Biochem FEEDs (2023) Flashcards
The enzyme HGPRT is found to be deficient. This will result in:
a. Increased synthesis of Krebs cycle intermediates
b. Activation of xanthine oxidase
c. Increased purine synthesis
d. Hyperuricemia
d. Hyperuricemia
Rationale: HGPRT (hypoxanthine-guanine phosphoribosyltransferase) is crucial for the salvage pathway of purines. A deficiency in HGPRT results in the accumulation of hypoxanthine and guanine, which are subsequently converted to uric acid, leading to hyperuricemia. This condition is associated with Lesch-Nyhan syndrome.
Deoxyribonucleotides are formed by reduction of:
a. Ribonucleosides
b. Ribonucleoside monophosphates
c. Ribonucleoside diphosphates
d. Ribonucleoside triphosphates
c. Ribonucleoside diphosphates
Rationale: Deoxyribonucleotides are synthesized from ribonucleoside diphosphates by the enzyme ribonucleotide reductase, which reduces the 2’-hydroxyl group of the ribose ring to a hydrogen atom, producing deoxyribonucleotides.
The action of allopurinol is best described as:
a. Competitive inhibition of xanthine oxidase
b. Inhibiting PRPP synthesis
c. Increasing the solubility of uric acid in plasma
d. Inhibiting leukocyte movement by affecting microtubule formation
a. Competitive inhibition of xanthine oxidase
Rationale: Allopurinol is a structural analog of hypoxanthine. It acts as a competitive inhibitor of xanthine oxidase, the enzyme responsible for converting hypoxanthine and xanthine to uric acid. This inhibition reduces uric acid production, helping to manage conditions like gout.
Which of the following is not a cause of gout?
a. Inefficient purine base salvage reactions
b. Increased PRPP synthetase activity
c. Overproduction of pyrimidine bases
d. von Gierke’s disease
c. Overproduction of pyrimidine bases
Rationale: Gout is caused by the accumulation of uric acid, which is a product of purine metabolism, not pyrimidine metabolism. The overproduction of pyrimidine bases does not contribute to gout.
Which of the following is absent in deoxyribonucleosides?
a. Phosphate group
b. 5-carbon sugar in pentose ring form
c. Purine or pyrimidine base
d. Glycosidic bond
a. Phosphate group
Rationale: Deoxyribonucleosides consist of a deoxyribose sugar attached to a purine or pyrimidine base via a glycosidic bond. They do not contain a phosphate group, which differentiates them from deoxyribonucleotides.
True of nitrogenous bases:
a. In nucleotides, they are attached to the phosphate by a phosphodiester bond
b. A prime (‘) symbol is used to define the carbon atoms in its ring
c. The N-9 atom of purines is linked to carbon 1 of the sugar
d. Nitrogenous base pairs are linked together by N-glycosidic bonds
c. The N-9 atom of purines is linked to carbon 1 of the sugar
Rationale: In nucleotides, the N-9 nitrogen of purine bases (adenine and guanine) is linked to the 1’ carbon of the sugar (ribose or deoxyribose) via an N-glycosidic bond. The other options are incorrect because (a) nitrogenous bases are attached to the sugar, not the phosphate, by a glycosidic bond, (b) the prime (‘) symbol is used to define carbon atoms in the sugar, not in the nitrogenous base, and (d) base pairs are linked together by hydrogen bonds, not N-glycosidic bonds.
PRPP acts as a substrate for:
a. Purine synthesis
b. Pyrimidine synthesis
c. Both Purine and pyrimidine synthesis
d. Neither purine nor pyrimidine synthesis
c. Both purine and pyrimidine synthesis
Rationale: PRPP (phosphoribosyl pyrophosphate) is a crucial substrate for the synthesis of both purine and pyrimidine nucleotides. It donates the ribose-phosphate group that is required for the formation of nucleotides.
True of dihydrofolate reductase:
a. It is inhibited by methotrexate
b. It catalyzes an ATP-requiring reaction
c. Its absence results in an accumulation of thymidine nucleotides
d. All of the above are true
a. It is inhibited by methotrexate
Rationale: Dihydrofolate reductase is an enzyme that catalyzes the reduction of dihydrofolate to tetrahydrofolate, a cofactor required for the synthesis of thymidine nucleotides. Methotrexate is a competitive inhibitor of this enzyme. The other options are incorrect as the reaction catalyzed by dihydrofolate reductase does not require ATP, and its absence results in a deficiency of thymidine nucleotides, not an accumulation.
Why are humans not affected by sulfonamides and trimethoprim?
a. Mammalian cells do not synthesize folate
b. Folate is not essential for DNA synthesis in humans
c. Humans can synthesize folate from PABA unlike microorganisms
d. Humans have enzymes that can digest sulfonamides and trimethoprim and render them inactive
a. Mammalian cells do not synthesize folate
Rationale: Sulfonamides and trimethoprim target bacterial folate synthesis. Humans obtain folate through their diet and do not synthesize it, rendering these drugs ineffective against human cells. Folate is essential for DNA synthesis in humans (b), humans cannot synthesize folate from PABA (c), and humans do not have enzymes that digest sulfonamides and trimethoprim (d).
A 50-pair DNA chain has 30 bases made up of thymine residues. How many guanine bases would you expect to see in this chain?
a. 10
b. 20
c. 30
d. 40
b. 20
Rationale: In a 50-pair DNA chain, there are 100 bases in total. Given that there are 30 thymine residues, there must be 30 adenine residues (as thymine pairs with adenine). This leaves 40 bases that must be cytosine and guanine. Since cytosine and guanine pair together in equal numbers, there must be 20 cytosine and 20 guanine bases.
Which of the following is an intracellular messenger?
a. cGMP
b. 6-mercaptopurine
c. ATP
d. UDP-glucose
a. cGMP
Rationale: cGMP (cyclic guanosine monophosphate) is a second messenger important in many biological processes. It is used for signal transduction in cells, particularly in processes such as vasodilation. The other options, such as 6-mercaptopurine, ATP, and UDP-glucose, have roles in metabolism and other cellular processes but are not typically classified as intracellular messengers.
What is the rate-limiting enzyme of pyrimidine synthesis?
a. PRPP synthetase
b. Carbamoyl phosphatase
c. Aspartate transcarbamoylase
d. Adenosine deaminase
b. Carbamoyl phosphatase
Rationale: The correct enzyme is actually carbamoyl phosphate synthetase II (CPS II), which catalyzes the formation of carbamoyl phosphate from glutamine and bicarbonate. This enzyme is the rate-limiting step in pyrimidine synthesis. The other enzymes listed are involved in different pathways.
The origin of replication is an area in the DNA strand where replication begins. Which statement regarding the origin of replication is true?
a. Prokaryotes have multiple origins of replication in one DNA strand
b. When the 2 strands separate from the origin of replication, a single replication fork is formed
c. The origin of replication is made up mostly of guanine-cytosine base pairs
d. The separation or melting of the strands is an ATP-dependent process
d. The separation or melting of the strands is an ATP-dependent process
Rationale: The process of strand separation at the origin of replication requires energy, which is provided by ATP hydrolysis. Prokaryotes typically have a single origin of replication per DNA molecule (a), two replication forks form at the origin (b), and the origin of replication is often rich in adenine-thymine base pairs, not guanine-cytosine (c), because A-T pairs are easier to separate.
True of the lagging strand:
a. Chain elongation occurs in the 3’→ 5’ direction
b. It is the strand that is being copied in the direction of the advancing replication fork
c. It is synthesized continuously as the replication fork advances
d. The enzyme responsible for joining its strands is DNA ligase
d. The enzyme responsible for joining its strands is DNA ligase
Rationale: The lagging strand is synthesized discontinuously in short fragments called Okazaki fragments. These fragments are later joined together by DNA ligase. Chain elongation on the lagging strand occurs in the 5’→ 3’ direction (a is incorrect). The lagging strand is synthesized in the direction opposite to the replication fork (b and c are incorrect).
This catalyzes DNA chain elongation:
a. DNA Polymerase I
b. DNA Polymerase III
c. Helicase
d. DNA Topoisomerase
b. DNA Polymerase III
Rationale: DNA Polymerase III is the primary enzyme responsible for DNA chain elongation during replication in prokaryotes. DNA Polymerase I is mainly involved in removing RNA primers and filling in the gaps, Helicase unwinds the DNA helix, and DNA Topoisomerase relieves the torsional strain ahead of the replication fork.
This type of DNA repair resolves pyrimidine dimers:
a. Nucleotide excision repair
b. Mismatch repair
c. Base excision repair
d. Double strand break repair
a. Nucleotide excision repair
Rationale: Nucleotide excision repair (NER) is the primary mechanism for repairing bulky lesions such as pyrimidine dimers caused by UV radiation. This process removes a short single-stranded segment containing the lesion and uses the complementary strand as a template for repair.
This is non-densely packed and transcriptionally active:
a. Euchromatin
b. Intron
c. Solenoid
d. Metaphase chromatid
a. Euchromatin
Rationale: Euchromatin is less densely packed than heterochromatin and is generally transcriptionally active, allowing for gene expression. The other options, such as introns, solenoids, and metaphase chromatids, do not describe a state of chromatin that is transcriptionally active.
Which of the following is responsible for the unwinding of double-stranded DNA?
a. DNA Helicase
b. DNA Ligase
c. DNA Topoisomerase
d. DNA Primase
a. DNA Helicase
Rationale: DNA helicase unwinds the double-stranded DNA during replication, creating the replication fork. DNA ligase joins Okazaki fragments on the lagging strand, DNA topoisomerase relieves torsional strain, and DNA primase synthesizes RNA primers.
How many percent of human DNA is made up of repetitive sequences?
a. 10%
b. 30%
c. 50%
d. 70%
b. 30%
Rationale: More than 50% of DNA in eukaryotic organisms is unique or non-repetitive sequences, while approximately 30% consists of repetitive sequences, such as centromeres, telomeres, and other repetitive elements.
In epigenetics, which of the following will give rise to a transcriptionally active chromosome?
a. DNA methylation
b. Histone acetylation
c. snRNA pairing
d. Telomerase signaling
b. Histone acetylation
Rationale: Histone acetylation is an epigenetic modification that relaxes chromatin structure, making it more accessible to transcription factors and thereby promoting gene expression. DNA methylation typically silences gene expression, snRNA pairing and telomerase signaling are not directly related to transcriptional activation.
A person ate mushrooms picked in a wooded area. Shortly thereafter, he was rushed to the hospital, where he died. He had no previous medical problems. Which stage of transcription was probably affected?
a. Initiation
b. Elongation
c. Termination
d. Post-transcriptional modification
a. Initiation
Rationale: Certain toxic mushrooms contain alpha-amanitin, a potent inhibitor of RNA polymerase II, which is essential for the initiation of transcription in eukaryotic cells. Inhibition of RNA polymerase II prevents the synthesis of mRNA, which is critical for protein production and cell survival.
This is required for transcription initiation:
a. Sigma factor
b. Rho factor
c. Spliceosome
d. RNA polymerase
d. RNA polymerase
Rationale: RNA polymerase is the enzyme responsible for synthesizing RNA from a DNA template. In prokaryotes, the sigma factor (a) is also essential for initiation, but RNA polymerase itself is required for the process in both prokaryotes and eukaryotes. The other options, Rho factor (b) and spliceosome (c), are involved in termination and RNA processing, respectively.
What is the metabolic fate of exons?
a. They are excised upon processing of heterogenous nuclear RNA (hnRNA) to messenger RNA (mRNA)
b. They are retained upon processing of ribosomal RNA and are converted to miRNA and siRNA
c. They are translated into mRNA sequences and participate in the synthesis of proteins
d. They are added to mRNA during the splicing reactions by the spliceosome to prevent mRNA digestion by exonucleases
c. They are translated into mRNA sequences and participate in the synthesis of proteins
Rationale: Exons are the coding sequences of a gene that are retained in the final mRNA product after RNA splicing. They are translated into protein sequences during translation. The other options are incorrect as exons are not excised (a), converted into miRNA or siRNA (b), or added to mRNA to prevent digestion (d).
Which of the following is a component of the 5’ cap?
a. 7-methylguanosine
b. Ribonuclease P
c. The sequence AAUAAA in the intron
d. Small nuclear ribonucleic acid (snRNA)
a. 7-methylguanosine
Rationale: The 5’ cap of eukaryotic mRNA consists of a 7-methylguanosine residue linked to the first nucleotide of the mRNA via a 5’-5’ triphosphate bridge. This modification is crucial for mRNA stability, nuclear export, and translation initiation. The other options are not components of the 5’ cap.