Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

module 2 > 2.1.4 - enzymes💯 > Flashcards

2.1.4 - enzymes💯 Flashcards

1
Q

enzymes

A

proteins that act as biological catalysts, without the need of harsh conditions

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

anabolic reactions

A

synthesis of larger molecules from smaller ones
chemical reactions required for growth

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

catabolic reactions

A

break down large chemicals and release energy

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

metabolism

A

all of the chemical reactions that take place within an organism

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

vmax

A

maximum initial velocity of an enzyme catalysed reaction

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

activation energy

A

the minimum amount of energy required to start a chemical reaction

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

enzymes and activation energy

A

enzymes lowe the activation energy

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

enzymes and collisions

A

enzymes increase the rate of successful collisions and overall rate of reaction

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

active site

A

part of enzyme where the chemical reaction happens

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

lock and key theory

A

enzymes active site (lock) us already in appropriate conformation for the substrate to bind. the substrate easily fits into the active site, and no alteration is needed

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

enzyme substrate complex

A

when the substrate collides with the active site

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

enzyme product complex

A

when the substrate reacts and the products are formed

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

induced fit hypothesis

A

theory that states that after partial binding of the substrate to an enzyme, alters the structure of the enzyme so that the active site becomes complementary.

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

intracellular enzymes

A

enzymes that function within cells

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

example of intracellular enzymes

A

catalase - catalyses the breakdown of hydrogen peroxide into water and oxygen

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

extracellular enzymes

A

enzymes that are synthesised and secreted to work outside the cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

example of extracellular enzymes

A

single celled organisms rely on these to make use of polymers for nutrition
bacteria and yeast release enzyjmes to break down large molecules lile proteins
digestion - amylase and trypsin.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

digestion of starch

A
  1. starch polymers are partially broken down into maltose, where amylase is produced.
  2. maltose is broken down into glucose where maltase is present
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

digestion of proteins

A

trypsin - catalyses the digestion of proteins into smaller peptides, which can then be broken down further. found in the pancreas.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

factors that affect enzyme activity

A

pH, temp, concentration of enzyme or substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

effect of temperature on enzyme activity

A

increasing temp of a reaction environment increases kinetic energy of the particles, leading to more successful collisions, so more ESCs made, increasing rate of reaction

22
Q

temperature coefficient

A

measure of how much the rate of reaction increases with a 10C rise in temperature - normally taken as 2

23
Q

denatured

A

loss of an enzymes normal shape so that it no longer functions as the bonds break due to vibrations. happens in the wrong conditions

24
Q

optimum temperature for ennzymes

A

temp where the enzyme has the highest rate of activity
- human - 37C
- thermophillic bacteria 70C
- psychrophilic organisms 5C

25
Q

pH and hydrogen ion concentration

A

a change in pH refers to a change in hydrogen ion concentration
more H ions - low pH
less H ions - high pH

26
Q

renaturation

A

regaining the correct tertiary structure after dentauration of the protein

27
Q

effect of H ions on R groups

A

more H ions present, the less R groups will be able to interact with eachother

28
Q

effect of increasing substrate concentration

A

increasing the number of substrate particles means a higher collision rate with the active site of enzymes and the formation of more enzyme substrate compleces - so the rate increases

29
Q

only way to increase rate of reaction at Vmax of substrate concentration

A

add more enzymes

30
Q

effect of increasing enzyme concentration

A

increasing the number of available active sites in a particular area or volume, leading to more ESCs

31
Q

inhibitor

A

molcules that prevent enzymes from carrying out their normal function of catalysis

32
Q

two types of enzyme inhibition

A

competitive and non competitive

33
Q

how competitive inhibitors work

A
  • molecule that has a similar shape to the substrate of an enzyme can fit into the active site of the enzyme
  • blocks substrate from active site, preventing the enzyme from catalysing the reaction
  • enzyme cannot carry out iys function
34
Q

reversible inhibitors

A

bind temporarily to the active site of the enzyme

35
Q

competitive inhibitors effect rate on reaction

A

reduce the rate of reaction but does not chage the Vmax - if enough substration concentration then there will be more substrates than the inhibitors, reaching the Vmax

36
Q

examples of competitive inhibitors

A

statins - stop cholesterol from being produced
aspirin - prevents the synthesis of prostaglandins

37
Q

non competitive inhibitor

A
  • inhibitor binds to the allosteric site, not the active site
  • causes the tertiary strucure to change, meaning the substrate is no longer complementary
  • enzyme cannot carry out function
38
Q

effect of a non competitive inhibitor

A

reduces the rate of reaction - adding more substrate will not overcome the effect.

39
Q

examples of non competitive inhibitors

A

organophosphates and proton pump inhibitors

40
Q

end product inhibition

A

the product of a reaction inhibits the enzyme required for the reaction

41
Q

examples of end product inhibition

A

glucose – (phosphofructokinase) –> ATP
- when ATP levels are too high more ATP binds to the allosteric site on PFK, preventing the productuon of more ATP

42
Q

cofactor

A

non protein enzyme helpers

43
Q

how cofactors are obrained

A

via diet as minerals - iron calcium chloride and zinc ions

44
Q

example of cofactor

A

amylase contains an inorganic cofactor (cl ion) which enables formation of the active site for the substrate starch

45
Q

coenzyme

A

organic co factor

46
Q

prosthetic group

A

cofactor that binds tightly to an enzyme and forms a permanent feature of that protei.

47
Q

example of a prosthetic group

A

Zn2+ for carbonic anhydrase

48
Q

precursor activation

A

inactive form of the enzyme due to the fact that they can cause damage to the body when active. undergo a change un shape to the active site to be activated

49
Q

apoenzyme

A

before the cofactor is added

50
Q

holoenzyme

A

apoenzyme + holoenzyme

51
Q

example of precursor activation

A

inactive pepsinogen released into the stomach to digest proteins activated by food acid pH then transforms into enzyme pepsin

module 2 (6 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions