NEET-PG 2012 - Biochemistry Practice Questions

Q: Enzyme causing covalent bond cleavage without hydrolysis ?

Lyase. ***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.

Q: Glucose oxidase converts glucose to?

Gluconic acid. ***Gluconic acid*** - **Glucose oxidase** specifically catalyzes the oxidation of glucose, producing **gluconic acid** and hydrogen peroxide. - This reaction forms the basis for many common **glucose diagnostic tests**, such as those used in blood glucose monitors. *Glucuronic acid* - **Glucuronic acid** is formed from the oxidation of glucose at carbon 6, typically through the **uronic acid pathway**. - It is known for its role in **detoxification** and conjugation reactions in the liver, not as a direct product of glucose oxidase. *Galactonic acid* - **Galactonic acid** is an oxidized form of galactose, a different monosaccharide from glucose. - Its formation is not associated with the action of **glucose oxidase**, an enzyme specific to glucose. *Iduronic acid* - **Iduronic acid** is a C5 epimer of glucuronic acid and is a common component of various **glycosaminoglycans** like dermatan sulfate and heparan sulfate. - It is not produced by the action of **glucose oxidase** on glucose.

Q: Fluoroacetate inhibits?

Aconitase. ***Aconitase*** - **Fluoroacetate** is metabolically converted to **fluorocitrate**, which is a potent competitive inhibitor of **aconitase**. - **Aconitase** is the enzyme responsible for converting **citrate to isocitrate** in the **Krebs cycle**, and its inhibition blocks the cycle. *Citrate synthase* - This enzyme is responsible for the formation of **citrate** from **acetyl-CoA** and **oxaloacetate**. - While fluoroacetate indirectly affects the cycle, it does not directly inhibit **citrate synthase**. *Succinate dehydrogenase* - This enzyme is part of the **Krebs cycle** and the **electron transport chain**, converting **succinate to fumarate**. - **Malonate** is a competitive inhibitor of succinate dehydrogenase, not **fluoroacetate**. *Alpha-ketoglutarate dehydrogenase* - This enzyme catalyzes the conversion of **alpha-ketoglutarate to succinyl-CoA** in the **Krebs cycle**. - Specific inhibitors of this enzyme include **arsenite** and **mercury compounds**, but not fluoroacetate.

Q: Which of the following is required for fatty acid synthesis ?

NADPH. ***NADPH*** - **NADPH** is crucial for fatty acid synthesis, providing the **reducing power** needed for the successive reduction steps. - The enzymes involved, such as **fatty acid synthase**, utilize **NADPH** for the conversion of keto groups to hydroxyl groups and then to saturated methylene groups. *NADH* - **NADH** plays a primary role in **oxidative phosphorylation** and the electron transport chain to generate ATP. - It is generally produced during **catabolic reactions** and is not primarily used as a reducing agent in anabolic processes like fatty acid synthesis. *FADH* - **FADH2** (reduced form of FAD, not FADH) is a coenzyme involved in redox reactions, particularly in the **Krebs cycle** and beta-oxidation of fatty acids. - Like NADH, it is mostly involved in **catabolic processes** that generate energy, rather than anabolic processes requiring reducing equivalents for synthesis. *None of the options* - This option is incorrect because **NADPH** is indeed required for fatty acid synthesis, serving as the essential reducing agent. - The other coenzymes mentioned (NADH, FADH) have different metabolic roles, primarily in energy production rather than biosynthesis.

Q: Which hormone inhibits hormone-sensitive lipase?

Insulin. ***Insulin*** - **Insulin** is a key anabolic hormone that promotes energy storage and inhibits catabolic processes, including the breakdown of triglycerides. - It directly inhibits **hormone-sensitive lipase (HSL)** activity, thus reducing the release of free fatty acids from adipose tissue. *Thyroid hormone* - **Thyroid hormones** (T3 and T4) generally promote catabolism and increase metabolic rate, including the mobilization of lipids. - They tend to **stimulate rather than inhibit** hormone-sensitive lipase expression and activity. *GH* - **Growth hormone (GH)** has lipolytic effects, meaning it promotes the breakdown of fats to provide energy. - GH typically **stimulates HSL activity** and increases the release of free fatty acids from adipocytes. *ACTH* - **Adrenocorticotropic hormone (ACTH)** primarily stimulates the adrenal cortex to produce cortisol. - **Cortisol** can have lipolytic effects in certain contexts and does not directly inhibit HSL; instead, catecholamines act as direct stimulators of HSL.

Q: What is the characteristic nitrogenous product of lecithin hydrolysis?

Choline. ***Choline*** - Lecithin is a type of **phospholipid** called **phosphatidylcholine**, meaning its head group contains choline. - Therefore, during hydrolysis, the **choline** component is released as the characteristic nitrogenous product. *Glucose* - **Glucose** is a simple sugar and a carbohydrate, not a component of lecithin. - It is a primary source of **energy** for cells but is not released during lipid hydrolysis. *Fatty acids* - While **fatty acids** are indeed components of lecithin (two fatty acid chains are attached to the glycerol backbone), they are not nitrogenous. - Fatty acids are **hydrophobic hydrocarbon chains** that make up a significant part of the lipid structure. *Phosphoric acid* - **Phosphoric acid** (or phosphate) is also a component of lecithin, connecting the glycerol backbone to the choline group. - However, it is an **inorganic acid** and does not contain nitrogen.

Q: What is the cofactor required for the enzyme xanthine oxidase?

Molybdenum. ***Molybdenum*** - **Xanthine oxidase** is a key enzyme in **purine metabolism**, responsible for the oxidation of **hypoxanthine to xanthine** and further to **uric acid**. - **Molybdenum** is an essential trace element that serves as a **cofactor** for several enzymes, including xanthine oxidase, where it helps facilitate electron transfer reactions. *Selenium* - **Selenium** is a cofactor for **glutathione peroxidase**, an enzyme involved in antioxidant defense. - It is not directly involved in the function of **xanthine oxidase**. *Zinc* - **Zinc** is a cofactor for a wide range of enzymes, including **carbonic anhydrase** and **alcohol dehydrogenase**. - It does not serve as a cofactor for **xanthine oxidase**. *Magnesium* - **Magnesium** is a critical cofactor for many enzymes, particularly those involved in **ATP hydrolysis and synthesis** and **DNA/RNA synthesis**. - It is not a cofactor for **xanthine oxidase**.

Q: NADH via glycerophosphate shunt makes how many ATP?

2. ***2*** - The **glycerol phosphate shuttle** transfers electrons from **cytosolic NADH** to **FAD** in the mitochondrial electron transport chain. - Each **FADH2** molecule produced then enters the electron transport chain at **Complex II**, ultimately leading to the generation of approximately **2 ATP** molecules. *1* - This option would be correct if the electrons were transferred to a molecule that yields only **one ATP** equivalent, which is not the case for **FADH2**. - No direct mechanism in a shunt generates exactly one ATP per NADH equivalent. *3* - This value represents the ATP yield from **NADH** when it directly enters the electron transport chain via the **malate-aspartate shuttle**, not the **glycerophosphate shuttle**. - The **glycerophosphate shuttle** is less efficient than the **malate-aspartate shuttle**. *4* - This number is not a standard ATP yield for either **NADH** or **FADH2** in the electron transport chain. - The maximum yield for NADH is typically considered to be 2.5 or 3 ATP, and for FADH2 is 1.5 or 2 ATP, depending on the shuttle and precise calculations.

Q: Which enzyme primarily initiates the electron transport process in oxidative phosphorylation?

NADH dehydrogenase. ***Correct NADH dehydrogenase*** - **NADH dehydrogenase**, also known as Complex I, is the enzyme that accepts electrons from **NADH** during oxidative phosphorylation, initiating the electron transport chain. - This enzyme **oxidizes NADH** to NAD+ and pumps protons from the mitochondrial matrix to the intermembrane space, contributing to the **proton gradient**. *Incorrect Pyruvate kinase* - **Pyruvate kinase** is an enzyme involved in **glycolysis**, catalyzing the final step of converting phosphoenolpyruvate to pyruvate. - It functions in the **cytoplasm** and is not directly involved in the electron transport chain or oxidative phosphorylation. *Incorrect Succinyl CoA thiokinase* - **Succinyl CoA thiokinase** (also known as succinate thiokinase or succinyl-CoA synthetase) is an enzyme in the **Krebs cycle** (citric acid cycle). - It catalyzes the reversible reaction of converting succinyl-CoA to succinate and is not directly part of the electron transport chain. *Incorrect ATP synthase* - **ATP synthase** (Complex V) is the enzyme responsible for synthesizing ATP using the **proton gradient** established by the electron transport chain. - While crucial for oxidative phosphorylation, it acts at the end of the process, utilizing the energy generated, rather than initiating electron transport.

Q: Apoenzyme is ?

Protein moiety. ***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 1

Enzyme causing covalent bond cleavage without hydrolysis ?

Accepted Answer

Lyase

Answer

Ligase

Answer

Hydrolase

Answer

Transferase

Question 2

Glucose oxidase converts glucose to?

Accepted Answer

Gluconic acid

Answer

Glucuronic acid

Answer

Galactonic acid

Answer

Iduronic acid

Question 3

Fluoroacetate inhibits?

Accepted Answer

Aconitase

Answer

Citrate synthase

Answer

Succinate dehydrogenase

Answer

Alpha-ketoglutarate dehydrogenase

Question 4

Which of the following is required for fatty acid synthesis ?

Accepted Answer

NADPH

Answer

NADH

Answer

FADH₂

Answer

None of the options

Question 5

Which hormone inhibits hormone-sensitive lipase?

Accepted Answer

Insulin

Answer

GH

Answer

ACTH

Answer

Thyroid hormone

Question 6

What is the characteristic nitrogenous product of lecithin hydrolysis?

Accepted Answer

Choline

Answer

Fatty acids

Answer

Glucose

Answer

Phosphoric acid

Question 7

What is the cofactor required for the enzyme xanthine oxidase?

Accepted Answer

Molybdenum

Answer

Selenium

Answer

Zinc

Answer

Magnesium

Question 8

NADH via glycerophosphate shunt makes how many ATP?

Accepted Answer

2

Answer

1

Answer

4

Answer

3

Question 9

Which enzyme primarily initiates the electron transport process in oxidative phosphorylation?

Accepted Answer

NADH dehydrogenase

Answer

Pyruvate kinase

Answer

Succinyl CoA thiokinase

Answer

ATP synthase

Question 10

Apoenzyme is ?

Accepted Answer

Protein moiety

Answer

Organic cofactor

Answer

Inactive enzyme component

Answer

Non-protein component required for enzyme activity

NEET-PG 2012 — Biochemistry