NEET-PG 2012 - Biochemistry Practice Questions

Q: Which of the following is an ω-6 fatty acid?

Linoleic acid. ***Linoleic acid*** - **Linoleic acid** (LA), an 18-carbon fatty acid with two double bonds (18:2), is classified as an **ω-6 fatty acid** because its first double bond is located at the sixth carbon atom from the methyl end of the fatty acid chain. - It is an **essential fatty acid** that must be obtained through diet, serving as a precursor for other ω-6 fatty acids like arachidonic acid. *Cervonic acid* - **Cervonic acid** is another name for **docosahexaenoic acid (DHA)**, which is an **ω-3 fatty acid** (22:6). - Its first double bond is located at the third carbon from the methyl end. *Alpha linolenic acid* - **Alpha-linolenic acid** (ALA) is an **ω-3 fatty acid** (18:3). - Its first double bond is located at the third carbon atom from the methyl end. *Elaidic acid* - **Elaidic acid** is a **trans fatty acid** (18:1 trans-9). - It is classified as an **ω-9 fatty acid** due to the position of its double bond, but its trans configuration is the primary distinguishing feature.

Q: What is the primary function of a primer in DNA replication?

Initiation of DNA replication. ***Initiation of DNA replication*** - DNA polymerase cannot synthesize new DNA strands de novo; it requires a pre-existing 3'-hydroxyl group to begin adding nucleotides. - The **primer**, a short RNA sequence, provides this necessary **3'-hydroxyl group**, allowing DNA polymerase to start synthesizing the new DNA strand. *Transcription* - This process involves synthesizing **RNA from a DNA template**, primarily carried out by **RNA polymerase**. - While primers are involved in DNA synthesis, they do not directly initiate the process of transcription. *Translation* - **Translation** is the process of synthesizing **proteins from mRNA templates** using ribosomes, tRNA, and amino acids. - This process is distinct from DNA synthesis and does not involve primers; its initiation involves start codons and ribosomal subunits. *Termination of DNA replication* - **Termination of DNA replication** occurs when replication forks meet or at specific termination sequences, often with the involvement of specialized proteins. - Primers are involved in the *start* of replication, not its conclusion.

Q: Which of the following is not a precursor in the synthesis of pyrimidines?

Thymidine. ***Thymidine*** - **Thymidine** is a *nucleoside* consisting of deoxyribose and thymine. It is a *product* and a component of DNA, not a precursor in the *de novo synthesis* of pyrimidine bases. - While it can be incorporated into DNA via the *salvage pathway*, it does not serve as an initial building block for the pyrimidine ring itself. *Glutamine* - **Glutamine** provides the **nitrogen atoms** crucial for the formation of the pyrimidine ring, specifically N3 in the pyrimidine base. - It is a key donor of *amino groups* in various anabolic pathways, including nucleotide synthesis. *Carbon dioxide (CO2)* - **Carbon dioxide (CO2)** contributes one of the carbon atoms (C2) to the pyrimidine ring. - It combines with **ammonia** (derived from glutamine) to form **carbamoyl phosphate**, an essential intermediate. *Aspartic acid* - **Aspartic acid** provides four atoms (N1, C4, C5, C6) of the pyrimidine ring. - Its carbon skeleton and amino group are directly incorporated into the pyrimidine structure during the *de novo synthesis* pathway.

Q: What is the rate-controlling enzyme of fatty acid synthesis?

Acetyl-CoA carboxylase. ***Acetyl-CoA carboxylase*** - **Acetyl-CoA carboxylase (ACC)** catalyzes the committed step in fatty acid synthesis, converting **acetyl-CoA** to **malonyl-CoA**. - This enzyme is subject to both allosteric regulation (e.g., activation by **citrate** and inhibition by **long-chain fatty acyl-CoA**) and hormonal regulation (e.g., phosphorylation by glucagon and dephosphorylation by insulin). *Thioesterase* - **Thioesterase** is the enzyme responsible for releasing the completed fatty acid chain from the **fatty acid synthase complex**. - While essential for the termination of synthesis, it does not regulate the initiation or overall rate of the pathway. *Transacetylase* - **Transacetylase** (specifically, acetyl-CoA-ACP transacetylase and malonyl-CoA-ACP transacetylase) is involved in transferring acetyl and malonyl groups to the **acyl carrier protein (ACP)** within the fatty acid synthesis complex. - This is an intermediary step, but not the primary **rate-controlling** or committed step. *Ketoacyl synthase* - **Ketoacyl synthase (or β-ketoacyl-ACP synthase)** is responsible for condensing the growing acyl chain with malonyl-ACP, leading to the formation of a **β-ketoacyl-ACP**. - This is a crucial chain elongation step within the fatty acid synthase complex, but not the enzyme that controls the overall commitment to fatty acid synthesis.

Q: Which of the following statements about protein denaturation is correct?

The primary structure of the protein is unaffected.. ***The primary structure of the protein is unaffected.*** - Denaturation refers to the disruption of a protein's **secondary, tertiary, and quaternary structures**, while the **covalent peptide bonds** that form the primary structure remain intact. - The sequence of amino acids, which defines the primary structure, is not typically altered by denaturing agents such as heat, pH changes, or chemicals. *Biological properties are retained after denaturation.* - Denaturation typically leads to the **loss of a protein's specific three-dimensional shape**, which is essential for its biological function. - Therefore, the biological properties and **activity of the protein are usually lost** or significantly impaired upon denaturation. *Denaturation is always irreversible.* - While many cases of denaturation are irreversible (e.g., cooking an egg), some proteins can **renature** if the denaturing conditions are removed, restoring their original structure and function. - This reversibility depends on the **severity and duration of the denaturing agent**, as well as the protein's inherent stability. *Denaturation never results in proteins becoming insoluble.* - Denaturation often exposes **hydrophobic regions** of a protein that were previously buried within its folded structure, leading to aggregation and **precipitation**, thereby making the protein insoluble. - This insolubility is a common consequence of denaturation, particularly with significant structural disruption.

Q: What coenzyme is required by gulonate dehydrogenase for its activity?

NAD. ***NAD*** - **Gulonate dehydrogenase** is an enzyme involved in the **uronic acid pathway**, specifically in the conversion of **L-gulonate to D-xylulose**. - This reaction is an **NAD-dependent oxidation**, meaning **NAD** acts as the electron acceptor, being reduced to **NADH**. *NADP* - **NADP** (nicotinamide adenine dinucleotide phosphate) is primarily involved in **anabolic pathways** like **fatty acid synthesis** and the **pentose phosphate pathway**, often in reduction reactions where it is converted to **NADPH**. - While structurally similar to NAD, it is generally not the direct coenzyme for gulonate dehydrogenase. *FAD* - **FAD** (flavin adenine dinucleotide) is a coenzyme derived from **riboflavin** (vitamin B2) and is typically involved in **redox reactions** where it repeatedly accepts and donates electrons, often in dehydrogenase reactions involving **carbon-carbon double bonds**. - Enzymes like **succinate dehydrogenase** (in the citric acid cycle) or acyl-CoA dehydrogenase (in fatty acid oxidation) utilize FAD, but not gulonate dehydrogenase. *FMN* - **FMN** (flavin mononucleotide) is another coenzyme derived from **riboflavin** and serves as a prosthetic group in various **flavoproteins**, often facilitating **single-electron transfers**. - It is frequently found in complexes like **NADH dehydrogenase** (Complex I of the electron transport chain) but is not the required coenzyme for gulonate dehydrogenase activity.

Q: Which of the following substances is not derived from tyrosine?

Nicotinic acid. ***Nicotinic acid*** - **Nicotinic acid** (niacin, vitamin B3) is synthesized from **tryptophan** in the body, not tyrosine. - It plays a crucial role in metabolism as a precursor for NAD+ and NADH, which are involved in various enzymatic reactions. *Thyroxine* - **Thyroxine** (T4), a thyroid hormone, is derived from the amino acid **tyrosine**. - **Iodine** is incorporated into tyrosine residues on thyroglobulin to form monoiodotyrosine (MIT) and diiodotyrosine (DIT), which then couple to form T4 (and T3). *Melanin* - **Melanin**, the pigment responsible for skin, hair, and eye color, is synthesized from **tyrosine** through a pathway involving the enzyme **tyrosinase**. - This process involves the hydroxylation of tyrosine to 3,4-dihydroxyphenylalanine (DOPA) and subsequent oxidation reactions. *Dopamine* - **Dopamine**, an important neurotransmitter, is synthesized from **tyrosine** in a two-step process in the brain and adrenal medulla. - Tyrosine is first hydroxylated to DOPA by **tyrosine hydroxylase**, and then DOPA is decarboxylated to dopamine by DOPA decarboxylase.

Q: Pantothenic acid is needed for donating the following moiety?

Acetyl group. ***Acetyl group*** - **Pantothenic acid** (vitamin B5) is a crucial component of **coenzyme A (CoA)**, which plays a central role in transferring **acetyl groups**. - This transfer is vital in numerous metabolic pathways, including the **Krebs cycle**, fatty acid synthesis, and fatty acid oxidation. *Carboxyl* - The transfer of **carboxyl groups** is typically mediated by a different coenzyme, **biotin** (vitamin B7), not pantothenic acid. - Biotin-dependent enzymes are involved in carboxylation reactions like those in gluconeogenesis and fatty acid synthesis. *Hydroxyl* - While hydroxyl groups are common in organic chemistry, pantothenic acid's primary role is not the donation of isolated **hydroxyl groups**. - Hydroxyl groups are often donated or accepted during redox reactions or hydrolysis, often by specific enzymes directly. *Amino* - The transfer of **amino groups** is primarily associated with **pyridoxal phosphate (PLP)**, the active form of vitamin B6. - PLP-dependent enzymes, such as **transaminases**, are critical for amino acid metabolism.

Q: What is the role of Apoprotein C-II in lipid metabolism?

Activates lipoprotein lipase. ***Activates lipoprotein lipase*** - **Apoprotein C-II (ApoC-II)** is a crucial **activator** of **lipoprotein lipase (LPL)**. - LPL is an enzyme responsible for **hydrolyzing triglycerides** from chylomicrons and VLDL, allowing fatty acids to be taken up by tissues. - **Deficiency of ApoC-II** leads to severe hypertriglyceridemia due to inability to activate LPL. *Inhibits lipoprotein lipase* - This is the function of **ApoC-III**, not ApoC-II. - ApoC-III **inhibits LPL activity**, which is the opposite role of ApoC-II. *Facilitates triglyceride transport* - While apoproteins are essential for **assembly and transport of lipoproteins** that carry triglycerides, this is not the specific primary role of ApoC-II. - ApoC-II's primary function is **regulating LPL enzyme activity**, not direct transport facilitation. *None of the options* - This is incorrect because ApoC-II clearly **activates lipoprotein lipase**, which is one of the given options.

Q: Acute intermittent porphyria is due to deficiency of?

Porphobilinogen deaminase. ***Porphobilinogen deaminase*** - **Acute intermittent porphyria (AIP)** results from a deficiency in **porphobilinogen deaminase** (also known as hydroxymethylbilane synthase). - This enzyme deficiency leads to the accumulation of **aminolevulinic acid (ALA)** and **porphobilinogen (PBG)**, which are neurotoxic and cause the characteristic symptoms of AIP. *Uroporphyrinogen III synthase* - A deficiency in **uroporphyrinogen III synthase** causes **congenital erythropoietic porphyria (Günther disease)**, which is characterized by severe photosensitivity and hemolytic anemia. - This enzyme defect leads to the accumulation of uroporphyrinogen I and coproporphyrinogen I, not the ALA and PBG associated with AIP. *Ferrochelatase* - Deficiency in **ferrochelatase** causes **erythropoietic protoporphyria (EPP)**, which presents with photosensitivity and chronic liver disease due to the accumulation of **protoporphyrin**. - This condition does not cause the acute neurological attacks seen in AIP. *ALA synthase* - **ALA synthase** is the **rate-limiting enzyme** in heme synthesis; while its activity is crucial, a congenital *deficiency* is not the cause of AIP. - Instead, the *upregulation* of ALA synthase activity in AIP (due to the PBG deaminase block) contributes to the accumulation of ALA and PBG.

Question 1

Which of the following is an ω-6 fatty acid?

Accepted Answer

Linoleic acid

Answer

Cervonic acid

Answer

Alpha linolenic acid

Answer

Elaidic acid

Question 2

What is the primary function of a primer in DNA replication?

Accepted Answer

Initiation of DNA replication

Answer

Transcription

Answer

Translation

Answer

Termination of DNA replication

Question 3

Which of the following is not a precursor in the synthesis of pyrimidines?

Accepted Answer

Thymidine

Answer

Glutamine

Answer

Carbon dioxide (CO2)

Answer

Aspartic acid

Question 4

What is the rate-controlling enzyme of fatty acid synthesis?

Accepted Answer

Acetyl-CoA carboxylase

Answer

Thioesterase

Answer

Transacetylase

Answer

Ketoacyl synthase

Question 5

Which of the following statements about protein denaturation is correct?

Accepted Answer

The primary structure of the protein is unaffected.

Answer

Biological properties are retained after denaturation.

Answer

Denaturation is always irreversible.

Answer

Denaturation never results in proteins becoming insoluble.

Question 6

What coenzyme is required by gulonate dehydrogenase for its activity?

Accepted Answer

NAD

Answer

FAD

Answer

FMN

Answer

NADP

Question 7

Which of the following substances is not derived from tyrosine?

Accepted Answer

Nicotinic acid

Answer

Thyroxine

Answer

Melanin

Answer

Dopamine

Question 8

Pantothenic acid is needed for donating the following moiety?

Accepted Answer

Acetyl group

Answer

Carboxyl

Answer

Hydroxyl

Answer

Amino

Question 9

What is the role of Apoprotein C-II in lipid metabolism?

Accepted Answer

Activates lipoprotein lipase

Answer

None of the options

Answer

Inhibits lipoprotein lipase

Answer

Facilitates triglyceride transport

Question 10

Acute intermittent porphyria is due to deficiency of?

Accepted Answer

Porphobilinogen deaminase

Answer

Uroporphyrinogen III synthase

Answer

Ferrochelatase

Answer

ALA synthase

NEET-PG 2012 — Biochemistry