Enzymes Flashcards

1
Q

Definition of an enzyme

A

Globular protein with a specific tertiary structure which acts as a biological catalyst and increases the reaction rate by lowering the activation energy

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2
Q

what is a catalyst?

A

speeds up reactions remains unchanged at the end

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3
Q

what happens to almost all reactions in living organisms?

A

they are catalysed by enzymes

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4
Q

a purpose of anabolic reaction?

A

to build complex molecules from simple ones

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5
Q

what is an intra cellular enzyme?

A

enzyme that act inside cells e.g. hydrolases in lysosomes

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6
Q

what is an extra cellular enzyme?

A

enzyme that acts outside of a cell e.g. digestive enzyme

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7
Q

how are enzymes named?

A

end in ase sometimes sin - derived from the substrate

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8
Q

what does lactase catalyse?

A

the break down of lactose into glucose and galactose

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9
Q

what enzyme catalyses creating glycogen?

A

Glycogensynthetase

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10
Q

what are globular proteins made of?

A

amino acids

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11
Q

what is the structure of a globular protein?

A

3D

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12
Q

what is a globular protein soluble in?

A

water

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13
Q

how does a globular protein hold its 3D structure?

A

hydrophilic r groups on the outside and hydrophobic r groups on the inside

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14
Q

what is an active site?

A

depression on the surface of an enzyme to which a specific substrate binds

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15
Q

what is unique about the active site?

A

it is complementary

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16
Q

in Lock and Key how does the substrate bond?

A

its held in active site by temporary bonds between r groups

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17
Q

what does the substrate form in lock and key?

A

enzyme substrate complex

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18
Q

what is the substrate converted to in lock and key?

A

the product enzyme product complex

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19
Q

what happens to the product in lock and key?

A

r groups don’t interact product and substrate is released

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20
Q

what happens to the enzyme at the end of lock and key?

A

it remains unchanged

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21
Q

what is different about induced fit?

A

active site is not complementary

22
Q

how does the substrate bind in induced fit?

A

it collides and the enzyme slightly changes to fit

23
Q

how is the substrate held? (induced fit)

A

oppositely charged groups (ESC)

24
Q

what do the oppositely charged groups do?

A

put strain on the substrate increase reaction rate

25
what forms in active site? (induced fit)
product is formed and is released due to it having a different shape
26
what do enzymes do to a reaction?
lower activation energy speed up reaction rate hold the substrate in a way to speed up reaction
27
what do enzyme reactions end with?
product formed or substrate conversion
28
how is product of an enzyme reaction measured?
oxygen can be measured using a gas syringe
29
how is substrate conversion measured? starch into maltose?
add iodine follow loss of blue colour with colourimeter
30
how does enzyme conc affect the reaction?
increases rate of reaction until no enzymes left
31
why does enzyme conc increase reaction rate?
increases the number of active sites more products can be formed increase reaction rate until all sites are filled
32
how does excess enzyme and substrate affect the reaction?
enzyme conc increases so does reaction rate its directly proportional
33
why does excess enzyme and substrate affect reaction?
enzyme conc increases active site number more products are formed reaction rate increases
34
how does substrate conc affect reaction rate?
substrate conc increases rate until substrate has no further effect
35
why does substrate conc affect rate?
collisions between substrate and enzyme increases more products form rate increases. more substrate has no effect enzymes are at V MAX
36
how does temp effect reaction rate?
temp increases reaction rate this happens gradually optimum temp is reached past this reaction rate decreases
37
why does temp effect reaction rate?
temp increases so does kinetic energy more collisions occur. more ESC is formed. optimum temp where collision are at their highest.
38
what happens past optimum temp?
enzyme vibrate until tertiary structure breaks enzymes are denatured site is no longer complementary rate decreases
39
how does pH affect reaction rate?
pH increases reaction rate does also until optimum pH past this reaction rate decreases.
40
what is pH a measure of ?
number of H+ ions
41
what do H+ ions do to hydrogen bonds?
they interfere with hydrogen bonds, ionic bonds and r groups of some amino acids.
42
how does pH affect the enzyme?
it can alter the tertiary structure changing the active site therefore ESC cant form rate decreases
43
what do inhibitors do?
reduce rate or stop enzyme catalysed reactions
44
how do competitive inhibitors work?
have a similar shape compete for the active site. occupy the site stop ESC formation reduce reaction rate
45
what will increasing the substrate conc do to the competitive inhibitor?
reduce its effectiveness more likely a substrate will bond
46
where do non competitive inhibitors bind?
allosteric site
47
how are non competitive different to competitive?
they do no compete they alter the active site so substrate cant bond increasing substrate has no effect
48
what is end product inhibition?
end product binds to enzyme away from the active site and alters the shape of the active site initial substrate cant bond
49
what is end product inhibition similar to?
reversible non competitive inhibition
50
what are inborn errors of metabolism?
if the DNA within a enzyme is mutated enzyme may not function
51
what are diseases caused by a disfunctioning enzyme in a metabolic sequence called?
in born errors of metabolism