Biochemistry Intermediate Exams

Enzymes
• Definition: They’re proteins that speed up chemical processes.

▪ Give three examples for each class of the following classes:

Class Type of Reaction Example

Oxidoreductases Oxidation-Reduction Lactate Dehydrogenase
Transferases Group Transfer Hexokinase
Hydrolases Hydrolytic cleavage of bonds Fructose 1,6 Bisphosphatase
Lyases Cleave of bonds leaving double Fumarase
bonds
Isomerase Geometric or structural changes Phosphohexose Isomerase
within a molecule
Ligases Joining of two substrates coupled Pyruvate Carboxylase
to ATP hydrolysis

▪ Factors affecting enzyme function:

1. pH
2. Temperature
3. Inhibitors
4. Activators
5. Enzyme Concentration
6. Substrate Concentration
7. Allosteric Factors
8. Salt Concentration (Salts can activate or deactivate the enzyme depending upon its
concentration)
▪ Define and explain the following terms relating to enzyme activity:
1. Coenzyme: Non-protein are small organic molecules
2. Active Site: The region where the substrate binds
3. Feedback Inhibition: A control mechanism by which the end product inhibits the enzyme
activity.
4. Allosteric Regulation: Modulation of enzyme activity by binding of allosteric effectors by
allosteric enzymes with no structural similarity to substrate or coenzyme

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 Carbohydrates
• Glycolysis:
▪ Definition: The major catabolic process concerned with the breakdown and oxidation of
glucose.
▪ Name two specific characteristics of glucokinase in contrast to hexokinase:

Characteristic Hexokinase Glucokinase

Location All Tissue Liver, Pancreas
Substrate All Hexoses Glucose
Function Energy Production Glucose → Glycogen for storage
Km Low Km → High Affinity High Km → Low Affinity

▪ Three enzymes catalysing irreversible steps in glycolysis:

1. Hexokinase
2. Phosphofructokinase-1
3. Pyruvate Kinase
▪ Describe the two initial reactions involved in the conversion of glycerol into glucose:
A. Glycerol → Glycerol 3 Phosphate, Enzyme: Glycerol Kinase, ATP → ADP
B. Glycerol 3 Phosphate → Dihydroxyacetone Phosphate, Enzyme: G3P DH, NAD → NADH
▪ Please select the single best answer that describes the activity of the following enzymes:

Column A Column B
Phosphoglycerate Kinase Catalyses a substrate level phosphorylation
Glucose 6 Phosphate Dehydrogenase Catalyses the first committed step in pentose
phosphate pathway
Phosphoglucomutase Isomerizes the position of a phosphate
Acetyl CoA Carboxylase Requires biotin
Pyruvate Dehydrogenase Regulated by phosphorylation
Triose Phosphate Isomerase Conversion from aldose to ketose

▪ Explain the term glucose-alanine cycle?

A. Is a gluconeogenesis mechanism for conversion of alanine (glucogenic amino acid) into glucose.
▪ Compare and contrast PPP & Glycolysis:
Glycolysis PPP
Definition Major energy yielding pathway for Biosynthetic pathway to generate precursors
carbon metabolism. for biosynthesis.
End Product Pyruvate Various intermediate precursors.
Lactate
Energy Provides 2 or 8 ATP by: No energy provision, due to the phosphate in
1. Reducing Equivalents the NADPH (reducing agent)
2. Substrate Level Phosphorylation
Site All cells Certain tissues that have requirement for PPP
products.

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 ▪ Mention fates of pyruvate, and the enzymes involved:

Substrate Enzyme Product

Pyruvate Pyruvate Dehydrogenase Complex Acetyl – CoA
Pyruvate Pyruvate Carboxylase Oxaloacetate
Pyruvate Pyrvuate Acetaldehyde Alcohol Ethanol
Decarboxylase Dehydrogenase
Pyruvate Lactate Dehydrogenase Lactate

▪ Outline the reaction catalysed by the enzyme lactate dehydrogenase, and explain why lactate
is the end product of glycolysis in exercising muscles:
A. Oxygen is not present during exercise in a
sufficient manner, so lactic acid is produced
more frequently.

▪ How can NAD be regenerated in anaerobic

glycolysis:
▪ A. Reduction of pyruvate to lactate will convert NADH → NAD

▪ What are the possible sources of glucose circulating in the blood stream:
1. Glycogenolysis
2. Gluconeogenesis
3. Dietary CHO

• Gluconeogenesis:
▪ Definition: The major anabolic process concerned with synthesis of glucose from non-
carbohydrate substrates.

▪ Key enzymes of gluconeogenesis:

1. Pyruvate Carboxylase
2. Phosphoenol Pyruvate Carboxykinase
3. Fructose 1,6-bisphosphatase
4. Glucose 6-phosphatase (Absent in muscles)
▪ Substrates of gluconeogenesis:
1. Lactate
2. Glycerol
3. Glucogenic Amino Acids
• Glycogen Metabolism:
▪ List two tissues or organs where glycogen is stored indicating its function in each:
1. Muscle: Glycogen converts to glucose during heavy use of muscle.
2. Liver: Regulation of the blood glucose level when the body enters fasting state.
▪ What is the reaction catalysed by the enzyme glycogen phosphorylase?
A. Glycogen + Inorganic Phosphate → Glucose-1-Phosphate (RATE LIMITING STEP)

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 ▪ List the three initial steps of glycogen synthesis starting with glucose:
A. Glucose → Glucose-6-Phosphate, Enzyme: Glucokinase
B. G6P → G1P, Enzyme: Mutase
C. G1P → UDP Glucose, Enzyme: UDP Glucose Phosphorylase

▪ Glycogen Storage Disease Types:

Type Deficient Enzyme

Von Gierke’s G6-Phosphatase
Pompe Lysosomal alpha-1,4 glycosidase
Cori Debranching Enzyme
Anderson Branching Enzyme
McArdle Muscle Glycogen Phosphorylase
Hers Hepatic Glycogen Phosphorylase

▪ Glycogen Degradation is carried out by: Glycogen Phosphorylase

▪ Glycogen Synthesis is carried out by: Glycogen Synthase
• TCA Cycle:
▪ Definition: Final common cyclic pathway for oxidation of carbohydrate, lipids, proteins or active
acetate.

▪ What are the NAD dependent steps in TCA cycle? (WITH ENZYMES)
1. Isocitrate → Alpha Ketoglutarate, ENZYME: Isocitrate Dehydrogenase
2. Alpha Ketoglutarate → Succinyl CoA, ENZYME: A-KG DH
3. Malate → Oxaloacetate, ENZYME: Malate Dehydrogenase
▪ List two possible functions of TCA in the liver, giving examples.
1. Fat oxidation
2. Metabolic precursor of gluconeogenesis
▪ Two examples illustrating anabolic role of TCA cycle:
1. Oxaloacetate → Aspartate → to purine and pyrimidine, Enzyme: Aspartate
Aminotransferase
2. Succinyl CoA in the synthesis of heme
3. Alpha Ketoglutarate → Glutamate, Enzyme: Glutamate Dehydrogenase
▪ Name two mechanisms for energy production by TCA:
1. Breakdown of Acetyl-CoA
2. Reducing Equivalent
▪ Inhibitors of TCA cycle & the reaction inhibited:
Inhibitors Fluoroacetate Arsenite Malonate
Enzymes Aconitase Alpha Succinate
Inhibited Ketoglutarate Dehydrogenase

▪ Show briefly the relationship between gluconeogenesis & TCA cycle:

A. Pyruvate is converted into oxaloacetate by pyruvate carboxylase.
B. Pyruvate into malate, now it can go to the cytosol.
C. Malate into oxaloacetate once again, then it will leave the TCA cycle.
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 • Pentose Phosphate Pathway
▪ Importance of PPP:
A. Production of NADPH
- Which is used in synthesis of:
1. Fatty Acid (Lipogenesis)
2. Steroid Hormones (Steroidogenesis)
- And protects against RBC membrane haemolysis.
B. Production of Ribose Sugar
- Enters in synthesis of DNA & RNA.
▪ Mention the consequences of G6P-DH deficiency:
A. Deficiency will lead to favism, taking any oxidants will lead to haemolytic anemia, as the
NADPH produced to enter the glutathione cycle is deficient, and so the primary protection
mechanism of RBC membrane is lost causing haemolysis of RBC membrane.

▪ List two enzymes in the non-oxidative phase of the pathway:

1. Transketolase
2. Transaldolase
3. Epimerase
4. Isomerase
▪ List two key enzymes in PPP:
A. Glucose-6-Phosphate Dehydrogenase
B. 6-Phosphogluconate Dehydrogenase

Lipid & Fatty Acids

‫ أحمد الكردي‬.‫برعاية ملخصات د‬
• β-Oxidation of fatty acids:
▪ Intracellular Location: Mitochondria
▪ What is the role of the following in lipid metabolism:
A. Hormone Sensitive Lipase (HSL): Catalyses the initial, rate limiting reaction in lipolysis.
B. Carnitine Acyl Transferase: Mediate the transport of long chain fatty acid across inner
mitochondrial membrane by binding them to carnitine.

▪ Mention two tissues in which this pathway is active, indicating the cellular location:
A. Liver, Outer mitochondrial membrane
B. Adipose Tissue, Outer mitochondrial membrane
- What is the role of carnitine in this pathway?
A: Transport fatty acid into mitochondria for oxidation.

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 ▪ Three products of the process that can act as substrates for energy production and their fates
are:
A. Acetyl-CoA → TCA Cycle → 12 ATP
B. NADH → ETC → 3 ATP
C. FADH2 → ETC → 2 ATP
▪ How many ATPs are produced by the complete oxidation of a fatty acid containing 22 carbon
atoms?
A. Carbon Atoms / 2 = Number of Acetyl CoA Produced, 22 / 2 = 11, Acetyl-CoA = 11
B. Subtract 1 from Acetyl-CoA, this gives you NADH & FADH produced, = 10
C. NADH = 3 ATP, FADH = 2 ATP, Acetyl-CoA = 12 ATP
D. ((11x12) + (10x3) + (10x2)) – 2  Previously Used Energy = 180 ATP

▪ Name the major lipid transported by the following lipoproteins:

Lipoprotein Lipid Transported Transport Site Note

Chylomicrons Exogenous, Dietary, Intestine → Tissue With highest TG
Triacylglyceride content.
VLDL Endogenous, Liver → Extrahepatic
Triacylglyceride Tissue
HDL (Good) Cholesterol Extrahepatic → Liver
LDL (Bad) Cholesterol Liver → Extrahepatic With highest cholesterol
Tissue content.

▪ What is the significance of HDL/LDL ratio?

A. Index for disease such as coronary artery disease, it’s used to assess the level of cholesterol
in the body.
▪ Cholesterol can be utilized in the synthesis of / precursor of:
1. Vitamin D
2. Steroid Hormones
3. Bile Acids
4. Plasma Membrane Components
• Ketone Metabolism:
▪ Name products of ketogenesis:
1. Acetone
2. Acetoacetate
3. Beta Hydroxybutyrate
▪ Q. What is the rate limiting step in ketogenesis?
- A. acetoacetyl-CoA + acetyl-CoA → B-Hydroxy B-Methylglutaryl-CoA, Enzyme: HMG-CoA
Synthase
▪ Mention organs that can utilize ketone bodies for energy use:
1. Brain
2. Heart
3. Muscle

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 ▪ What is the main building block of ketone bodies:
A. Acetyl-CoA
▪ Mention two tissues actively involved in ketogenesis indicating the intracellular location:
A. Liver, Mitochondrial Matrix
B. Kidney, Mitochondrial Matrix
▪ Under what conditions is the pathway active and what is its biochemical importance:
A. Physiological in starvation state.
B. Pathological in diabetes
▪ Show briefly how one of the ketogenesis products are utilized for energy production:
A. Activation of acetoacetate consumes 1 ATP to acetoacetyl-CoA
B. Acetoacetyl-CoA is converted into two acetyl-CoA by thiolase.
C. 2 Acetyl-CoA gives 24 ATP.

Protein & Amino Acids

▪ Definition of the following:

Term Definition
Glucogenic AA Are amino acids that are degraded to pyruvate, or TCA cycle intermediates, finally
gives glucose or glycogen
Ketogenic AA Are amino acids that are degraded to acetyl-CoA or acetoacetate, finally gives
ketone bodies or fat.
Essential AA Are amino acids which the body cannot synthesize.
Non-essential AA Are amino acids which the body can synthesize.

➢ TIP: All amino acids are glucogenic except lysine and leucine.

▪
What is the role of the following enzymes in amino acid metabolism:
-
Glutamate Dehydrogenase: catalyzes the reversible inter-conversion of glutamate to α-
ketoglutarate and ammonia
- Transaminase: enzymes that catalyze a transamination reaction between an amino acid and
an α-keto acid.
▪ Explain the difference in roles of these enzymes:
Characteristic Glutaminase Glutamate Dehydrogenase
Role Catalyses the reaction of Catalyses the reaction of
glutamine to ammonia. ammonia to glutamate

▪ Mention two transaminases used in diagnosis of disease:

A. Aspartate Aminotransferase (AST)
B. Alanine Aminotransferase (ALT)

• Urea Cycle:
▪ Concerning the committed step in the urea cycle, mention the following:
1. Substrates: NH4, HCO3, CO2
2. Enzyme: Carbamoyl Phosphate Synthetase 1
3. Product: Carbamoyl Phosphate
4. Activator: N – Acetyl Glutamate (NAG)

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 ▪ Name the enzyme that catalyses the first reaction of urea cycle and the subcellular location:
A. Carbamoyl Phosphate Synthetase 1
B. Mitochondrial Matrix
➢ Tip: Reaction 1 and 2 in the mitochondria, while 3, 4 and 5 in the cytosol.

▪ Explain the difference in roles between:

Characteristic Carbamoyl Phosphate Carbamoyl Phosphate
Synthetase 1 Synthetase 2
Subcellular Location Mitochondrial Matrix Cytosol
Pathway / Role Initiates the urea cycle Biosynthesis of pyrimidines
Regulation Activated by N-acetyl glutamate. Activated by ATP
Inhibited by UTP
Nitrogen Source Ammonia Amide group of glutamine

▪ What are the sources of the two nitrogens of urea:

1. Aspartate
2. Ammonium
• Biosynthesis:
▪ What are the specialized products formed from the following amino acids?

Amino Acid Short Specialized Product

Tyrosine Tyr 1. Catecholamines
2. Melanin
3. Thyroid Hormones
Glutamate Glu 1. Glutathione
2. Gamma Aminobutyric Acid
Cysteine Cys Glutathione
Glycine Gly Glutathione, Heme
Tryptophan Trp Serotonin
Histidine His Histamine
Lysine Lys Carnitine
Active SAM Carnitine, Creatine
Methionine

• Ammonia:
▪ List two reactions which produce free ammonia:
A. Glutamate → a-Ketoglutarate, Enzyme: Glutamate Dehydrogenase, NADP → NADPH
B. Glutamine → NH3, Enzyme: Glutaminase, H2O → Glutamate
▪ Mention two reasons to explain ammonia toxicity in the brain:
A. Glutamate DH reaction is shifted towards Glu synthesis resulting in consumption of TCA cycle
intermediates [α -KG] and decrease in brain energy.
B. Gln synthetase consumes Glu which forms GABA, this causes neurotoxic effects in the brain.

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 • Inborn Errors of Metabolism:

Disorder Defective Enzyme AA Pathway Notes

Phenylketonuria Phenylalanine Phe Present in Urine:
Hydroxylase (Type 1. Phenylalanine (↑ in Tissue & Blood)
1) 2. Phenyllactate
3. Phenylacetate
Dihydrobiopterin 4. Phenylpyruvate
Reductase (Type Characterized by:
2&3) 1. Mousy Odor
2. Hypopigmentation (↓ Tyrosinase)
3. Mental Retardation
Albinism Tyrosinase Tyr Characterized By:
(Tyrosine 1. Lack of Melanin
Hydroxylase) 2. Vision Defects
3. Photophobia
Alkaptonuria Homogentisate Phe, Tyr Characterized By:
Oxidase 1. Ochronosis (Dark Tissue)
2. Arthritis (Joint Pain)
3. Urine turns black when oxidized by air.
Maple Syrup Branched-Chain Leu, Ile, Val Characterized By:
Urine Disease α-Keto Acid 1. Maple / Burnt sugar odor of urine.
(MSUD) Dehydrogenase 2. May lead to mental retardation & death if
untreated.
Homocystinuria Cystathionine Met Present in Plasma & Urine:
β-Synthase 1. ↑ Homocysteine
2. ↑ Methionine
3. ↓ Cysteine
Characterized By:
1. Cardiovascular Disease Mortality
2. Thrombosis
3. Mental Retardation

▪ NOTE: The amino acids in these disorders are non-essential but become essential due to their
deficiency.

Genetics
▪ Define the terms:

Term Definition
Nucleosome Basic structural unit of DNA packaging in eukaryotes consisting of DNA segment
wrapped around eight histone proteins.
Lagging Strand A single discontinuous DNA strand, during DNA replication it is replicated from 5’ to 3’
direction, containing Okazaki fragments.
Splicing The process of removing introns then fusing exons in a precursor m-RNA transcript.
Silent Mutation A mutation in the nucleotide sequence that doesn’t affect the amino acid making up
the gene.

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 ▪ Name one difference between eukaryotes and prokaryotes in the following:

Process Eukaryotes Prokaryotes

Replication Multiple origins of replication
Transcription 1. Initiation requires transcription
factors
2. Takes place in the nucleus
Translation 1. Occurs in 80s ribosome
2. m-RNA – Monocistronic
Single origin of replication
1. Initiation requires no transcription
factors.
2. Takes place in the cytoplasm
1. Occurs in 70s ribosome
2. m-RNA - Polycistronic

▪ Match each item in Column A with the item in Column B, that it is most closely associated
with, each answer may only be used once:

Column A Column B
28S RNA Silent mutation
7-Methyl Guanosine m-RNA Cap
AUG Initiation codon
CAAT Promoter region
cDNA A collection of cloned fragments only representing the exons.
CRP / CAP Binds to promoter with cAMP
eIF-3 Ribosome subunit, antiassociation binding to 40S subunit.
GAATTC Palindrome recognized by EcoRi
Histones Basic proteins that help in packaging of eukaryotic DNA
mRNA Leading Strand
Nucleosome The lowest DNA packaging level
Okazaki Fragment Lagging Strand
Operator Binds repressor molecule
PCR Amplify specific DNA sequences
Peptidyl transferase (PTC) Catalyses addition of amino acid residue
Promoter A sequence in DNA that directs RNA synthesis by binding RNA Polymerase
Relief of stress in DNA Topoisomerase
RFLP Genetic test to determine paternity
Rho factor Termination of transcription
snRNP / Snurps Splicing
Telomerase Adds chromosomal ends
tRNA CCA Sequence
UAG, UAA, UGA Termination Codon
Large Ribosomal Unit Contains peptidyl transferase in eukaryotes
Dideoxy nucleotides DNA Sequencing
GEF
Cyclohexamide Inhibits protein synthesis
eIF-2 Binds 40S Subunit
➢ Red are the ones I am not sure about.

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 ▪ What is the function of the following enzymes?

Enzyme Function
Helicase Unwinds the DNA strands.
Topoisomerase Solves supercoiling and supertwisting during replication.
Primase Synthesis of a RNA primers during DNA synthesis.
Ligase Seals the gaps during excision of RNA primer and replacement by DNA
DNA Main enzyme in DNA replication.
Polymerase III
SSDBP Prevent reannealing of DNA strands during replication.

Reverse Enzyme used to make DNA copies of RNA

Transcriptase

▪ Consequences of point mutation:

1. Silent Mutation (Mutation in nucleotide sequence that doesn’t affect amino acid)
2. Missense Mutation (Mutation in nucleotides that affect the amino acid)
3. Non-sense Mutation (Mutation in nucleotide sequence that gives a stop codon)
▪ Give two examples of the following:
- Posttranscriptional Modifications:
1. Adding 7-methylguanosine 5’ Cap
2. Removal of Introns & fusion of Exons.
3. Adding Poly A at 3’ as a tail.
- Posttranslational Modifications:
1. Proteolytic Cleavage
2. Glycosylation
3. Acylation
4. Methylation
5. Phosphorylation
6. Sulfation
7. Ubiquitination
- TIP: Memorize 3.
▪ List four characteristics of the genetic code explaining each one:
A. Universal: All living organisms use the same genetic code.
B. Triplet Code: Codon of 3 nucleotides → 43 = 64, there are 61 codons, each codon consists of
3 bases, remaining 3 are nonsense (stop) codons, they don’t code for amino acids.
C. Degeneracy: More than one codon can code for a single amino acid.
D. Unambiguous: A single codon can only code for a single amino acid.
E. Non-overlapping: A base cannot be read twice.
F. No Punctuations: There are no gaps between codons.

▪ Mention four of the required components of replication in Eukaryotes:

1. Substrates
2. Template
3. Primer
4. Enzymes

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 ▪ What are the different types of RNA polymerases in eukaryotes and what’s their function:
Type Function
RNA Polymerase 1 Synthesis of r-RNA & 28S, 18S and 5.8S subunits.
RNA Polymerase 2 Synthesis of m-RNA
RNA Polymerase 3 Synthesis of t-RNA

▪ List different types of DNA polymerase in eukaryotes with their function:

Type Function
DNA Polymerase Synthesis of r-RNA & 28S, 18S and 5.8S subunits.
Alpha
DNA Polymerase Synthesis of m-RNA
Beta
DNA Polymerase Synthesis of t-RNA
Gamma

▪ Enzymes required in DNA replication:

1. DNA Polymerase
2. Helicase
3. Topoisomerase
4. Primase
5. Ligase
6. Single Strand Binding Proteins

▪ Initiation site of transcription in prokaryotes and eukaryotes is called:

A. Pribnow Box (TATAAT) in prokaryotes.
B. TATA Box in eukaryotes

▪ NOTE: 4 ATP is required for the synthesis of one peptide bond in protein synthesis.

▪ List four posttranscriptional modifications in the following:

Compound Modifications
m-RNA 1. Adding 7-methylguanosine 5’ cap
2. Splicing introns and fusing exons.
3. Adding Poly A 3’ tail
t-RNA 1. RNA splicing of introns
2. Extra nucleotides at both 5’ and 3’ ends are
cleaved
3. CCA sequences is added at 3’ end
r-RNA 1. RNA Splicing

▪ What is the function of the following?

Compound Function
m-RNA Acts as a messenger to carry the genetic info transcribed from DNA to the ribosomes
where it acts as a template for the synthesis of protein.
t-RNA Connects to m-RNA to decode the RNA sequence into proteins.
r-RNA Forms part of the ribosome, and catalyses the steps of protein synthesis.
Poly A Protects the 3’ end of the strand from exonucleases.

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 Cases:
• Carbohydrates:
▪ Q1. A patient has a history consistent with hypoglycaemia that is relieved by eating, and he
metabolizes fat normally (there’s no ketosis), although alanine fails to increase his blood
glucose levels, fructose or glycerol administration restores blood glucose to normal, which of
the following liver enzymes is defective?

A. Glucose 6 Phosphatase
B. Fructose 1,6 Bisphosphatase
C. PEP Carboxykinase
D. Aldolase B
- Explanation: Von Gierke’s Disease, a glycogen storage disease is caused by the deficiency of
G6-phosphatase, this leads to

• Protein:
▪ Q. A 17 days old neonate was brought to the paediatric clinic because of strange mousy odor
in urine and eczema for the last two weeks, 2 days ago he developed seizures (convulsions).
Urine was investigated and was found to be positive for aromatic keto-acids. An inborn error
of amino acid metabolism was suspected.

- Diagnosis: Phenylketonuria (PKU)

- Mention two abnormalities in urine:
A. Phenylalanine, Phenylpyruvate
- What is the deficient enzyme in this case:
A. Phenylalanine Dehydrogenase

▪ The net energy yield by utilization of acetoacetate by the nervous system as an alternative
energy source is:
A. ATP = 23, since the first step requires 1 ATP, and it’s transformed into 2 acetyl-CoA, which
gives us 24 ATP – 1 = 23.

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 ▪ A 3-month-old female infant seemed normal until she developed seizures. She had lactic
acidosis and an elevated plasma pyruvate level. Plasma alanine concentration was high, and
alanine load failed to induce a normal gluconeogenic response. Pyruvate carboxylase activity
measured using cultured fibroblasts was found to be less than normal. Fibroblasts from the
patient also accumulated five times greater than normal amounts of lipids.
- Q. What is the metabolic function of pyruvate carboxylase?
A. Converts pyruvate into oxaloacetate directly.
- Q. Explain the failure of alanine load to induce gluconeogenesis in the patient:
A. Due to the conversion of alanine to pyruvate, and the pyruvate carboxylase will lead to
no result.
- Q. Why did lipids accumulate excessively in the patient’s fibroblasts?
A. Pyruvate will bypass, and become acetyl-CoA, will become triacylglycerol.
- Q. Glutamine greatly stimulated the growth of fibroblasts from this patient. Explain why?
A. Accumulation of alanine will lead to transamination of glutamate, then glutamate with
ammonia will provide glutamine, during starvation fibroblasts increase.

▪ A new-born present with severe acidosis, vomiting, hypotonia and neurologic deficits. Serum
analysis reveals elevated levels of lactate and alanine. These observations suggest a
deficiency in which of the following enzymes? Explain:
A. Pyruvate Dehydrogenase, since they don’t have hypoglycemia which would suggest
pyruvate carboxylase, but there’s no hypoglycemia.

▪ The concentration of TCA cycle intermediates can be reduced under certain conditions.
Consider a patient who initiates taking barbiturates (Barbiturates are metabolized via
cytochrome P450 enzymes, which are induced by their substrates) During the initial phase of
his taking this drug, which TCA cycle intermediate is reduced in concentration? Explain:
▪ A. Alpha Ketoglutarate, barbiturate inhibits complex 1 in the ETC, complex 1 is responsible of
reduction of NADH, so it will be inhibited, thus it won’t work in the TCA cycle, the first step that
utilizes NADH is isocitrate dehydrogenase, in this case, NADH is absent, so alpha ketoglutarate
won’t be produced.

• Lipid
▪ Q. Liver fatty oxidation leads to an enhancement of gluconeogenesis via which of the
following? Explain:
A. Activation of pyruvate carboxylase, it increases the levels of Acetyl-CoA, and Acetyl-CoA
is an activator of pyruvate carboxylase.

▪ A 57-year-old man has been taking low-dose aspirin to reduce his risk of heart disease. He
adds phytosterols to his daily regime. ( N.B. Plant sterols interfere with cholesterol
absorption in the intestine) Which of the following is likely to be true? Explain.
A. To reduce circulating cholesterol levels, phytosterols inhibit cholesterol absorption in
the intestine

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