Enzymes Practice Questions

Q: Fumarase is an example of which class of enzymes?

Lyase. **Explanation:** **1. Why Lyase is the correct answer:** Enzymes are classified by the IUBMB into seven classes based on the reactions they catalyze. **Lyases (Class 4)** are enzymes that catalyze the cleavage of C-C, C-O, C-N, and other bonds by means other than hydrolysis or oxidation, often resulting in the formation of a double bond or the addition of a group to a double bond. **Fumarase** (fumarate hydratase) catalyzes the reversible addition of a water molecule across the double bond of fumarate to form L-malate in the TCA cycle. Since it adds water to a double bond without breaking a bond via hydrolysis, it is classified as a Lyase (specifically a hydro-lyase). **2. Why other options are incorrect:** * **Hydrolases (Class 3):** These enzymes catalyze the cleavage of bonds (like ester, peptide, or glycosidic bonds) by the **addition of water**. While Fumarase involves water, it does not "split" a molecule into two smaller components via water; it adds water to a double bond. * **Ligases (Class 6):** These enzymes catalyze the joining of two large molecules, coupled with the **hydrolysis of ATP** (e.g., Pyruvate carboxylase). Fumarase does not require ATP for its reaction. **3. High-Yield Clinical Pearls for NEET-PG:** * **TCA Cycle Context:** Fumarase is a crucial enzyme in the mitochondrial matrix. * **Clinical Correlation:** A deficiency of Fumarase leads to **Fumaric Aciduria**, characterized by severe neurological impairment and encephalopathy. * **Oncogene Link:** Mutations in the fumarate hydratase (FH) gene are associated with **Hereditary Leiomyomatosis and Renal Cell Cancer (HLRCC)**, as fumarate acts as an "oncometabolite" when it accumulates. * **Mnemonic for Enzyme Classes:** **O**ver **T**he **H**ill **L**I**L** **T** (Oxidoreductase, Transferase, Hydrolase, Lyase, Isomerase, Ligase, Translocase).

Q: Which of the following is NOT a rate-limiting enzyme?

Malonate dehydrogenase. **Explanation:** In metabolic pathways, a **rate-limiting enzyme** is typically the slowest step (bottleneck), often regulated by allosteric effectors or hormones to control the flux of the entire pathway. **Why Malonate Dehydrogenase is the correct answer:** There is no enzyme called "Malonate dehydrogenase" in human metabolism. **Malonate** is actually a classic **competitive inhibitor** of the enzyme *Succinate dehydrogenase* in the TCA cycle. It mimics the structure of succinate but cannot be dehydrogenated. Therefore, it is a pharmacological/biochemical tool rather than a functional rate-limiting enzyme. **Analysis of Incorrect Options:** * **ALA Synthase (Aminolevulinic acid synthase):** This is the key rate-limiting and committed step of **Heme synthesis**. It requires Pyridoxal Phosphate (B6) as a cofactor and is feedback-inhibited by Heme. * **Phosphofructokinase-1 (PFK-1):** This is the most important rate-limiting enzyme of **Glycolysis**. It is allosterically activated by Fructose-2,6-bisphosphate and AMP, and inhibited by ATP and Citrate. * **Acetyl CoA Carboxylase (ACC):** This is the rate-limiting step for **Fatty Acid Synthesis**. It converts Acetyl CoA to Malonyl CoA and is activated by Citrate and inhibited by Palmitoyl-CoA. **Clinical Pearls for NEET-PG:** * **HMG-CoA Reductase:** Rate-limiting for Cholesterol synthesis (Target of Statins). * **Carbamoyl Phosphate Synthetase I (CPS-I):** Rate-limiting for the Urea Cycle (Activated by N-acetylglutamate). * **Fructose-1,6-Bisphosphatase:** Rate-limiting for Gluconeogenesis. * **Glycogen Synthase:** Rate-limiting for Glycogenesis.

Q: Which one of the following enzymes is not a protein, but an RNA molecule?

Peptidyl transferase. ### Explanation The correct answer is **Peptidyl transferase**. **1. Why Peptidyl Transferase is Correct:** Traditionally, all enzymes were thought to be proteins. However, **ribozymes** are RNA molecules that possess catalytic activity. Peptidyl transferase is a classic example of a ribozyme. It is located in the large ribosomal subunit (28S rRNA in eukaryotes and 23S rRNA in prokaryotes). During translation, it catalyzes the formation of peptide bonds between amino acids. Because the catalytic activity resides in the RNA component rather than a protein, it is classified as a non-protein enzyme. **2. Why the Other Options are Incorrect:** * **RNA Polymerase (B):** This is a complex protein enzyme responsible for synthesizing RNA from a DNA template during transcription. * **Restriction Endonuclease (C):** These are bacterial protein enzymes (often called "molecular scissors") used in recombinant DNA technology to cut DNA at specific palindromic sequences. * **Reverse Transcriptase (D):** This is an RNA-dependent DNA polymerase protein, famously found in retroviruses like HIV, which synthesizes DNA from an RNA template. **3. High-Yield Clinical Pearls for NEET-PG:** * **Other Ribozymes:** Apart from Peptidyl transferase, other notable ribozymes include **RNase P** (involved in tRNA processing) and **SnRNAs** (involved in splicing). * **Antibiotic Link:** Many antibiotics target the 50S subunit (e.g., Chloramphenicol), effectively inhibiting the peptidyl transferase activity of the ribozyme. * **Abzymes:** These are catalytic antibodies (proteins) that mimic enzymes; do not confuse them with ribozymes (RNA).

Q: Pentostatin acts by inhibiting which enzyme?

Adenosine deaminase. **Explanation:** **Pentostatin** (also known as 2'-deoxycoformycin) is a potent transition-state analog that irreversibly inhibits **Adenosine Deaminase (ADA)**. 1. **Mechanism of Action:** ADA is a critical enzyme in the purine salvage pathway that converts adenosine to inosine and deoxyadenosine to deoxyinosine. By inhibiting ADA, Pentostatin leads to an intracellular accumulation of **deoxyadenosine triphosphate (dATP)**. High levels of dATP are toxic to lymphocytes as they inhibit ribonucleotide reductase, thereby halting DNA synthesis and inducing apoptosis. 2. **Clinical Application:** Because it specifically targets lymphocytes, Pentostatin is primarily used as a chemotherapeutic agent in the treatment of **Hairy Cell Leukemia** and certain T-cell lymphomas. **Analysis of Incorrect Options:** * **A. RNA-dependent DNA polymerase:** Also known as Reverse Transcriptase; this is the target of NRTIs (like Zidovudine) used in HIV treatment. * **B. Aldolase:** An enzyme in glycolysis (Aldolase A) and fructose metabolism (Aldolase B). Deficiency of Aldolase B leads to Hereditary Fructose Intolerance. * **D. Adenylyl cyclase:** This enzyme converts ATP to cAMP. It is regulated by G-proteins and is the target of various bacterial toxins (e.g., Cholera toxin, Pertussis toxin) rather than Pentostatin. **High-Yield NEET-PG Pearls:** * **ADA Deficiency:** A genetic deficiency of Adenosine Deaminase is the second most common cause of **Autosomal Recessive SCID** (Severe Combined Immunodeficiency). * **Drug of Choice:** While Pentostatin is effective, **Cladribine** (a purine analog) is currently considered the first-line treatment for Hairy Cell Leukemia. * **Transition State Analog:** Pentostatin is a classic example of a drug that mimics the transition state of a substrate to achieve high-affinity enzyme inhibition.

Q: Plasma cholinesterase is reduced in all of the following conditions except?

Hemolysis. ### Explanation **Plasma Cholinesterase (Pseudocholinesterase)** is a glycoprotein enzyme synthesized by the **liver** and secreted into the blood. It is clinically significant because it hydrolyzes drugs like succinylcholine and mivacurium. **Why Hemolysis is the correct answer:** Hemolysis involves the destruction of Red Blood Cells (RBCs). While RBCs contain **True Cholinesterase** (Acetylcholinesterase), they do not contain Plasma Cholinesterase. Therefore, the breakdown of RBCs does not decrease the levels of plasma cholinesterase; in fact, it has no significant effect on its concentration. **Why the other options are incorrect:** * **Liver Disease:** Since the liver is the primary site of synthesis for plasma cholinesterase, any hepatic dysfunction (cirrhosis, hepatitis) leads to decreased production and lower plasma levels. * **Pregnancy:** Plasma cholinesterase levels naturally decrease by about 20–30% during the first trimester and remain low until delivery, likely due to hemodilution and hormonal changes. * **Malnutrition:** As a protein synthesized by the liver, its levels drop in states of protein-energy malnutrition (like Kwashiorkor) due to a lack of substrate for protein synthesis. **Clinical Pearls for NEET-PG:** 1. **Succinylcholine Apnea:** Patients with inherited or acquired deficiency of plasma cholinesterase cannot metabolize succinylcholine, leading to prolonged neuromuscular blockade and respiratory paralysis. 2. **Organophosphate Poisoning:** Plasma cholinesterase is a sensitive marker for organophosphate poisoning (it decreases earlier than RBC cholinesterase), though RBC cholinesterase is more specific for monitoring chronic exposure. 3. **True vs. Pseudo:** Remember, **True** cholinesterase is found in the **N**erve endings, **G**ray matter, and **R**BCs (Mnemonic: **NGR**), while **Pseudo**cholinesterase is found in the **P**lasma, **L**iver, and **W**hite matter (Mnemonic: **PLW**).

Q: NAD+ acts as a coenzyme for which of the following enzymes?

Malate dehydrogenase. ### Explanation **1. Why Malate Dehydrogenase is Correct:** Malate dehydrogenase is a key enzyme in the **TCA cycle** and the **Malate-Aspartate shuttle**. It catalyzes the reversible oxidation of L-malate to oxaloacetate. This reaction involves the transfer of two electrons and a proton to **NAD+**, reducing it to NADH + H⁺. In biochemistry, most dehydrogenases involved in the oxidation of hydroxyl groups (like malate or lactate) to carbonyl groups utilize NAD+ as the electron acceptor. **2. Analysis of Incorrect Options:** * **Xanthine oxidase (Option A):** This enzyme, involved in purine catabolism, is a metalloflavoprotein. It utilizes **FAD** and Molybdenum as cofactors, not NAD+. * **L-amino acid oxidase (Option B):** This enzyme catalyzes the oxidative deamination of amino acids. It is a flavoprotein that uses **FMN** (Flavin Mononucleotide) as its coenzyme. * **Succinate dehydrogenase (Option C):** A unique enzyme that is part of both the TCA cycle and Complex II of the Electron Transport Chain. It utilizes **FAD** (covalently bound) because the free energy change of succinate oxidation is insufficient to reduce NAD+. **3. Clinical Pearls & High-Yield Facts:** * **Niacin (Vitamin B3):** NAD+ and NADP+ are derived from Niacin. Deficiency leads to **Pellagra** (3Ds: Dermatitis, Diarrhea, Dementia). * **NAD+ vs. NADPH:** Generally, **NAD+** is used in **catabolic** pathways (oxidative), while **NADPH** is used in **anabolic** pathways (reductive biosynthesis like fatty acid synthesis) and to maintain reduced glutathione. * **Mnemonic:** Most "Dehydrogenases" use NAD+, EXCEPT for **Succinate Dehydrogenase**, **Acyl-CoA Dehydrogenase**, and **Glycerol-3-Phosphate Dehydrogenase (mitochondrial)**, which use FAD.

Q: All digestive enzymes are?

Hydrolases. **Explanation:** **1. Why Hydrolases is correct:** Digestive enzymes belong to the **Hydrolase** class (Class 3) of enzymes. Their primary function is to catalyze the cleavage of chemical bonds (C-O, C-N, C-C) by the **addition of a water molecule** (hydrolysis). In the gastrointestinal tract, complex macromolecules are broken down into simpler units: * **Proteases/Peptidases** (e.g., Pepsin, Trypsin) hydrolyze peptide bonds. * **Glycosidases** (e.g., Salivary Amylase, Lactase) hydrolyze glycosidic bonds. * **Lipases** hydrolyze ester bonds in triglycerides. **2. Why other options are incorrect:** * **Ligases (Class 6):** These enzymes join two molecules together, usually coupled with the hydrolysis of ATP (e.g., Pyruvate carboxylase). Digestion is a catabolic (breakdown) process, not synthetic. * **Transferases (Class 2):** These transfer functional groups (like methyl or phosphate groups) from one substrate to another (e.g., Hexokinase). They do not break down food into absorbable units. * **Lyases (Class 4):** These catalyze the breakage of bonds by means other than hydrolysis or oxidation, often forming double bonds or adding groups to double bonds (e.g., Carbonic anhydrase, Fumarase). **3. NEET-PG High-Yield Pearls:** * **Classification Tip:** Remember the mnemonic **OTH LIL** (Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases, Ligases) for the IUBMB classification. * **Zymogens:** Most digestive hydrolases are secreted as inactive precursors (zymogens) to prevent autolysis of the secretory organs (e.g., Trypsinogen). * **Location:** Most digestive enzymes are extracellular enzymes, unlike most other enzyme classes which function intracellularly.

Question 1

Fumarase is an example of which class of enzymes?

Accepted Answer

Lyase

Answer

Hydrolase

Answer

Ligase

Answer

None of the above

Question 2

Which of the following is NOT a rate-limiting enzyme?

Accepted Answer

Malonate dehydrogenase

Answer

ALA synthase

Answer

Phosphofructokinase

Answer

Acetyl CoA carboxylase

Question 3

Which of the following acts as a coenzyme and not as a co-factor?

Accepted Answer

Ascorbic acid

Answer

Biotin

Answer

Thiamine

Answer

Folic acid

Question 4

Which one of the following enzymes is not a protein, but an RNA molecule?

Accepted Answer

Peptidyl transferase

Answer

RNA polymerase

Answer

Restriction endonuclease

Answer

Reverse transcriptase

Question 5

Pentostatin acts by inhibiting which enzyme?

Accepted Answer

Adenosine deaminase

Answer

RNA dependent DNA polymerase

Answer

Aldolase

Answer

Adenylyl cyclase

Question 6

Plasma cholinesterase is reduced in all of the following conditions except?

Accepted Answer

Hemolysis

Answer

Pregnancy

Answer

Liver disease

Answer

Malnutrition

Question 7

NAD+ acts as a coenzyme for which of the following enzymes?

Accepted Answer

Malate dehydrogenase

Answer

Xanthine oxidase

Answer

L-amino acid oxidase

Answer

Succinate dehydrogenase

Question 8

All digestive enzymes are?

Accepted Answer

Hydrolases

Answer

Ligases

Answer

Transferases

Answer

Lyases

Question 9

All of the following enzymes are regulated by calcium or calmodulin, except:

Accepted Answer

Hexokinase

Answer

Adenylate cyclase

Answer

Glycogen synthase

Answer

Guanylyl cyclase

Question 10

What is true about allosteric enzymes?

Accepted Answer

Hill's equation is used to study the kinetics of allosteric enzymes.

Answer

They are single-unit enzymes.

Answer

They follow Michaelis-Menten saturation kinetics.

Answer

Allosteric activity is most prominent in the active site of the enzyme.

Enzymes — MCQs

Enzymes — MCQs

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