PROTEIN METABOLISM (SUBJECTIVE QUESTIONS)

Question 1
Humans have lost the ability to synthesise ten amino acids, so these must be
supplied in the diet. They are known as essential amino acids. Humans have no
method of storing amino acids. After immediate needs are met, surplus amino acids
are oxidised or converted to glycogen or fat and their amino group nitrogen is
excreted as urea. Which of the following statements about the metabolism of amino acids is

correct?
a) Essential amino acids can be formed from other amino acids supplied in the diet.
b) Excess dietary amino acids cannot be converted to other metabolites.
c) Excess dietary amino acids that cannot be oxidised are stored as muscle proteins.
d) Essential amino acids cannot be formed from other amino acids but must be supplied in
the diet.

Question 2
Most amino acids are deaminated by a process known as deamination. Their amino groups are
transferred by transaminases to -ketoglutarate forming glutamate. Glutamate dehydrogenase
plays a central role in amino acid deamination. Using either NAD + or NADP+ as coenzyme
(which is unusual) it removes two hydrogen a0020\atoms from the glutamate so formed,
producing an -ketoglutarate ammonia Schiff base. This spontaneously hydrolyses to give
-ketoglutarate and ammonia. The carbon skeletons of the deaminated amino acids are
metabolized to acetyl-CoA or intermediates of the citric acid cycle depending on the particular
amino acid they were derived from. -ketoglutarate can be a source of energy since it can enter
the citric acid cycle and lead to increased ATP production. Accordingly, glutamate
dehydrogenase is allosterically inhibited by ATP and GTP, high levels of which indicate a high
energy charge, and activated by ADP and GDP. Which of the following statements about the role
of glutamate dehydrogenase iscorrect?
a) Glutamate dehydrogenase has an FAD prosthetic group.
b) Glutamate dehydrogenase has a pyridoxal phosphate cofactor.
c) Glutamate dehydrogenase transaminates glutamate producing -ketoglutarate.
d) Glutamate dehydrogenase oxidativelydeaminates glutamate producing -ketoglutarate.

Question 3
Most amino acids are deaminated in a two-step process in which their amino groups are
transferred to -oxoglutarate by transaminases (amino transferases) forming glutamate. The latter
is then deaminated by glutamate dehydrogenase. Transaminases have pyridoxal phosphate as a
cofactor tightly bound to their active site. It acts as an intermediary in the transfer of amino

groups. It accepts the amino group from the donor amino acid transiently forming pyridoxamine
phosphate. The amino group is then transferred to the acceptor -keto acid, reforming pyridoxal
phosphate.Which of the following statements about transamination reactions is correct?
a) Transamination reactions involve ATP hydrolysis.
b) Transamination reactions are irreversible.
c) Transamination reactions require NAD+ or NADP+.
d) Transamination reactions require pyridoxal-5'-phophate.

Question 4
Urea is the major excreted form of amino acid nitrogen. One of the urea nitrogens is supplied as
free ammonia from the oxidative deamination of glutamate by glutamate dehydrogenase. The
hydrolysis of two ATP molecules is used to incorporate this ammonia and carbon dioxide into
carbamoyl phosphate. Carbamoyl phosphate condenses with ornithine to form citrulline. This is
transported out of the mitochondrial matrix to the cytosol and condenses with aspartate. Another
ATP is used to form argininosuccinate which is lysed to fumarate and arginine. Arginase cleaves
this to urea and ornithine is regenerated and transported back to the mitochondrion. Which of the
following statements about the urea cycle is correct?
a) Argininosuccinate is lysed to urea and ornithine in the urea cycle.
b) Carbamoyl phosphate supplies both of the nitrogen atoms of urea in the urea cycle.
c) The formation of urea from the urea cycle yields energy.
d) Arginine is hydrolysed to urea and ornithine in the urea cycle.

Question 5
The haem biosynthesis pathway begins with glycine and succinyl-CoA forming aminolevulinic
(ALA) acid using aminolevulinate synthase (ALA synthase) in the mitochondrial matrix. This is
the committed step in porphyrin synthesis. Two molecules of ALA condense to form
porphobilinogen finally producing haem via protoporphyrin synthesis. When drugs such as
barbiturates are administered to a patient the synthesis of hepatic cytochrome P450 required for
their metabolism, is increased. The synthesis of ALA synthase is also increased in response to the
demand for haem. Individuals with acute intermittent porphyria cannot handle the increased
supply of ALA due to a deficiency in an enzyme of the biosynthetic pathway. This results in the
preceding metabolites ALA and porphobilinogen accumulating. The symptoms of the disease are
associated with this. Which of the following statements about aminolevulinate synthase (ALA
synthase) is correct?
a) ALA synthase synthesis decreases in individuals treated with drugs such as barbiturates.

b) ALA synthase catalyses the rate-limiting reaction in haem degradation.

c) ALA synthase catalyses the rate-limiting reaction in haem synthesis.
d) ALA synthase is decreased in patients with acute intermittent porphyria.

Question 6
Aminotransferase enzymes require pyridoxal phosphate as a co-enzyme. Most amino acids are
glucogenic i.e. they are metabolized to an intermediate of the TCA cycle or pyruvate. Only
leucine and lysine are purely ketogenic and phenylalanine produces both fumarate and acetyl
CoA, so it is both glucogenic and ketogenic. The average man has a store or a pool of about 300g
of free amino acids. Which of the following statements about amino acid and protein metabolism
is true?
a) Most amino acids are both ketogenic and glucogenic.
b) Both sulphur containing amino acids are essential amino acids.
c) Aminotransferase enzymes require pyridoxal phosphate as a co-enzyme.
d) The average man has a store of about 1kg of free amino acids.

Question 7
Phenylalanine cannot be converted into tyrosine because of an enzyme defect or more rarely
because of lack of tetrahydropterin. It accumulates in the blood and is converted into
phenylpyruvate which is toxic. Inability of phenylalanine to be converted into tyrosine means
that it cannot be deaminated and metabolised properly. Which metabolic abnormality gives rise
to the serious disease phenylketonuria?
a) Homocysteine cannot be converted into methionine
b) Phenylalanine cannot be converted into tyrosine
c) Phenylalanine cannot be converted into alanine
d) Tyrosine cannot be converted into phenylalanine

Question 8
Most amino acids are deaminated by a two-step transdeamination process. Firstly a
transamination reaction with -ketoglutarate occurs forming glutamate, then an oxidative
deamination of glutamate. Which of the following statements about the deamination of amino
acids is correct?
a) Most amino acids are directly deaminated by dehydrogenation reactions.

b) Most amino acids are deaminated by a two-step transdeamination process.

c) Most amino acids are deaminated by transferring their amino groups to oxaloacetate.
d) Most amino acids are deaminated by irreversible transamination reactions.

Question 9
The first step of a transamination reaction is the spontaneous (noncatalysed) formation of a
Schiff base between the carbonyl group of pyridoxal-5'-phosphate and the amino group of the
amino
acid.
ATP hydrolysis is not used to transfer the amino group on the Schiff base to the carbonyl group
of keto acid acceptor. The formation of a Schiff base is freely reversible so it can readily
hydrolyse without the use of ATP. Which of the following statements about the mechanism of
transamination reactions is correct?
a) ATP hydrolysis is used to transfer the amino group on the Schiff base to the carbonyl
group of keto acid acceptor.
b) The first step of a transamination reaction is the formation of a Schiff base between
pyridoxal-5'-phosphate and the carbonyl group of the keto acid.
c) The first step of a transamination reaction is the formation of a Schiff base between the
carbonyl group of pyridoxal-5'-phosphate and the amino group of the amino acid.
d) The first step of a transamination reaction is the formation of a Schiff base between
pyridoxamine phosphate and the keto acid.

Question 10
Deaminated amino acids produce -keto acids. Their carbon skeletons are metabolised. Amino
acids that give rise to acetyl-CoA are ketogenic while those that give rise to oxaloacetate are
glucogenic. Some amino acids are both ketogenic and glucogenic. Phenylalanine for example
produces fumarate (an intermediate in the citric acid cycle) and acetyl-CoA, so it is both
ketogenic and glucogenic. Which of the following statements about the carbon skeletons of
amino acids are correct? Please select all that apply.
a) Ketogenic amino acids can give rise to acetyl-CoA.
b) Glucogenic amino acids can give rise to glucose in starvation.
c) Ketogenic amino acids give rise to glucose.
d) Ketogenic amino acids are always converted to ketone bodies.

e) Some amino acids are both glucogenic and ketogenic.