Course Code: BIO 024
Module #10
Name: ____________________________________________________________ Class number: _______
Section: ____________ Schedule: ____________________________________ Date: _______________
Module 10: CHECK YOUR UNDERSTANDING - RATIONALE
1. C: Isoleucine:
ISOLEUCINE – both glucogenic (produces Succinyl CoA) and ketogenic but it directly produces acetyl CoA
and not Acetoacetyl CoA
LYSINE – ketogenic but the ultimately converted to acetoacetyl CoA
PHENYLALANINE – both glucogenic (produces fumarate) and ketogenic (produces acetoacetyl CoA and
Acetyl CoA and vice versa)
ALANINE – both glucogenic (produce pyruvate then enter the CTC) and ketogenic (pyruvate is converted to
acetyl CoA)
LEUCINE – ketogenic but yields both acetyl CoA and acetoacetyl coA
2. D: Leucine: ketogenic but yields both acetyl CoA and acetoacetyl coA
3. D: In positive nitrogen balance the excretion of nitrogenous metabolites is less than the dietary intake of nitrogenous
compounds.
TWO TYPES OF NITROGEN BALANCE:
negative nitrogen balance
▪ protein degradation exceeds protein synthesis, the amount of nitrogen in the urine exceeds the amount of nitrogen
ingested (dietary protein).
▪ accompanies a state of “tissue wasting,” because more tissue proteins are being catabolized than are being replaced
by protein synthesis.
▪ Protein-poor diets, starvation, and wasting illnesses produce a negative nitrogen balance.
positive nitrogen balance –
▪ nitrogen intake exceeds nitrogen output, indicates that the rate of protein anabolism (synthesis) exceeds
that of protein catabolism.
▪ state indicates that large amounts of tissue are being synthesized, such as during growth, pregnancy, and
convalescence from an emaciating illness.
4. B: Arginine and Histidine.
Histidine is an essential amino acid for infants, but was not demonstrated to be required by adults until recently (Cho
et al., 1984; Kopple and Swendseid, 1981). Under special circumstances (e.g., in premature infants or in people with
liver damage), amino acids such as cystine and tyrosine, not normally essential, may become so because of impaired
conversion from their precursors (Horowitz et al., 1981). Arginine is synthesized by mammals but not in amounts
sufficient to meet the needs of the young of most species. Although it is not believed to be required by the human
infant for normal growth, the need for arginine by the premature infant is unknown. When arginine is present in small
amounts relative to other amino acids (such as in intravenous solutions or amino acid mixtures), or when liver function
is compromised, arginine synthesis may be insufficient for adequate function of the urea cycle (Heird et al., 1972).
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Course Code: BIO 024
Module #10
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5. D: Ammonium ion is the form the nitrogen is incorporated into an amino acid.
6. C: The needed enzyme for a transamination reaction is an aminotransferase. Most aminotransferases accept only a-
ketoglutarate and to a lesser extent oxaloacetate. Thus glutamate (from a-ketoglutarate) and aspartate (from
oxaloacetate) are the two amino acids produced in transamination reactions. Its action effects the transfer of the amino
group from one carbon skeleton to another.
7. B: The pathways for the biosynthesis of amino acids are diverse. However, they have an important common feature:
their carbon skeletons come from intermediates of glycolysis, the pentose phosphate pathway, or the citric acid cycle.
On the basis of these starting materials, amino acids can be grouped into six biosynthetic families.
8. D: pyridoxal phosphate (PLP).
A transamination reaction is a biochemical reaction that involves the interchange of the amino group of an a-amino acid
with the keto group of an a-keto acid.
The needed enzyme for a transamination reaction is an aminotransferase. Most aminotransferases accept only a-
ketoglutarate and to a lesser extent oxaloacetate. Thus glutamate (from a-ketoglutarate) and aspartate (from oxaloacetate)
are the two amino acids produced in transamination reactions. Its action effects the transfer of the amino group from one
carbon skeleton to another. There is no loss or gain of amino groups in transamination. Amino group transfer is all that
occurs; hence the name transamination (transfer of an amino group) for this type of reaction. Although a transamination
reaction appears to involve the simple transfer of an -NH3+ group between two molecules, the reaction involves several
steps and requires the presence of pyridoxal phosphate, a coenzyme produced from pyridoxine (vitamin B6).
9. C: Oxidative deamination of glutamate requires the enzyme glutamate dehydrogenase. This enzyme is unusual in that
it is the only known enzyme that can function with either NADP+ or NAD+ as a coenzyme. Note that a-ketoglutarate is
a product of this process. It can be reused in the first series of transamination reactions. The NADH and H+ formed
can participate in the electron transport chain and oxidative phosphorylation to produce ATP molecules. The NH4+
so produced, a toxic substance if left to accumulate in the body, is then converted to urea in the urea cycle.
10. B: Aspartate
NH4+ and aspartate, the forms in which nitrogen enters the urea cycle, are produced from amino acids in the liver by
a series of transamination and deamination reactions. Glutamate dehydrogenase is a key enzyme in the process
because it generates the free NH4+ previously transferred to α-ketoglutarate from many amino acids by transaminases.
As dietary protein increases (a protein-rich diet) the concentration of the enzymes of the urea cycle increase,
suggesting a regulated response to meet the increased need for nitrogen disposal.
11. C: Phenylketonuria, also called PKU, is a rare inherited disorder that causes an amino acid called phenylalanine to
build up in the body. PKU is caused by a defect in the gene that helps create the enzyme needed to break down
phenylalanine.
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Course Code: BIO 024
Module #10
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Without the enzyme necessary to process phenylalanine, a dangerous buildup can develop when a person with PKU eats
foods that contain protein or eats aspartame, an artificial sweetener. This can eventually lead to serious health problems.
Phenylalanine hydroxylase is an enzyme your body uses to convert phenylalanine into tyrosine, which your body needs to
create neurotransmitters such as epinephrine, norepinephrine, and dopamine. PKU is caused by a defect in the gene that
helps create phenylalanine hydroxylase.
12. C: Aspartate, α-ketoglutarate.
The product of transamination reactions depend on the availability of α-keto acids. The products usually are
either
alanine, aspartate or glutamate, since their corresponding alpha-keto acidsa-ketoglutarate)
( are produced through
metabolism of fuels.
13. D: Urinary urea is increased by a diet rich in protein.
14. D: In patients with PKU, tyrosine cannot be synthesized from phenylalanine and hence, becomes essential and must
be supplied in the diet. Phenylalanine in the diet must be controlled but cannot be eliminated entirely because it is an
essential amino acid. Dietary treatment must begin during the first 7-10 days of life to prevent intellectual disability,
and lifelong restriction of phenylalanine is recommended to prevent cognitive decline. Additionally, elevated levels of
phenylalanine are teratogenic to developing fetus.
15. B: Maple syrup urine disease is an autosomal recessive metabolic disorder affecting branched-chain amino acids. It is
one type of organic acidemia. The condition gets its name from the distinctive sweet odor of affected infants' urine,
particularly prior to diagnosis and during times of acute illness.
SUGGESTED VIDEOS:
Protein digestion and absorption: [Link]
Protein digestion Osmosis version at 2:30th to 3:35th minute: [Link]
Protein metabolism general overview: [Link]
Urea cycle: [Link]
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