NEET-PG 2015 - Biochemistry Practice Questions

Q: How many isoenzymes does lactate dehydrogenase (LDH) have?

5, based on H and M polypeptide subunits. **5, based on H and M polypeptide subunits** - **Lactate dehydrogenase (LDH)** is a tetrameric enzyme, meaning it is composed of four polypeptide subunits. - These subunits can be either **H (heart)** type or **M (muscle)** type, leading to five distinct isoenzymes (**LDH-1, LDH-2, LDH-3, LDH-4, LDH-5**) based on their combinations (HHHH, HHHM, HHMM, HMMM, MMMM). *7, based on H and M polypeptide subunits* - While LDH is composed of two types of subunits, H and M, the possible combinations of these four subunits result in **five distinct isoenzymes**, not seven. - Seven isoenzymes are not a recognized number for LDH. *9, based on H and M polypeptide subunits* - The combination of two types of subunits in a tetrameric structure cannot yield nine unique isoenzymes. - This number is incorrect and not supported by the biochemistry of LDH. *3, based on H and M polypeptide subunits* - Three isoenzymes would imply either fewer than four subunits or a more restricted combination, which is not the case for LDH's tetrameric structure with H and M subunits. - This number is insufficient to account for all possible combinations.

Q: Rate limiting enzyme in bile acid synthesis?

7α-hydroxylase. ***7α-hydroxylase*** - This enzyme, specifically **cholesterol 7α-hydroxylase**, catalyzes the first and rate-limiting step in the classic pathway of **bile acid synthesis**, converting cholesterol to 7α-hydroxycholesterol. - Its activity is tightly regulated, primarily by the availability of cholesterol and feedback inhibition by bile acids, making it a key control point. *Desmolase* - **Cholesterol desmolase** (CYP11A1) is the rate-limiting enzyme in **steroid hormone synthesis** in the adrenal glands, converting cholesterol to pregnenolone. - It is not involved in the committed steps of bile acid synthesis from cholesterol. *21α-hydroxylase* - **21α-hydroxylase** (CYP21A2) is crucial in the synthesis of **cortisol and aldosterone** from progesterone and 17-hydroxyprogesterone, respectively. - Deficiency in this enzyme is the most common cause of **congenital adrenal hyperplasia**, but it has no direct role in bile acid synthesis. *12α-hydroxylase* - **12α-hydroxylase** (CYP8B1) is an enzyme involved in the later steps of bile acid synthesis, specifically in the formation of **cholic acid** from 7α-hydroxy-4-cholesten-3-one. - While essential for synthesizing primary bile acids, it is not the *rate-limiting enzyme* for the overall pathway; 7α-hydroxylase holds that distinction.

Q: Enzyme activity is expressed as?

Micromoles/min. ***Micromoles/min*** - Enzyme activity is typically measured by the rate at which an enzyme converts its **substrate into product**. - This rate is often expressed as the amount of product formed (e.g., **micromoles**) or substrate consumed per unit of time (e.g., **per minute**). *Millimoles/lit* - This unit expresses **concentration** (moles per liter) rather than a rate of reaction. - While enzyme reactions involve changes in substrate/product concentration, this unit alone does not describe the **activity or catalytic speed** of the enzyme. *Milli gm/lit* - This unit also expresses **concentration by mass** (milligrams per liter), not enzyme activity. - It does not account for the **time-dependent nature** of enzyme catalysis or the molar quantity of reactants/products. *Mg/dl* - This unit represents **concentration by mass** (milligrams per deciliter), commonly used for measuring substances like glucose or cholesterol in blood. - It is not appropriate for expressing the **catalytic rate or activity** of an enzyme.

Q: What is the mechanism of conversion of trypsinogen to trypsin?

Removal of part of protein. ***Removal of part of protein*** - The conversion of **trypsinogen to trypsin** is an example of **proteolytic activation**, where a specific part of the inactive precursor (zymogen) is cleaved off. - This cleavage occurs at the N-terminus of trypsinogen by **enteropeptidase (or enterokinase)** in the duodenum, exposing the active site and forming active trypsin. *Hydrolysis* - While the removal of a part of the protein involves **hydrolysis of peptide bonds**, this option is too general. - It does not specify the selective nature of the cleavage that leads to activation, nor the fact that it's a specific segment being removed. *Phosphorylation* - **Phosphorylation** is a common mechanism for regulating enzyme activity, but it involves the addition of a **phosphate group**, not the removal of a protein segment. - This process is typically mediated by kinases and does not activate trypsinogen. *Removal of Carboxyl group* - The activation of trypsinogen involves the removal of a small N-terminal peptide, not specifically the removal of a **carboxyl group** from the protein. - While enzymatic cleavage does involve breaking peptide bonds, stating "removal of carboxyl group" is imprecise and does not accurately describe the mechanism.

Q: The mechanism of action of uncouplers of oxidative phosphorylation involves:

Disruption of proton gradient across the inner membrane. ***Disruption of proton gradient across the inner membrane*** - Uncouplers such as **2,4-dinitrophenol** increase the permeability of the **inner mitochondrial membrane** to protons. - This dissipates the **proton motive force** that is normally used by ATP synthase to produce ATP, leading to the uncoupling of electron transport from ATP synthesis. *Inhibition of ATP synthase* - Inhibitors of ATP synthase directly block the enzyme's activity, preventing the synthesis of ATP while the **proton gradient** remains intact. - This mechanism is distinct from uncouplers, which allow electron transport to continue while dissipating the proton gradient. *Stimulation of ATP synthase* - Uncouplers do not stimulate ATP synthase; rather, their action prevents ATP synthase from effectively utilizing the **proton gradient** for ATP production. - Stimulation of ATP synthase would lead to increased ATP synthesis, which is contrary to the effect of uncouplers. *Blocking electron transport chain complexes* - Inhibitors of the **electron transport chain** (e.g., cyanide, rotenone) directly prevent the flow of electrons, thereby preventing the pumping of protons and the formation of a **proton gradient**. - Uncouplers, in contrast, allow electron transport to proceed but dissipate the proton gradient after it has been established.

Q: Which protein is responsible for conserving iron in the body?

Ferritin. ***Ferritin*** - **Ferritin** is the primary intracellular protein that **conserves iron** in the body by storing it in a safe, non-toxic, and bioavailable form - It is found mainly in the liver, spleen, and bone marrow, serving as the body's **iron reserve** - When iron is abundant, ferritin stores it; when iron is needed, ferritin releases it, thus **conserving iron for future use** - Serum ferritin levels directly reflect total body iron stores *Hepcidin* - **Hepcidin** is a regulatory peptide hormone that controls iron homeostasis by inhibiting **ferroportin**, the iron export channel - It reduces iron absorption from the intestine and iron release from macrophages during inflammation or iron overload - While it regulates iron distribution, it is a hormone, not a storage protein, and does not directly conserve iron within cells *Hemopexin* - **Hemopexin** binds free **heme** in plasma, preventing oxidative damage and delivering it to the liver for catabolism - It helps recover iron from heme but does not store or conserve iron in the body *Transferrin* - **Transferrin** is a plasma protein that **transports iron** from absorption sites (intestine) and storage sites (liver, spleen) to tissues that need it - Its role is iron delivery, not conservation or storage

Q: Which of the following statements about NADP is correct?

Involved in HMP shunt. ***Involved in HMP shunt*** - **NADPH**, the reduced form of NADP+, is primarily generated in the **hexose monophosphate shunt (HMP shunt)**, specifically during the oxidative phase. - The NADPH produced in the HMP shunt is crucial for **reductive biosynthesis** reactions and maintaining the **redox balance** of the cell. *Acts as a coenzyme form of Riboflavin* - **NADP is derived from Niacin (Vitamin B3)**, not Riboflavin (Vitamin B2). - **Flavin adenine dinucleotide (FAD)** and **flavin mononucleotide (FMN)** are the coenzyme forms of Riboflavin. *Involved in glycolysis* - **NADP is not directly involved in glycolysis**; instead, **NAD+** is the primary coenzyme that accepts electrons in glycolysis, specifically during the oxidation of glyceraldehyde-3-phosphate. - While some enzymes in glycolysis can interact with NADP+ under specific conditions, its main role is not within the glycolytic pathway. *Involved in fatty acid oxidation* - **Fatty acid oxidation (beta-oxidation)** primarily utilizes **NAD+** and **FAD** as electron acceptors. - **NADP+** is not a direct participant in the electron transport chain during fatty acid breakdown.

Q: In the malate shuttle, how many ATPs are produced from one NADH?

2.5 ATP. ***2.5 ATP*** - In the **malate-aspartate shuttle**, mitochondrial **NADH** is regenerated from cytosolic NADH, and then enters the electron transport chain at **Complex I**. - **Complex I** entry means that NADH contributes to the pumping of enough protons to generate approximately **2.5 ATP** through oxidative phosphorylation. *1 ATP* - **1 ATP** is not the direct equivalent produced from the reoxidation of one NADH via the malate shuttle into the electron transport chain. - This value is typically associated with the direct hydrolysis of **ATP** or the energy equivalent of **GTP** produced in the citric acid cycle. *3 ATP* - Historically, **3 ATP** was the accepted stoichiometry for one NADH, but more accurate measurements of proton pumping and ATP synthase activity have revised this. - The value of 3 ATP per NADH does not reflect the most current understanding of mitochondrial bioenergetics. *2 ATP* - **2 ATP** is the approximate yield for **FADH2** entering the electron transport chain at **Complex II**, bypassing Complex I, and thus pumping fewer protons. - This value is not applicable to NADH transferred via the malate-aspartate shuttle, as NADH enters at Complex I.

Q: Which of the following is not a substrate for gluconeogenesis?

Leucine. ***Leucine*** - **Leucine** is an exclusively **ketogenic amino acid**, meaning its breakdown products can only be converted into **ketone bodies** or fatty acids, not glucose. - It does not have a carbon skeleton that can be directly converted into **pyruvate** or **oxaloacetate**, which are key intermediates in gluconeogenesis. *Lactate* - **Lactate** is a major substrate for gluconeogenesis, particularly during exercise or fasting. - It is converted to **pyruvate** by **lactate dehydrogenase**, and pyruvate can then enter the gluconeogenic pathway. *Propionate* - **Propionate** is a fatty acid with an odd number of carbon atoms, primarily derived from the catabolism of odd-chain fatty acids or from bacterial fermentation in the colon. - It can be converted into **succinyl CoA**, an intermediate of the citric acid cycle, which can then be used for gluconeogenesis. *Glycerol* - **Glycerol**, released during the breakdown of triglycerides, is an important substrate for gluconeogenesis. - It is phosphorylated to **glycerol-3-phosphate**, which is then oxidized to **dihydroxyacetone phosphate (DHAP)**, an intermediate in glycolysis and gluconeogenesis.

Q: Which of the following is an example of an exopeptidase?

Carboxypeptidases. ***Carboxypeptidases*** - **Carboxypeptidases** are enzymes that cleave the **C-terminal** (carboxyl end) amino acid from a polypeptide chain, making them a type of exopeptidase. - They are crucial in protein digestion, releasing individual amino acids from the end of protein chains. *Trypsin* - **Trypsin** is an **endopeptidase** that cleaves peptide bonds within protein chains, specifically at the carboxyl side of **lysine** or **arginine** residues. - It does not cleave amino acids from the ends of polypeptide chains. *Chymotrypsin* - **Chymotrypsin** is an **endopeptidase** that cleaves peptide bonds within a polypeptide chain, primarily at the carboxyl side of **tyrosine**, **tryptophan**, or **phenylalanine**. - Its action is internal to the protein sequence, not at the termini. *Elastase* - **Elastase** is also an **endopeptidase** that cleaves peptide bonds internally, specifically targeting small, uncharged amino acid residues like **alanine**, **glycine**, and **valine**. - Its primary role is to break down elastin, an elastic protein in connective tissues, but it does so by internal cleavage.

Question 1

How many isoenzymes does lactate dehydrogenase (LDH) have?

Accepted Answer

5, based on H and M polypeptide subunits

Answer

7, based on H and M polypeptide subunits

Answer

9, based on H and M polypeptide subunits

Answer

3, based on H and M polypeptide subunits

Question 2

Rate limiting enzyme in bile acid synthesis?

Accepted Answer

7α-hydroxylase

Answer

Desmolase

Answer

21α-hydroxylase

Answer

12α-hydroxylase

Question 3

Enzyme activity is expressed as?

Accepted Answer

Micromoles/min

Answer

Millimoles/lit

Answer

Milli gm/lit

Answer

Mg/dl

Question 4

What is the mechanism of conversion of trypsinogen to trypsin?

Accepted Answer

Removal of part of protein

Answer

Hydrolysis

Answer

Phosphorylation

Answer

Removal of Carboxyl group

Question 5

The mechanism of action of uncouplers of oxidative phosphorylation involves:

Accepted Answer

Disruption of proton gradient across the inner membrane

Answer

Inhibition of ATP synthase

Answer

Stimulation of ATP synthase

Answer

Blocking electron transport chain complexes

Question 6

Which protein is responsible for conserving iron in the body?

Accepted Answer

Ferritin

Answer

Hepcidin

Answer

Hemopexin

Answer

Transferrin

Question 7

Which of the following statements about NADP is correct?

Accepted Answer

Involved in HMP shunt

Answer

Involved in fatty acid oxidation

Answer

Involved in glycolysis

Answer

Acts as a coenzyme form of Riboflavin

Question 8

In the malate shuttle, how many ATPs are produced from one NADH?

Accepted Answer

2.5 ATP

Answer

1 ATP

Answer

3 ATP

Answer

2 ATP

Question 9

Which of the following is not a substrate for gluconeogenesis?

Accepted Answer

Leucine

Answer

Lactate

Answer

Propionate

Answer

Glycerol

Question 10

Which of the following is an example of an exopeptidase?

Accepted Answer

Carboxypeptidases

Answer

Trypsin

Answer

Chymotrypsin

Answer

Elastase

NEET-PG 2015 — Biochemistry