competitive inhibitor do

A

it causes the active site to change shape so the substrate molecules can no longer bind to it

28
Q

why don’t non competitive inhibitors compete with the substrate molecules

A

because they are a different shape

29
Q
A