Enzymes Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

give an example of an extracellular enzyme

A

amylase, secreted by mouth cells and catalyses hydrolysis of starch

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

give an example of an intracellular enzyme

A

catalyses, breaks down hydrogen peroxide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

what type of proteins are enzymes

A

globular

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

what is the active site

A

the part of the enzyme where the substrate molecules bind

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

the active site shape is determined by what

A

tertiary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

what is it called when a substrate binds to an active site

A

enzyme-substrate complex

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

how do enzymes speed up reactions

A

reduce the activation energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

what are the two reasons for why the formation of an enzyme-substrate complex lowers activation energy

A

-if two substrates need to be joined, attaching to the enzyme holds them close together so there is less repulsion and can bond more easily
- in a breakdown reaction, fitting into the active site puts a strain on bonds in the substrate so it can break down more easily

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

describe the lock and key model

A

the idea that the substrate fits into the enzyme as they have the exact complementary shape

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

describe the induced fit model

A

the substrate has to have the right shape to bind to the active site but also has to change the shape of the active site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

how does temperature affect enzyme activity

A

if temperature is too high, molecules vibrate more causing to break bonds that hold enzyme shape and the active site will change shape and become denatured
if temperature is too low then the number of successful collisions will reduce due to lack of kinetic energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

what is the temperature at which the rate of an enzyme controlled reaction is at its fastest

A

optimum temperature

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

what is the equation for temperature coefficient

A

Q10= R2 (rate at higher temperature)/ R1 (rate at lower temperature

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

How does pH affect enzyme activity

A

the H+ ions and OH- ions produced above and below optimum pH, can break the ionic bonds in the tertiary structure, causing Mayme to denature

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

what enzyme works best at pH two and is found in stomach

A

pepsin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

how does enzyme conc affect enzyme activity

A

the more enzyme molecules in a solution the more likely there is for a collision to occur with a substrate molecule
however if substrate is limited there comes a point where adding further enzyme has no further affect

17
Q

what is the effect of substrate conc on enzyme activity

A

the higher the substrate conc, the faster the reaction, more likely for collisions to occur, only true up to a saturation point where enzyme conc becomes the limiting factor
substrate conc also decreases over tike during a reaction so if no other substrate is added then the speed of reaction will also decrease over time

18
Q

what is a cofactor

A

a non protein substance that binds to an enzyme to help it function

19
Q

what is an inorganic cofactor

A

help substrate and enzyme bind but don’t participate directly so aren’t used up or changed in any way

20
Q

what are organic cofactors called and how do they aid enzyme function

A

coenzymes, participate in reaction and often act as carriers by moving chemical groups between different enzymes

21
Q

what are competitive inhibitors

A

molecules that have the same shape as substrate molecules, block active site so substrate cannot bind, high conc of inhibitor means most active sits will be take up, however if there is a higher conc of substrate than the chance of it reaching an active site before the inhibitor is high

22
Q

what are non-competitive inhibitors

A

bind to enzyme away from the active site and to the allosteric site, changing active site shape so substrate molecules can no longer bind

23
Q

what type of drugs act as enzyme inhibitors

A

antiviral drugs, prevent replication of DNA
antibiotics

24
Q

what metabolic potions act as enzyme inhibitors

A

cyanide- non competitive, irreversible
malonate- competitive
arsenic- non competitive

25
Q

what is a prosthetic group and give an example

A

a cofactor tightly bound to an enzyme- Zn2+ for carbonic anhydrase

26
Q

what nutrition group is often a source of coenzymes

A

vitamins

27
Q

what is the cofactor for amylase

A

chloride ion

28
Q

what is end product inhibitor and what do they regulate

A

metabolic pathways are regulated by end-product inhibition, a metabolic pathway isa series of metabolic reactions, the product of the first takes part in the second reaction and so on, each reaction uses a different enzyme, many enzymes are inhibited by the product of the reaction they catalyse, the final product in the metabolic pathway inhibits an enzyme that acts easier on in the pathway