What is the end product of purine metabolism in humans?
Rate limiting step in pyrimidine synthesis?
Hereditary orotic aciduria Type-I is due to deficiency of?
Which of the following molecular interactions are found in the structure of DNA?
Which enzyme polymerises Okazaki fragments?
Which type of DNA polymerase is responsible for the replication of mitochondrial DNA?
Which type of RNA contains codons for specific amino acids?
Which type of RNA is most commonly associated with pseudouridine?
In eukaryotic cells, where does the majority of functional RNA activity occur?
Which of the following is NOT a characteristic of the genetic code?
NEET-PG 2013 - Biochemistry NEET-PG Practice Questions and MCQs
Question 71: What is the end product of purine metabolism in humans?
- A. Uric acid (Correct Answer)
- B. Carbon Dioxide
- C. Allantoin
- D. None of the options
Explanation: ***Uric acid*** - **Uric acid** is the final breakdown product of **purine metabolism** in humans. - It is formed from the degradation of **adenosine** and **guanosine**, with xanthine oxidase playing a key role in its synthesis. *Allantoin* - **Allantoin** is the end product of **purine metabolism** in most mammals other than primates, as they possess the enzyme **uricase** to further break down uric acid. - Humans lack **uricase**, hence allantoin is not the end product in humans. *Carbon Dioxide* - **Carbon dioxide** is a major end product of **carbohydrate** and **fat metabolism** through cellular respiration. - It is not directly associated with the degradation pathway of purines. *None of the options* - This option is incorrect because **uric acid** is indeed the definitive end product of purine metabolism in humans.
Question 72: Rate limiting step in pyrimidine synthesis?
- A. Aspartate transcarbamoylase (ATCase)
- B. Dihydroorotate dehydrogenase
- C. Dihydro-orotase
- D. Carbamoyl phosphate synthase-II (Correct Answer)
Explanation: ***Carbamoyl phosphate synthetase II (CPS-II)*** - **CPS-II** is the **committed and rate-limiting enzyme** in **de novo pyrimidine synthesis** in **mammals (including humans)** - It catalyzes the formation of **carbamoyl phosphate** from glutamine, CO₂, and 2 ATP in the **cytoplasm** - This is the **first committed step** and the main **regulatory checkpoint**, inhibited by UTP (feedback inhibition) and activated by PRPP and ATP - CPS-II is part of the **CAD complex** (carbamoyl phosphate synthetase, aspartate transcarbamoylase, dihydroorotase) in mammals *Aspartate transcarbamoylase (ATCase)* - ATCase catalyzes the **second step**: condensation of carbamoyl phosphate with aspartate to form carbamoyl aspartate - While ATCase is the **rate-limiting step in bacteria** (E. coli), in **mammals** it is part of the CAD complex and **not the primary regulatory step** - This option is incorrect for human/mammalian biochemistry tested in NEET PG *Dihydro-orotase* - The **third enzyme** in the pathway, converting carbamoyl aspartate to dihydroorotate - Part of the CAD complex in mammals but **not the rate-limiting step** *Dihydroorotate dehydrogenase* - Catalyzes the **fourth step**: oxidation of dihydroorotate to orotate - Located on the **outer surface of the inner mitochondrial membrane** (only mitochondrial enzyme in the pathway) - Important enzyme but **not rate-limiting**
Question 73: Hereditary orotic aciduria Type-I is due to deficiency of?
- A. Orotate phosphoribosyl transferase
- B. UMP synthase (Correct Answer)
- C. Orotic acid decarboxylase
- D. All of the options
Explanation: ***UMP synthase*** - Hereditary orotic aciduria Type-I is caused by a deficiency of the **bifunctional enzyme UMP synthase** (also called UMP synthase complex). - UMP synthase catalyzes two sequential reactions in the *de novo* pyrimidine synthesis pathway: 1. **OPRT activity**: Converts orotate → orotidine 5'-monophosphate (OMP) 2. **ODC activity**: Converts OMP → uridine 5'-monophosphate (UMP) - This is the **most precise and complete answer** as it identifies the actual enzyme complex that is deficient. - **Clinical features**: Megaloblastic anemia, growth retardation, immunodeficiency; responds to oral uridine supplementation. *Orotate phosphoribosyl transferase* - This represents only **one of the two catalytic activities** of the UMP synthase enzyme (the first step). - While this activity is indeed deficient in Type-I orotic aciduria, naming only this activity is **incomplete** because the enzyme has two functions. - This would be a **partial answer** rather than the complete enzyme name. *Orotic acid decarboxylase* - This represents only **the second catalytic activity** of the UMP synthase enzyme (converts OMP to UMP). - Like OPRT, this activity is also deficient, but naming only this component is **incomplete**. - **Type II orotic aciduria** (extremely rare) involves isolated ODC deficiency without OPRT deficiency. *All of the options* - While technically both OPRT and ODC activities are affected in Type-I orotic aciduria, the **standard nomenclature** refers to the deficient enzyme as **"UMP synthase"** - the name of the complete bifunctional enzyme. - In medical terminology and examination context, we identify enzyme deficiencies by the **name of the enzyme complex**, not by listing all its individual catalytic activities. - Therefore, **"UMP synthase"** is the single most accurate and complete answer.
Question 74: Which of the following molecular interactions are found in the structure of DNA?
- A. Hydrogen bond
- B. Glycosidic bond
- C. Covalent interactions
- D. All of the options (Correct Answer)
Explanation: ***All of the options*** - All three types of molecular interactions listed are present in DNA structure, making this the correct answer. - **Hydrogen bonds** hold together the two strands of the DNA double helix, forming between complementary base pairs (A-T with 2 hydrogen bonds, G-C with 3 hydrogen bonds). - **Glycosidic bonds** (N-glycosidic bonds) link the nitrogenous bases to the C1' carbon of the deoxyribose sugar in each nucleotide. - **Covalent interactions** (phosphodiester bonds) form the strong, stable sugar-phosphate backbone by linking the 3' hydroxyl group of one sugar to the 5' phosphate group of the next. *Hydrogen bond* - This is a **true statement** - hydrogen bonds are essential structural components of DNA. - However, this option alone is **incomplete** as DNA structure also contains glycosidic bonds and covalent phosphodiester bonds. - If only hydrogen bonds were present, there would be no nucleotides or backbone structure. *Glycosidic bond* - This is a **true statement** - glycosidic bonds are present in every nucleotide of DNA. - However, this option alone is **incomplete** as DNA also requires hydrogen bonds for base pairing and phosphodiester bonds for the backbone. - Without other bonds, individual nucleotides could not form a functional double helix. *Covalent interactions* - This is a **true statement** - covalent phosphodiester bonds form the DNA backbone within each strand. - However, this option alone is **incomplete** as it doesn't account for glycosidic bonds (nucleotide formation) or hydrogen bonds (strand pairing). - While the strongest bonds in DNA, they alone cannot create the complete double helix structure.
Question 75: Which enzyme polymerises Okazaki fragments?
- A. DNA polymerase I
- B. DNA polymerase II
- C. DNA polymerase III (Correct Answer)
- D. RNA polymerase
Explanation: ***DNA polymerase III*** - **DNA polymerase III** is the primary replicative enzyme in **prokaryotes (bacteria)** responsible for synthesizing new DNA strands, including the **polymerization of Okazaki fragments** on the lagging strand. - It possesses high processivity (can add ~500 nucleotides without dissociating), essential for rapid and efficient DNA synthesis during replication, adding nucleotides in a **5' to 3' direction**. - In **eukaryotes**, DNA polymerase δ (delta) performs the analogous function of polymerizing Okazaki fragments. *DNA polymerase I* - **DNA polymerase I** in prokaryotes primarily functions in **removing RNA primers** left by primase and **filling the resulting gaps** with DNA nucleotides. - It has 5' to 3' exonuclease activity for primer removal and polymerase activity for gap filling, but is **not the main enzyme for elongating Okazaki fragments**. - Its role is in **DNA repair and finishing replication**, not the extensive synthesis of Okazaki fragments. *DNA polymerase II* - **DNA polymerase II** in prokaryotes is primarily involved in **DNA repair mechanisms**, particularly in **restarting stalled replication forks** and responding to DNA damage. - It is not the main enzyme responsible for the polymerization of **Okazaki fragments** during normal DNA replication. *RNA polymerase* - **RNA polymerase** (specifically **primase**, a specialized RNA polymerase) synthesizes short **RNA primers** (8-12 nucleotides) during DNA replication, which provide the 3'-OH group necessary to initiate DNA synthesis. - It does not synthesize DNA or polymerize **Okazaki fragments**; its function is to create RNA primers, not extend DNA strands.
Question 76: Which type of DNA polymerase is responsible for the replication of mitochondrial DNA?
- A. DNA polymerase delta
- B. DNA polymerase alpha
- C. DNA polymerase gamma (Correct Answer)
- D. DNA polymerase beta
Explanation: ***DNA polymerase gamma*** - **DNA polymerase gamma** is the sole DNA polymerase responsible for replicating and repairing the mitochondrial DNA in eukaryotic cells. - It consists of a large catalytic subunit and two smaller accessory subunits that provide **proofreading** and processivity functions. *DNA polymerase alpha* - **DNA polymerase alpha** is primarily involved in initiating DNA replication on both the leading and lagging strands of nuclear DNA. - It forms a complex with **primase** to synthesize short RNA primers followed by a short stretch of DNA. *DNA polymerase delta* - **DNA polymerase delta** is a key enzyme in nuclear DNA replication, primarily responsible for the **elongation of the lagging strand**. - It also plays a significant role in various DNA repair pathways, including **nucleotide excision repair**. *DNA polymerase beta* - **DNA polymerase beta** is mainly involved in **DNA repair processes**, specifically **base excision repair (BER)** in the nucleus. - It has a low processivity and lacks **proofreading activity**, making it unsuitable for bulk DNA replication.
Question 77: Which type of RNA contains codons for specific amino acids?
- A. Transfer RNA (tRNA)
- B. Messenger RNA (mRNA) (Correct Answer)
- C. Small nuclear RNA (snRNA)
- D. Ribosomal RNA (rRNA)
Explanation: ***Messenger RNA (mRNA)*** - **mRNA** carries the genetic information from **DNA** in the nucleus to the **ribosomes** in the cytoplasm. - This information is encoded in sequences of three nucleotides called **codons**, each specifying a particular amino acid. *Transfer RNA (tRNA)* - **tRNA** molecules are responsible for **carrying specific amino acids** to the ribosome during protein synthesis. - Each **tRNA** has an **anticodon** that base-pairs with a complementary **codon** on the **mRNA** strand. *Small nuclear RNA (snRNA)* - **snRNA** is primarily involved in **RNA splicing**, a process that removes introns from pre-mRNA. - It forms part of the **spliceosome** complex, which is crucial for mature mRNA formation but does not contain codons itself. *Ribosomal RNA (rRNA)* - **rRNA** is a major component of **ribosomes**, the cellular machinery responsible for protein synthesis. - While it plays a critical structural and catalytic role in translation, it does not carry genetic code in the form of codons.
Question 78: Which type of RNA is most commonly associated with pseudouridine?
- A. messenger RNA (mRNA)
- B. ribosomal RNA (rRNA)
- C. transfer RNA (tRNA) (Correct Answer)
- D. DNA
Explanation: ***Transfer RNA (tRNA)*** - **Pseudouridine (ψ)** is one of the most abundant modified nucleosides in RNA, and **tRNA contains the highest proportion** of pseudouridine modifications among all RNA types. - **tRNA molecules can contain up to 10-15% modified bases**, with pseudouridine being particularly abundant in the **TψC arm** (thymine-pseudouridine-cytosine loop). - These modifications are critical for **tRNA stability, proper folding, and accurate codon-anticodon recognition** during translation. - Pseudouridine enhances base stacking and stabilizes RNA structure through additional hydrogen bonding capability. *Ribosomal RNA (rRNA)* - While rRNA does contain pseudouridine modifications, they are present in **lower proportions compared to tRNA**. - rRNA pseudouridine modifications do play important roles in **ribosomal assembly and function**, but tRNA remains the RNA type most commonly associated with this modification. *Messenger RNA (mRNA)* - **mRNA is generally much less modified** than tRNA or rRNA. - Pseudouridine modifications in mRNA are relatively rare in prokaryotes and were only recently discovered to be more common in eukaryotic mRNA. - When present, they may affect **mRNA stability and translation efficiency**. *DNA* - **DNA does not contain pseudouridine** as this is an RNA-specific modification. - Pseudouridine is formed by **post-transcriptional isomerization** of uridine residues in RNA.
Question 79: In eukaryotic cells, where does the majority of functional RNA activity occur?
- A. Nucleus
- B. Ribosome
- C. Cytoplasm (Correct Answer)
- D. None of the options
Explanation: ***Cytoplasm*** - The **cytoplasm** is the cellular compartment where the **majority of functional RNA activity** occurs, including **translation** (protein synthesis) involving mRNA, tRNA, and rRNA. - **Ribosomes** (the sites of translation) are located in the cytoplasm, either free-floating or bound to the endoplasmic reticulum. - Many types of **regulatory RNAs** such as microRNAs (miRNAs) and small interfering RNAs (siRNAs) exert their functions in the cytoplasm by targeting mRNAs for degradation or translational repression. - **mRNA degradation** and **RNA interference pathways** primarily operate in the cytoplasm. - The question asks for the broader location rather than the specific molecular machinery, making cytoplasm the most comprehensive answer. *Nucleus* - While RNA is **transcribed** from DNA and **processed** (capping, polyadenylation, splicing) in the nucleus, these are preparatory steps. - The nucleus is primarily the site of **RNA synthesis**, not where most RNA performs its functional roles. - Only a small fraction of functional RNA activity (like rRNA processing in the nucleolus) occurs here compared to the cytoplasm. *Ribosome* - While **ribosomes are the specific sites of translation** and are composed of rRNA and proteins, they represent molecular machinery rather than a cellular location. - Ribosomes themselves are located **within the cytoplasm**, making cytoplasm the more inclusive answer for where RNA activity occurs. - The question asks "where" in terms of cellular compartment, not which molecular complex. *None of the options* - This is incorrect as the cytoplasm is indeed the primary site where the majority of functional RNA activities occur in eukaryotic cells.
Question 80: Which of the following is NOT a characteristic of the genetic code?
- A. Overlapping (Correct Answer)
- B. Universal
- C. Degeneracy
- D. Nonambiguous
Explanation: ***Overlapping*** - The genetic code is generally **non-overlapping**, meaning each nucleotide is part of only one codon, and codons are read sequentially. - An overlapping code would mean that a single nucleotide could be part of multiple codons, which is not how protein synthesis typically occurs. *Nonambiguous* - This statement IS a characteristic; each codon specifies **only one amino acid**, meaning there is no ambiguity about which amino acid will be added. - While multiple codons can specify the same amino acid, a single codon never specifies more than one different amino acid. *Universal* - This statement IS a characteristic; the genetic code is largely **universal** across almost all organisms, from bacteria to humans. - The same codons typically specify the same amino acids in different species, which supports the idea of common ancestry. *Degeneracy* - This statement IS a characteristic; the genetic code is **degenerate**, meaning that most amino acids are specified by more than one codon. - This redundancy helps protect against the effects of single-nucleotide mutations.