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Structured questions
9
Succinic acid
[1]
substrate
succinic acid
enzyme succinic
dehydrogenase
inhibitor binds to
active site hence no
enzymesubstrate
complex formed; no
products formed
56 points [3]
34 points [2]
12 points [1]
Rate of reaction
(b)
(d)
Substrate concentration
10 a
b
[2]
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-andkey theory)
Enzymesubstrate 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]
ii
COO
NH2
COOH
+
NH3
inactive
11 a
active
inactive
Diagram [3]
Correct activity [2]
disappearance of substrate
appearance of product
[1]
[1]
at 22 C
iii
optimum pH = 7
lowest activity is at pH 3
active over a narrow range
increasing activity as pH increases to optimum / pH 7
decreasing activity as pH increases above optimum / pH 7
45 points [2]
23 points [1]
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 enzymesubstrate complexes formed
[1]
At pH 7
optimum activity: active site unchanged, enzymesubstrate complexes formed,
maximum products
[1]
At pH 8
low concentration of H+ ions
enzyme acts a buffer
NH2 groups unionised
Hydrogen bonds and ionic interactions broken
tertiary structure of enzyme disrupted
shape of active site changes
few enzymesubstrate complexes formed
[1]
[2]
[1]
Essay questions
12 a
ii
7 points [4]
56 points [3]
34 points [2]
12 points [1]
13 a
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
NH2 groups unionised
Hydrogen bonds and ionic interactions
In both cases
tertiary structure of enzyme disrupted
shape of active site changes
few enzymesubstrate complexes formed
[2]
ii
Enzyme concentration
[1]
Explanation
More active sites are available
More collisions between enzyme and substrate molecules
More enzymesubstrate complexes formed
More product as enzyme concentration increases
[2]
iii
Substrate concentration
[2]
Inhibitors
[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 enzymesubstrate 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
b
14 a
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
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
Graph [1]
Annotations [3]
ii
ii
Example [1]
10