5. Examine the following two fatty acids.

Classify them as cis or

trans. Which of the two do you believe would be more densely
packed together? Which would have the lower melting point?
Explain.
(5 marks)

Answer:

i) cis

ii) trans

I believe that trans-isomer is more densely packed together

because its carbon
backbone is surrounded with atoms, and straighter in shape
compared to cis-isomer. Meanwhile, cis-isomer is less densely
packed together because it is curved and almost U-shaped which
makes it more flexible.
Next, cis-isomer would have lower melting point than transisomer because the
shape of cis-isomer results in poor packing which means that the
intermolecular
forces of the isomer are not very effective. Therefore, less energy
is needed to
melt the molecule resulting in lower melting point of the isomer.

8. The rate of an enzymatic reaction is measured with three

similar but different substrates. From the experiments, the Km
and kcat values were determined for each substrate.
Substrat

Carbazole Dibenzofuran

Biphenyl

e
km(mM)

31

15

25

kcat(s-1)

0.06

0.14

2.80

Based on this data, answer the following questions:

(a)

Which substrate binds tightest to the enzyme? Explain

your answer.
Dibenzofuran binds tightest to the enzyme because it has the lowest
Km value among the substrates which is 15mM. Substrate with lower
Km value has higher tendency to bind with the enzyme as the
enzymes affinity for the substrate becomes larger.

(b)

Which substrate is the best substrate for the enzyme?

Explain your answer.

The best substrate for the enzyme is biphenyl. Based on the table,
biphenyl has the largest Kcat/Km ratio which is 0.112. This means that
it has higher catalytic efficiency than the other substrates where the
enzyme will react faster in M/sec with biphenyl as it encounters the

substrate. With high specificity constant Kcat/Km, diffusion or the

upper limit of Kcat/Km, can be overcome as the substrate will be able
to diffuse and collide with the enzyme and fits perfectly into the active
site.

9. Explain why very tight binding of substrate to an enzyme is

not desirable for enzyme catalysis, whereas tight binding of
the transition state is desirable.
(10marks)
A very tight binding of substrate to an enzyme is not desirable for enzyme
catalysis because the desired product will not be formed as the reaction does
not move to the right. The role of enzyme in the reaction of two substrates is
as a catalyst where it only helps the two substrates to form a product, not
forming a product with either of the substrates. Therefore, a tight but not
very tight binding is needed in the reaction so that the binding of substrates
with the enzyme can be avoided and no substrates are left out in the
reaction.