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4

Answers to end-of-chapter questions

1 A

[1]

2 B

[1]

3 C

[1]

4 B

[1]

5 C

[1]

6 B

[1]

7 B

[1]

8 D

[1]

Structured questions

9

a Succinic acid

[1]

b Malonic acid is a competitive inhibitor

 

Since it has a similar structure to succinic acid – the substrate – it competes for the active site and binds to it

Less substrate (succinic acid) attaches to the active site of enzyme

Less product (fumaric acid) is formed

Explanation [2]

substrate –

succinic acid

malonic acid – competitive inhibitor, similar shape to substrate

acid – competitive inhibitor, similar shape to substrate enzyme – succinic dehydrogenase inhibitor binds to
acid – competitive inhibitor, similar shape to substrate enzyme – succinic dehydrogenase inhibitor binds to

enzyme – succinic dehydrogenase

inhibitor binds to active site hence no enzyme–substrate complex formed; no products formed

Diagram only [1] Explanation on diagram [3] Max [3]

c Ethanol has a similar molecular structure to ethylene glycol / substrate

 

Therefore, it would also be complementary to the active site of enzyme

Ethanol would act as a competitive inhibitor

It would compete for the active site of enzyme

It would prevent ethylene glycol (the substrate) from binding with active site

5–6 points [3]

d

e

Fewer enzyme–substrate complexes and less product (oxalic acid) formed

3–4 points [2] 1–2 points [1]

Heavy metals form covalent bonds with the –SH groups of the enzyme

These bonds may be formed in the active site

If bonds are formed at the active site, the active site would be permanently blocked

So no enzyme–substrate complexes could be formed

If the covalent bonds with the heavy metal and –SH groups are formed away from the active site (at allosteric site), these bonds would disrupt the tertiary structure of the enzyme

This would change the shape of the active site

Hence the active site would no longer be complementary to substrate

Substrate would no longer be able to fit in the active site (lock and key)

Or the active site would be prevented from changing shape to fit the substrate (induced fit)

No enzyme–substrate complexes formed hence no

Well explained with either bond formation at

the active site or elsewhere [2]

products

bond formation at the active site or elsewhere [2] products heavy metal permanently bonded at the

heavy metal permanently bonded at the active site so substrate no longer fits in the active site

active site so substrate no longer fits in the active site substrate no longer fits in
active site so substrate no longer fits in the active site substrate no longer fits in

substrate no longer fits in the active site

shape of the active site changes

Good diagram [2]

(b) (d) Substrate concentration Rate of reaction
(b)
(d)
Substrate concentration
Rate of reaction

Each curve [2]

10

a Metabolic reactions – the chemical reactions occurring within an organism’s body

[2]

b Lock-and-key

The substrate molecule is complementary in shape to that of the active site

The active site on the surface of the enzyme is so contoured and charged that it attracts only one substrate and the shape of the active site is complementary to that of the substrate

It was thought that the substrate exactly fitted into the active site of the enzyme molecule like a key fitting into a lock (lock-and- key theory)

Enzyme–substrate complexes formed

This explained why an enzyme would only work on one substrate (specificity)

[2]

Induced fit

Active site is not perfectly contoured to fit substrate

When the substrate attaches to the active site, the shape of the whole enzyme changes slightly so it can accommodate and hold the substrate

[1]

c i From 10 °C to 41 °C , the rate of activity increases from 0% to 100%

For every 10 °C increase in temperature, the activity doubled

Rate increased because there is more kinetic energy

Enzyme and substrate molecules collide more often, also because more molecules have sufficient energy to overcome the activation energy

Optimum is 41 °C

Above the optimum temperature, the rate decreases as more of the enzyme molecules denature

The thermal energy breaks the hydrogen bonds holding the secondary and tertiary structure of the enzyme together

So the enzyme loses its shape and becomes a random coil – and the substrate can no longer fit into the active site

This is irreversible

5 points well explained [5]

ii

COOH + NH 3
COOH
+ NH 3

COO

NH 2

inactive

active

inactive

Diagram [3] Correct activity [2]

11

a

disappearance of substrate

[1]

 

appearance of product

[1]

b

i

b i at 22 ° C Graph showing the effect of pH on enzyme activity of

at 22 °C

Graph showing the effect of pH on enzyme activity of catalase

x-axis labelled, with appropriate intervals [1] y-axis, with appropriate intervals [1] Points correctly plotted and joined [1] Title [1]

ii optimum pH = 7

 

lowest activity is at pH 3

active over a narrow range

increasing activity as pH increases to optimum / pH 7

4–5 points [2]

decreasing activity as pH increases above optimum / pH 7

2–3 points [1]

iii At pH 3

high concentration of H + ions

 

enzyme acts a buffer

–COOH groups unionized

H and ionic bonds broken

tertiary structure of enzyme disrupted

shape of active site changes

few enzyme–substrate complexes formed

[1]

 

At pH 7

optimum activity: active site unchanged, enzyme–substrate complexes formed, maximum products

[1]

At pH 8

low concentration of H + ions

 

enzyme acts a buffer

–NH 2 groups unionised

Hydrogen bonds and ionic interactions broken

tertiary structure of enzyme disrupted

shape of active site changes

few enzyme–substrate complexes formed

[1]

 

c See graph above: same basic shape / lower activity

[2]

d To maintain the pH of each experimental solution

[1]

e volume of hydrogen peroxide used

 

volume of enzyme used

time for reaction to take place

Any 2 points [1]

Essay questions

 

12

a

i

 

Activation energy is the minimum free energy that must be possessed by the molecules on collision for the particles to react

It is the amount of energy needed to raise the reactants to an activated state

It is amount of energy given temporarily to a substrate to be converted into a product

Any point [2]

ii

 
  Each curve [1]

Each curve [1]

 

b

Enzyme has tertiary structure

 

Active site of enzyme is made up of few amino acids

With a specific shape

Shape of active site complementary to substrate

7 points [4]

Only one substrate or type of substrate will fit into active site

5–6 points [3]

To form enzyme–substrate complexes

3–4 points [2]

Refer to lock-and-key and induced fit

1–2 points [1]

 

c

Substrate binds to active site of enzyme

 

Few amino acids are involved

Remainder of amino acids maintains the globular shape

Shape of active site complementary to substrate

Can interact by exact fit: lock-and-key

Then moulds around the substrate: induced fit

Substrate held to active site by hydrogen bonds and ionic interactions bonds as well as hydrophobic and hydrophilic interactions

To form the enzyme–substrate complex

 

Enzyme–substrate complex activated into forming products

Substrate changes shape slightly

To put strain on bonds in the substrate / weakens bonds

Activated into forming products

Which no longer fit the active site

Products move way, leaving the active site free to form more enzyme–substrate complexes

Each point [1] Max [7]

13

a

i

pH

 
  Well drawn and labelled [1]

Well drawn and labelled [1]

Description

Normally enzyme works in narrow pH range

Rate reduces quickly when pH changes from optimum pH

[1]

Explanation

 

Changes in pH from optimum affect H + ion concentration in solution At low PH

high concentration of H + ions

 

enzyme acts a buffer

–COOH groups unionised

At high pH

low concentration of H + ions

enzyme acts a buffer

–NH 2 groups unionised

Hydrogen bonds and ionic interactions

In both cases

tertiary structure of enzyme disrupted

shape of active site changes

few enzyme–substrate complexes formed

[2]

ii

Enzyme concentration

Description Well drawn and labelled [1] • Rate of reaction increases as enzyme concentration increases

Description

Well drawn and labelled [1]

Rate of reaction increases as enzyme concentration increases

Rate directly proportional / linear to enzyme concentration

[1]

Explanation

More active sites are available

More collisions between enzyme and substrate molecules

More enzyme–substrate complexes formed

More product as enzyme concentration increases

[2]

iii

Substrate concentration

increases [2] iii Substrate concentration Description Well drawn and labelled [1] • Initial

Description

Well drawn and labelled [1]

Initial substrate concentration limits the rate of reaction / rate directly proportional to substrates concentration

Reaches maximum velocity and plateaus

[1]

Explanation

All active sites initially available

More frequent collisions between substrate and active sites

Then as substrate concentration increases, all active sites become occupied / saturated

No more enzyme–substrate complexes can be formed until product is formed.

[2]

iv

Inhibitors

Description • Inhibitor reduces rate of reaction • Can be competitive or non-competitive • Can

Description

Description • Inhibitor reduces rate of reaction • Can be competitive or non-competitive • Can be

Inhibitor reduces rate of reaction

Can be competitive or non-competitive

Can be reversible or irreversible

Well drawn and labelled [1]

[1]

Explanation Competitive

similar shape to substrate

competes for active site / occupies active site / binds at active site

blocks entry of substrate

less substrate bind / less enzyme–substrate complex formed

does not bind permanently to active site

increasing concentration lessens effect of inhibitor Non-competitive

 

not similar in shape to substrate

binds permanently to active site and blocks it

hence irreversible

or binds to a site away from active site / allosteric site

this distorts the tertiary structure of the enzyme

shape of active site changes

this could be reversible or irreversible

increasing substrate concentration does not lessen effect of inhibitor

Well explained [2]

b

Held in place in active site by temporary bonds

e.g. hydrogen, ionic, hydrophobic and hydrophilic interactions

That form between the substrate and some of the R groups of the enzyme’s amino acids

1 point each [max 3]

14

a

optimum temperature = 40 °C: more kinetic energy, more collisions between enzyme and substrate, more enzyme–substrate complexes formed

and substrate, more enzyme–substrate complexes formed temperature above optimum: more kinetic energy; molecules
and substrate, more enzyme–substrate complexes formed temperature above optimum: more kinetic energy; molecules

temperature above optimum: more kinetic energy; molecules vibrate quickly; hydrogen bonds broken in tertiary structure of enzyme; shape of active site changes; fewer/no enzyme– substrate complexes formed; enzyme denatured; irreversible

at low temperatures:

slow reaction; less kinetic energy; fewer collisions between enzyme and substrate; fewer enzyme– substrate complexes formed, enzyme is not denatured; for every 10 °C increase in temperature, rate

for every 10 ° C increase in temperature, rate   Graph [1] Annotations [3] b i
 

Graph [1]

Annotations [3]

b

i General class is hydrolases

General class [1]

For proteins (e.g. blood and grass): proteases

Grease/oil: lipases

Starch-based products (e.g. gravy / sauces): amylases

Example [1]

ii Temperature between 40 °C and 50 °C

Conditions [2]

Cleaning power depends on enzyme activity

Optimum temperature for enzyme

Maximum collisions between enzyme and substrate

More products

Substrate / stain broken down

Neutral pH / detergent and water only

If pH decreases from optimum, H + ions would interact with amino acids of enzymes

Hydrogen bonds and ionic interactions broken

Tertiary structure of enzyme disrupted

Shape of active site changes

Few enzyme–substrate complexes formed

Well explained [3]

c

i Non-competitive inhibition

Tertiary structure of enzyme distorted when aspirin attaches to R group of amino acid of enzyme

Changes shape of active site

Substrate for COX no longer fits in active site

No enzyme–substrate complexes formed

Well explained [2]

ii Competitive inhibition occurring

Since penicillin resembles the substrate

It is also irreversible since bonds permanently at the active site

Therefore stops activity of transpeptidase

Well explained [2]