enzymes Flashcards

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

What are enzymes?

A

Biological catalysts that interact with
substrate molecules to facilitate
chemical reactions. Usually globular
proteins

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

Why are enzymes

important?

A
The allow reactions to happen 
quickly without extreme conditions 
(e.g. high temperatures and 
pressures) that are not possible in 
living cells because they would 
damage the cell components
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is a substrate?

A

A substance used, or acted on, by
another process or substance, e.g. a
reactant in an enzyme-catalysed
reaction

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

What is anabolism?

A
Anabolic reactions of metabolism 
that construct molecules from 
smaller units. These reactions 
require energy from the hydrolysis of 
ATP, and are catalysed by enzymes
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is catabolism?

A
Catabolic reactions of metabolism 
that break molecules down into 
smaller units. These reactions 
release energy, and are catalysed by 
enzymes
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What is metabolism?

A

The sum of all of the different
reactions and reaction pathways
happening in a cell or organism

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

What is meant by ‘Vmax’?

A

Maximum initial velocity or rate of an

enzyme-catalysed reaction

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

Describe the mechanism of

enzyme action

A

Enzymes help the molecules collide
successfully, and therefore reduce
the activation energy required

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

What is the active site of an

enzyme?

A
An area within the tertiary structure 
of the enzyme that has a shape that 
is complementary to the shape of a 
specific substrate molecule. This 
allows the enzyme to bind to a 
substrate with specificity
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is the ‘Lock and Key
Hypothesis’ of enzyme
action?

A
In the same way that only the right 
key will fit into a lock, only a specific 
substrate will ‘fit’ the active site of 
an enzyme
Enzyme + Substrate —> ESC —> 
Enzymes + Products
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

How does the enzyme act
on the substrate in the Lock
and Key Hypothesis?

A
• The substrate and enzyme 
molecules each have KE and are 
constantly moving randomly 
• If a substrate molecule 
successfully collides with an 
enzyme molecule, an ESC forms
• The substrate is held in such a 
way by the enzyme that the right 
atom-groups are close enough to 
react
• The R-groups within the active site 
of the enzyme will also interact 
with the substrate forming 
temporary bonds 
• These put strain on the bonds 
within the substrate, which also 
helps the reaction along 
• The substrate is converted into the 
product, an EPC formed, and then 
the products leave the enzyme
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is the ‘Induced Fit

Hypothesis’?

A

Modified lock and key explanation
for enzyme action: the active site of
the enzyme is modified in shape by
binding to the substrate

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

How does the enzyme act
on the substrate in the
Induced Fit Hypothesis?

A
• The active site of the enzyme 
changes shape slightly as the 
substrate enters to fit it better 
• An ESC is formed, and noncovalent R-group interactions (e.g. 
hydrogen bonds, ionic attractions, 
van Der Waals forces and 
hydrophobic interactions) bind the 
substrate molecule to the 
enzyme’s active site
• This can weaken bonds in the 
substrate, lowering the activation 
energy for the reaction 
• The substrate is converted into the 
product forming an EPC
• As the product molecules have a 
slightly different shape from the 
substrate molecule, they detach 
from the active site
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What are intracellular

enzymes? (Give an example)

A
Enzymes that act within cells 
• Hydrogen peroxide is a toxic 
product of many metabolic 
pathways 
• Enzyme catalase break it down 
into O2 and H2O quickly, 
preventing its accumulation
• Found in both animal and plant 
tissues
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What are extracellular

enzymes?

A
Enzymes that act outside the cell 
that made them (in some organisms 
e.g. fungi, they work outside the 
body)
• The substrates for intracellular 
enzymes (e.g. nutrients) are large 
molecules that can’t enter the cell 
directly though the cell membrane 
• Extracellular enzymes are released 
from cells to break down the large 
nutrient molecules into smaller 
molecules in the process of 
digestion
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Describe the process of the

digestion of starch

A
1. Starch polymers are broken 
down into maltose (disaccharide) 
by amylase which is produced 
by the salivary glands and the 
pancreas. It’s released in saliva 
into the mouth, and in pancreatic 
juice into the small intestine 
2. Maltose is broken down into 
glucose (monosaccharide) by 
maltase in the small intestine
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Describe the process of the

digestion of proteins

A
Trypsin is a protease that 
catalyses the digestion of proteins 
into smaller peptides which can be 
broken further into amino acids by 
other proteases 
• It’s produced in the pancreas and 
released with the pancreatic juice 
into the small intestine, where it 
acts on proteins
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Why does increasing the
temperature initial increase
the rate of reaction?

A
If a reactant mixture containing 
enzyme and substrate molecules is 
heated:
• Both types of molecule will gain 
KE and move faster
• This will increase the rate of 
successful collision 
• The rate of formation of ESCs 
increases and the rate of reaction 
increases, increasing the number 
of EPCs per second, up to a point
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What is a enzyme’s optimum

temperature?

A
The temperature at which the 
enzyme has the highest rate of 
activity 
• Around 40˚C in humans 
• 70˚C for thermophilic bacteria 
• Below 5˚C for psychrophilic 
organisms
20
Q

What does denaturation

mean?

A

Change in the tertiary structure of a
protein or enzyme, resulting in loss
of normal function

21
Q

What happens when the
temperature is increased
past the optimum?

A
Increasing temperature makes 
molecules vibrate 
• This may break some of the weak 
bonds (e.g. hydrogen and ionic 
bonds) that hold the tertiary 
structure of the enzyme’s active 
site 
• As the active site shape begins to 
change, the substrate won’t fit in 
so well, and the rate of reaction 
begins to decrease
• As more heat is applied, the active 
site completely and irreversibly 
changes so that it is no longer 
complementary to the substrate
• The reaction can’t proceed at all
• The enzyme is denatures 
• (primary structure is not altered as 
heat doesn’t break peptide bonds)
22
Q

What is the temperature

coefficient, Q10?

A
A measure of how much the rate of 
reaction increases with a 10˚C 
temperature increase.
Usually taken as 2 for enzymecontrolled reactions i.e rate of 
reaction doubles with 10˚C increase
23
Q

Why does pH affect

enzymes?

A
• A change in pH refers to a change 
in hydrogen ion concentration
• Active site is only the right shape 
at a certain hydrogen ion 
concentration
• Hydrogen bonds and ionic bonds 
between amino acid R-groups 
hold proteins in their precise 3D 
shapes 
• Hydrogen ions interact with polar 
and charged R-groups, affecting 
the interaction of the R-groups 
with each other
• The more hydrogen ions present 
(low pH) the less R-groups can 
interact with each other leading to 
bonds breaking and the shape of 
the enzyme changing. The reverse 
is true when less hydrogen ions 
present (high pH)
• Shape of enzyme will change, so it 
can only function within a narrow 
pH range
24
Q

Why do enzymes only work

within a narrow pH range?

A
Small changes of pH either side of 
the optimum slow ROR because 
the shape of the active site is 
disrupted
• If normal optimum pH is restored, 
the hydrogen bonds can reformat 
the active site’s shape is restored
• At extremes of pH, the active site 
may be permanently changed; the 
enzyme is denatured
25
Q

What happens when the
concentration of substrate
is increased?

A
• Higher collision rate, so the rate of 
reaction increases 
• Leads to the formation of ESCs at 
a faster rate
• The rate of reaction increases up 
to its maximum (Vmax) - at this 
point all of the active sites are 
occupied and no more ESCs can 
be formed until products are 
released from active sites
• The only way to increase the ROR 
would be to add more enzyme or 
increase the temperature 
• If the concentration of enzyme is 
increased, more active sites are 
available so the ROR can rise 
towards a higher Vmax.
26
Q

What is an inhibitor?

A
A factor that prevents or reduces the 
rate of an enzyme-catalysed 
reaction. 
There are 2 types: competitive and 
non-non-competitive
27
Q

What is a competitive

inhibitor?

A

An inhibitor that competes with
substrate to bind to active site on an
enzyme

28
Q

How does competitive

inhibition work?

A
1. A molecule or part of a molecule 
that has a similar shape to the 
substrate of an enzyme can fit 
into the active site of the enzyme 
2. This blocks the substrate from 
entering the active site, 
preventing the enzyme from 
catalysing the reaction 
3. The enzyme cannot carry out its 
function and is said to inhibited
29
Q

What is the effect of

competitive inhibition?

A
• Substrate and inhibitor molecules 
present in a solution will compete 
with each other to bind to the 
active sites of the enzymes 
catalysing the reaction
• The rescues the number of 
substrate molecules binding to 
active sites in a given time and 
slows down the rate of reaction 
• Degree of inhibition will depend on 
the relative concentrations of 
substrate, inhibitor, and enzyme
• Most competitive inhibitors only 
bind temporarily to the active site
30
Q

What is the effect of a
competitive inhibitor on rate
of reaction?

A
• Reduces the rate of reaction for a 
given concentration of substrate
• Doesn’t change the Vmax of the 
enzyme 
• If substrate concentration is 
increased, there will be so much 
more substrate than the inhibitor 
that the original Vmax can still be 
reached
31
Q

Give 2 examples of

competitive inhibitiors

A
Statins
• Competitive inhibitors of an 
enzyme used in cholesterol 
synthesis
• Prescribed to help people reduce 
blood cholesterol concentration
• High blood cholesterol levels can 
result in heart disease
Aspirin 
• Irreversibly inhibits the active site 
of COX enzymes, preventing the 
synthesis of prostaglandins and 
thromboxane, the chemicals 
responsible for producing pain and 
fever
32
Q

What is a non-competitive

inhibitor?

A

A inhibitor that binds to an enzyme

at an allosteric site

33
Q

How does non-competitive

inhibition work?

A
• Inhibitor binds to the enzyme at a 
location other than the active site. 
This alternative sites called an 
allosteric site
• Binding of the inhibitor causes the 
tertiary structure of the enzyme to 
change, meaning the active site 
changes shape
• Active site no longer has 
complementary shape to 
substrate, so its is unable to bind 
to the enzyme
• Enzyme cannot carry out its 
function and is said to be inhibited
34
Q

What is the effect of a noncompetitive inhibitor on rate

of reaction?

A
• Increasing concentration of 
enzyme or substrate will not 
overcome the effect of a noncompetitive inhibitor
• Increasing the concentration of 
inhibitor will decrease rate of 
reaction further as more active 
sites become unavailable 
• Lower Vmax
35
Q

Give examples of
irreversible non-competitive
inhibitors

A
Organophosphates
• Used as insecticides and 
herbicides
• Irreversibly inhibit the enzyme 
acetyl cholinesterase (necessary 
for nerve impulse transmission)
• Can lead to muscle cramps, 
paralysis and death if ingested 
Protein Pump Inhibitors (PPI)
• Used to treat long-term indigestion 
• Irreversibly block an enzyme 
system responsible for secreting 
hydrogen ions into the stomach 
• Makes PPIs very effective in 
reducing the production of excess 
acid which, if left untreated, can 
lead to the formation of stomach 
ulcers
36
Q

What is end-product

inhibition?

A
The product of a reaction inhibits the 
enzyme required for the reaction.
• Negative-feedback control 
mechanism for the reaction
• Excess products are not made and 
resources are not wasted
• Example of non-non-competitive 
reversible inhibition
37
Q

Describe the metabolic

pathway of respiration

A
• Results in the production of ATP
• Glucose is broken down 
• Addition of 2 phosphate groups to 
glucose molecule 
• The addition of the 2nd phosphate 
group results in the initial 
breakdown of the glucose 
molecule, and is catalysed by the 
enzyme phosphofructokinase 
(PFK)
• This enzyme is competitively 
inhibited by ATP
• Therefore ATP regulates its own 
production
38
Q

Describe how ATP regulates

its own production

A
When ATP levels are high…
• More ATP binds to the allosteric 
site of PFK, preventing the 
addition of the 2nd phosphate 
group to glucose 
• Glucose is not broken down, and 
ATP is not produced at the same 
rate
As ATP is used up…
• Less binds to PFK 
• PFK is able to catalyse the 
addition of the 2nd phosphate 
group to glucose
• Respiration resumes, leading the 
the production of more ATP
39
Q

What are cofactors needed

for?

A
Needed by enzymes in order to 
carry out their function as 
biological catalysts
• May transfer atom groups from 
one reaction to another in a multistep pathway
• May form part of the active site of 
an enzyme
40
Q

What is a cofactor?

A
Non-protein components necessary 
for the effective functioning of an 
enzyme
Inorganic cofactors:
• Obtained via the diet as minerals, 
including iron, calcium, chloride 
and zinc ions 
• e.g. Amylase contains a chloride 
ion that is necessary for the 
formation of a correctly shaped 
active site
41
Q

What is a coenzyme?

A
An organic cofactor
• Derived from vitamins 
• e.g. vitamin B3 is used to 
synthesise NAD (nicotinamide 
adenine dinucleotide), a coenzyme 
responsible for the transfer of 
hydrogen atoms between 
molecules involved in respiration
• e.g. vitamin B5 is used to make 
Coenzyme A, which is essential in 
the breakdown of fatty acids and 
carbohydrates in respiration
42
Q

How are prosthetic groups

different to other cofactors?

A
Prosthetic groups are cofactors 
required by certain enzymes to carry 
out their catalytic function 
• Some cofactors are loosely or 
temporarily bound to the enzyme 
protein in order to activate them, 
but prosthetic groups are tightly 
bound and form a permanent 
feature of the protein
• e.g. Zn2+ ions form an important 
part of the structure of carbonic 
anhydrase, an enzyme necessary 
for the breakdown of CO2
43
Q

What are inactive precursor

enzymes?

A
• Enzymes produces in a inactive 
form 
• Esp. enzymes that can cause 
damage within the cells producing 
them or tissues where they are 
released 
• OR enzymes whose action needs 
to be controlled and only activated 
under certain conditions
44
Q

How do precursor enzymes

work?

A
• They need to undergo a change in 
shape (tertiary structure), esp.to 
the active site to be activated 
• This happens with the addition of 
a cofactor
• Before the cofactor is added, the 
precursor protein is called an 
apoenzyme
• When the cofactor is added and 
the enzyme activated, it is called a 
holoenzyme
45
Q

How else can the change in
tertiary structure be brought
about?

A
• The action of another enzyme, e.g. 
protease, which cleaves certain 
bonds in the molecule
• A change in conditions e.g. pH or 
temperature can result in a change 
in tertiary structure and activate a 
precursor enzyme 
• These types of precursor enzymes 
are called zymogens or 
proenzymes
46
Q

Give an example of

precursor activation

A
• When inactive pepsinogen is 
released into the stomach to 
digest proteins,acid pH transforms 
it into the active enzyme pepsin 
• This adaptation protects body 
tissues against the digestive action 
of pepsin