NEET-PG 2012 — Biochemistry
184 Previous Year Questions with Answers & Explanations
In apoptosis, cytochrome C acts through:
Which of the following enzymes does not catalyze a reaction that directly produces ATP via substrate-level phosphorylation?
The rate-limiting step in glycolysis is catalyzed by?
Which reaction requires Vitamin B1?
Cell-matrix adhesions are mediated by?
What are isoenzymes?
At which positions does pancreatic lipase hydrolyze the ester linkages of triacylglycerides?
Enzymes that move a molecular group from one molecule to another are known as -
Apoenzyme is ?
Enzyme causing covalent bond cleavage without hydrolysis ?
NEET-PG 2012 - Biochemistry NEET-PG Practice Questions and MCQs
Question 1: In apoptosis, cytochrome C acts through:
- A. FADD
- B. TNF
- C. Apaf1 (Correct Answer)
- D. Bcl-2
Explanation: ***Apaf1*** - Cytochrome C released from the mitochondria binds to **Apaf1**, which leads to the formation of the **apoptosome** [1][2]. - This complex activates **caspase-9**, initiating the caspase cascade that leads to apoptosis [2]. *TNF* - Tumor Necrosis Factor (TNF) is involved in **necrosis** and **inflammatory processes**, not directly in the intrinsic pathway of apoptosis. - It activates **caspase-8**, which is part of the **extrinsic pathway**, differing from the role of cytochrome C [1]. *FADD* - FADD (Fas-associated protein with death domain) is part of the **death receptor pathway**, linking to caspase-8, not associated with cytochrome C [1]. - It does not play a role in the assembly of the apoptosome like Apaf1 does. *Bcl_2* - Bcl-2 is an **anti-apoptotic protein** that inhibits apoptosis rather than inducing it or acting through cytochrome C [1]. - It functions by preventing the release of cytochrome C from mitochondria, thereby opposing the apoptotic process [1]. **References:** [1] Kumar V, Abbas AK, et al.. Robbins and Cotran Pathologic Basis of Disease. 9th ed. Neoplasia, p. 310. [2] Kumar V, Abbas AK, et al.. Robbins and Cotran Pathologic Basis of Disease. 9th ed. Cellular Responses to Stress and Toxic Insults: Adaptation, Injury, and Death, pp. 64-67.
Question 2: Which of the following enzymes does not catalyze a reaction that directly produces ATP via substrate-level phosphorylation?
- A. Pyruvate kinase
- B. Hexokinase (Correct Answer)
- C. Succinate thiokinase
- D. Phosphoglycerate kinase
Explanation: ***Correct: Hexokinase*** **Hexokinase** catalyzes the transfer of a phosphate group from **ATP to glucose**, producing **glucose-6-phosphate** and ADP. This step **consumes ATP** rather than producing it via substrate-level phosphorylation. **Substrate-level phosphorylation** directly synthesizes ATP from ADP by transferring a high-energy phosphate group from a phosphorylated substrate; hexokinase performs the **opposite reaction** (ATP consumption). *Incorrect: Pyruvate kinase* **Pyruvate kinase** catalyzes the transfer of a phosphate group from **phosphoenolpyruvate (PEP)** to ADP, forming **pyruvate** and ATP. This is a classic example of **substrate-level phosphorylation** in glycolysis, directly generating ATP. *Incorrect: Succinate thiokinase* **Succinate thiokinase** (also known as succinyl-CoA synthetase) catalyzes the conversion of **succinyl-CoA to succinate**, simultaneously forming **GTP** (or ATP in some organisms) from GDP (or ADP) and inorganic phosphate. The GTP produced can be converted to ATP through nucleoside diphosphate kinase, representing substrate-level phosphorylation in the TCA cycle. *Incorrect: Phosphoglycerate kinase* **Phosphoglycerate kinase** catalyzes the transfer of a phosphate group from **1,3-bisphosphoglycerate** to ADP, yielding **3-phosphoglycerate** and ATP. This is a key enzymatic step in glycolysis that directly produces ATP through **substrate-level phosphorylation**.
Question 3: The rate-limiting step in glycolysis is catalyzed by?
- A. Phosphofructokinase (Correct Answer)
- B. Enolase
- C. Glucokinase
- D. Pyruvate kinase
Explanation: ***Phosphofructokinase*** - **Phosphofructokinase-1 (PFK-1)** is the primary regulatory enzyme and **rate-limiting step** in glycolysis. - It catalyzes the irreversible phosphorylation of **fructose-6-phosphate to fructose-1,6-bisphosphate**, a crucial commitment step. *Enolase* - **Enolase** catalyzes the conversion of **2-phosphoglycerate to phosphoenolpyruvate** in glycolysis. - While essential for glycolysis, it is not the rate-limiting step. *Glucokinase* - **Glucokinase** catalyzes the phosphorylation of glucose to **glucose-6-phosphate** in the liver and pancreatic beta cells. - This is the first step in glycolysis but is not the rate-limiting step for the entire pathway once glucose has entered the cell. *Pyruvate kinase* - **Pyruvate kinase** catalyzes the final step of glycolysis, converting **phosphoenolpyruvate to pyruvate**. - Although it is a regulated enzyme, it is not the primary rate-limiting step that controls the overall flux through the glycolytic pathway.
Question 4: Which reaction requires Vitamin B1?
- A. None of the options
- B. Oxidative decarboxylation (Correct Answer)
- C. Carboxylation
- D. Transamination
Explanation: ***Oxidative decarboxylation*** - Vitamin B1, in its active form **thiamine pyrophosphate (TPP)**, is a crucial coenzyme for enzymes catalyzing **oxidative decarboxylation** reactions. - Key examples include the **pyruvate dehydrogenase complex** and **alpha-ketoglutarate dehydrogenase complex**, essential for cellular respiration and the citric acid cycle. *Transamination* - This type of reaction, involving the transfer of an **amino group**, primarily requires **pyridoxal phosphate (PLP)**, the active form of **Vitamin B6**. - It is vital for amino acid metabolism but does not utilize Vitamin B1. *Carboxylation* - **Carboxylation** reactions, which add a carboxyl group to a substrate, typically require **biotin** (Vitamin B7) as a coenzyme. - Examples include pyruvate carboxylase and acetyl-CoA carboxylase, which are not dependent on Vitamin B1. *None of the options* - As **oxidative decarboxylation** specifically requires Vitamin B1, this option is incorrect. - The other listed reactions depend on different vitamins as coenzymes.
Question 5: Cell-matrix adhesions are mediated by?
- A. Integrins (Correct Answer)
- B. Selectins
- C. Calmodulin
- D. Cadherins
Explanation: ***Integrins*** - **Integrins** are transmembrane receptors that mediate cell adhesion to the **extracellular matrix (ECM)**, linking it to the cell's cytoskeleton. - They bind to various ECM components like **fibronectin**, **collagen**, and **laminin**. *Cadherins* - **Cadherins** are primarily involved in **cell-to-cell adhesion**, forming junctions like **adherens junctions** and **desmosomes**. - They are **calcium-dependent adhesion molecules** that do not directly bind to the extracellular matrix. *Selectins* - **Selectins** are cell adhesion molecules involved in **leukocyte rolling** and **adhesion to endothelial cells** during inflammation. - They mediate **transient cell-to-cell interactions**, not cell-matrix adhesion. *Calmodulin* - **Calmodulin** is a **calcium-binding protein** that acts as a signal transducer, regulating various intracellular processes. - It is involved in **calcium-dependent signaling pathways** and enzyme activation, not cell adhesion.
Question 6: What are isoenzymes?
- A. Physically same forms of different enzymes
- B. Forms of same enzyme that catalyze different reactions
- C. Forms of different enzyme that catalyze same reactions
- D. Physically distinct forms of the same enzyme (Correct Answer)
Explanation: ***Physically distinct forms of the same enzyme*** - Isoenzymes are **multiple forms of an enzyme** that catalyze the **same reaction** but differ in their **physical or biochemical properties**, such as electrophoretic mobility, optimal pH, or kinetic parameters. - These differences usually arise from **genetic variations** (different genes encoding isoforms) or **post-translational modifications** (e.g., phosphorylation, glycosylation). *Physically same forms of different enzymes* - This statement is incorrect as isoenzymes are forms of the **same enzyme**, not different enzymes. - While different enzymes can catalyze similar reactions in certain pathways, they are not referred to as isoenzymes if they are structurally identical. *Forms of same enzyme that catalyze different reactions* - This describes enzymes with **broad substrate specificity** or those that act on different substrates but are not necessarily isoenzymes. - Isoenzymes specifically catalyze the **same chemical reaction**, but they may do so with different efficiencies or under different regulatory controls. *Forms of different enzyme that catalyze same reactions* - This describes a scenario where different enzymes might exhibit **catalytic promiscuity** or broad specificity, but not isoenzymes. - Isoenzymes are always derived from the **same parent enzyme** and catalyze the identical reaction.
Question 7: At which positions does pancreatic lipase hydrolyze the ester linkages of triacylglycerides?
- A. 1 and 2
- B. 2 and 3
- C. Only 3
- D. 1 and 3 (Correct Answer)
Explanation: **Correct: 1 and 3** - Pancreatic lipase specifically targets the **ester bonds at the sn-1 and sn-3 positions** (primary alcohol positions) on the glycerol backbone of triacylglycerides. - This positional specificity results in the formation of **2-monoacylglycerol (2-MAG)** and **two free fatty acids**. - This is the characteristic action of pancreatic triacylglycerol lipase during fat digestion in the intestinal lumen. *Incorrect: 1 and 2* - Hydrolysis at positions 1 and 2 would produce a 3-monoacylglycerol and free fatty acids, which is not the physiological product of pancreatic lipase. - The enzyme's positional specificity favors the outer sn-1 and sn-3 positions, not the middle sn-2 position. *Incorrect: 2 and 3* - Hydrolysis at positions 2 and 3 would yield a 1-monoacylglycerol and free fatty acids, which does not reflect pancreatic lipase activity. - The enzyme specifically spares the sn-2 position due to its structural specificity. *Incorrect: Only 3* - If only position 3 were hydrolyzed, the product would be a 1,2-diacylglycerol and one free fatty acid. - This represents incomplete hydrolysis; pancreatic lipase typically hydrolyzes **both outer positions (sn-1 and sn-3)** due to its regiospecificity.
Question 8: Enzymes that move a molecular group from one molecule to another are known as -
- A. Transferases (Correct Answer)
- B. Ligases
- C. Dipeptidases
- D. Oxido-reductases
Explanation: ***Transferases*** - **Transferases** are a class of enzymes that catalyze the transfer of a specific functional group (e.g., methyl, acetyl, phosphate) from one molecule (the donor) to another (the acceptor). - This broad category includes enzymes vital for many metabolic pathways, such as **kinases** (transferring phosphate groups) and **transaminases** (transferring amino groups). *Ligases* - **Ligases** are enzymes responsible for joining two large molecules together, typically by forming a new chemical bond. - This process usually involves the concomitant hydrolysis of a small, energy-rich molecule such as **ATP**, to provide the necessary energy for bond formation. *Dipeptidases* - **Dipeptidases** are a type of hydrolase enzyme that specifically cleaves the peptide bond within a **dipeptide**, releasing two free amino acids. - They are crucial for the final stages of protein digestion, breaking down small peptides into absorbable **amino acid units**. *Oxido-reductases* - **Oxido-reductases** are enzymes that catalyze **oxidation-reduction reactions** (redox reactions), where electrons are transferred from one molecule to another. - This class includes enzymes like **dehydrogenases** and **oxidases**, which play critical roles in cellular respiration and energy production.
Question 9: Apoenzyme is ?
- A. Protein moiety (Correct Answer)
- B. Organic cofactor
- C. Inactive enzyme component
- D. Non-protein component required for enzyme activity
Explanation: ***Protein moiety*** - An **apoenzyme** is the **protein component of an enzyme** that is catalytically inactive by itself. - It requires a **non-protein cofactor** (either an inorganic ion or an organic molecule) to become active. *Organic cofactor* - An **organic cofactor** is also known as a **coenzyme**, which binds to the apoenzyme to form a functional holoenzyme. - While essential for enzyme activity, the apoenzyme itself is the protein part, not the organic cofactor. *Inactive enzyme component* - While an apoenzyme is **inactive on its own**, this description is too broad and doesn't specify its chemical nature. - It is specifically the **protein component** that is inactive until bound to its cofactor. *Non-protein component required for enzyme activity* - This describes a **cofactor** (either inorganic or organic), not the apoenzyme itself. - The apoenzyme is the **protein portion**, which *requires* the non-protein component for activity.
Question 10: Enzyme causing covalent bond cleavage without hydrolysis ?
- A. Lyase (Correct Answer)
- B. Ligase
- C. Hydrolase
- D. Transferase
Explanation: ***Lyase*** - **Lyases** are enzymes that catalyze the cleavage of **covalent bonds** (C-C, C-O, C-N, and others) by means other than hydrolysis or oxidation, often creating a new double bond or a ring structure. - They remove groups from substrates to form double bonds, or conversely, add groups to double bonds. - **Examples:** Aldolase (cleaves C-C bonds in glycolysis), carbonic anhydrase (reversible cleavage of C-O bond), fumarase (C-C bond cleavage in TCA cycle). *Ligase* - **Ligases** are enzymes that join two large molecules by forming a new chemical bond, usually accompanied by the **hydrolysis of ATP**. - They are involved in synthesis reactions, not the cleavage of bonds. *Hydrolase* - **Hydrolases** specifically catalyze the hydrolysis of a chemical bond, involving the **addition of water** across the bond. - They break down large molecules into smaller ones using water - this is the key difference from lyases. *Transferase* - **Transferases** catalyze the transfer of a **functional group** from one molecule (the donor) to another (the acceptor). - They do not cause covalent bond cleavage without hydrolysis but rather move existing groups between molecules.