Enzymes Practice Questions

Q: What type of enzyme is hexokinase?

Transferase. ***Transferase*** - Hexokinase catalyzes the transfer of a **phosphate group** from **ATP** to glucose, forming glucose-6-phosphate. - Enzymes that catalyze the transfer of functional groups from one molecule to another are classified as **transferases**. *Ligase* - **Ligases** are enzymes that catalyze the joining of two large molecules by forming a new chemical bond, usually accompanied by the hydrolysis of a small pendant chemical group on one of the larger molecules or the less-stable of the two products. - This activity usually involves reactions like **DNA ligation**, not phosphate group transfer to a sugar. *Oxidoreductase* - **Oxidoreductases** catalyze **oxidation-reduction reactions**, involving the transfer of electrons from one molecule to another. - Hexokinase does not perform redox reactions; it transfers a phosphate group. *Reductase* - **Reductases** are a specific type of **oxidoreductase** that catalyze reactions where a molecule is reduced (gains electrons). - This is a subset of oxidation-reduction chemistry and is not the function of hexokinase.

Q: Carboxypeptidase contains which mineral?

Zinc. ***Zinc*** - **Carboxypeptidase** is a **metalloenzyme**, meaning it requires a metal ion for its catalytic activity. - **Zinc** acts as a crucial cofactor in the active site of carboxypeptidase, enabling its proteolytic function. *Copper* - **Copper** is a component of enzymes like **cytochrome c oxidase** and **superoxide dismutase**, but not carboxypeptidase. - Its presence is essential for processes like **electron transport** and **antioxidant defense**. *Iron* - **Iron** is a central component of **hemoglobin** and **myoglobin** for oxygen transport, and in enzymes like **catalase** and **peroxidase**. - It is not involved in the catalytic mechanism of carboxypeptidase. *None of the options* - This option is incorrect because **Zinc** is a known and essential mineral for the function of carboxypeptidase. - Carboxypeptidase is a metalloenzyme, and a metal cofactor is required for its activity.

Q: Which isoenzyme of lactate dehydrogenase (LDH) is predominantly elevated in liver injury?

LDH-5. ***LDH-5 isoenzyme most significant in hepatic conditions*** - **LDH-5** is the predominant isoenzyme found in the **liver** and skeletal muscle. - An elevation of **LDH-5** is highly indicative of **hepatocellular damage** or injury. *LDH-1 isoenzyme associated with cardiac tissue* - **LDH-1** is primarily present in the **heart** and red blood cells. - Its elevation suggests conditions like **myocardial infarction** or hemolytic anemia, not liver injury. *LDH-3 isoenzyme typical in respiratory system* - **LDH-3** is found in the **lungs**, kidneys, and other tissues. - While it can be elevated in **pulmonary embolism** or renal disease, it is not specific for liver injury. *LDH-2 isoenzyme linked to erythrocyte metabolism* - **LDH-2** is abundant in **red blood cells** and also found in the heart and kidneys. - Elevations are often seen in conditions involving **hemolysis** or myocardial damage, similar to LDH-1.

Q: What are isoenzymes?

Physically distinct forms of the same enzyme. ***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.

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: What are digestive enzymes classified as?

Hydrolases. ***Hydrolases*** - Digestive enzymes like **amylase**, **lipase**, and **proteases** break down complex food molecules by adding water, a process known as **hydrolysis**. - This class of enzymes catalyzes the cleavage of a chemical bond with the concurrent addition of a water molecule. - All major digestive enzymes belong to this class according to the **EC enzyme classification system**. *Oxidoreductases* - These enzymes catalyze **redox reactions**, involving the transfer of electrons from one molecule to another. - Examples include **dehydrogenases** and **oxidases**, which are not primarily involved in breaking down food molecules in digestion. *Transferases* - Transferases catalyze the transfer of functional groups (such as methyl, acyl, or phosphate groups) from one molecule to another. - Examples include **kinases** and **transaminases**, which are involved in metabolic pathways but not in the digestive breakdown of food. *Ligases* - Ligases are enzymes that catalyze the joining of two large molecules by forming a new chemical bond, typically with the concomitant hydrolysis of ATP. - They are involved in **DNA repair** and **biosynthetic reactions**, not in the breakdown of food during digestion.

Q: Which cofactor is primarily associated with the activity of glutamate dehydrogenase?

NAD+. ***NAD+*** - Glutamate dehydrogenase catalyzes the oxidative deamination of **glutamate** to **α-ketoglutarate** and ammonia, and this reaction primarily uses **NAD+** as an electron acceptor. - In some organisms and contexts, it can also use **NADP+**, but **NAD+** is the more common and significant cofactor for its catabolic role. *FAD* - **FAD (flavin adenine dinucleotide)** is typically associated with **flavoproteins** and enzymes involved in oxidation-reduction reactions, such as those in the **electron transport chain** and the **Krebs cycle**. - Enzymes like **succinate dehydrogenase** use FAD, not glutamate dehydrogenase. *FMN* - **FMN (flavin mononucleotide)** is another flavin coenzyme, similar to FAD, and is found in various **flavoproteins** and enzymes of the **electron transport chain**, such as **NADH dehydrogenase (Complex I)**. - It does not serve as a primary cofactor for **glutamate dehydrogenase** activity. *FADH2* - **FADH2** is the reduced form of **FAD**, carrying high-energy electrons to the **electron transport chain** for ATP synthesis. - It's a product or reactant of various metabolic pathways, but not a direct cofactor for **glutamate dehydrogenase**.

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.

Q: Selenocysteine is associated with ?

Deiodinase. ***Deiodinase*** - Selenocysteine is a critical component of **iodothyronine deiodinases**, a family of enzymes that regulate **thyroid hormone metabolism**. - These enzymes catalyze the removal of iodine from thyroid hormones, converting **thyroxine (T4)** into the more active **triiodothyronine (T3)** or inactive forms. *Carbonic anhydrase* - This enzyme contains **zinc** as its essential metal cofactor and is involved in the interconversion of **carbon dioxide** and **bicarbonate**. - Its primary role is in pH regulation and CO2 transport, without any direct association with selenocysteine. *Catalase* - Catalase is an enzyme primarily found in **peroxisomes** and contains **iron-porphyrin** groups as its prosthetic group. - Its function is to convert **hydrogen peroxide** into water and oxygen, protecting cells from oxidative damage. *Transferase* - Transferases are a broad class of enzymes that catalyze the transfer of **functional groups** (e.g., methyl, glucose) from one molecule to another. - While essential for many metabolic processes, there is no inherent association of the general class of transferases with selenocysteine.

Question 1

What type of enzyme is hexokinase?

Accepted Answer

Transferase

Answer

Ligase

Answer

Oxidoreductase

Answer

Reductase

Question 2

Carboxypeptidase contains which mineral?

Accepted Answer

Zinc

Answer

Copper

Answer

Iron

Answer

None of the options

Question 3

Which isoenzyme of lactate dehydrogenase (LDH) is predominantly elevated in liver injury?

Accepted Answer

LDH-5

Answer

LDH-3

Answer

LDH-1

Answer

LDH-2

Question 4

What are isoenzymes?

Accepted Answer

Physically distinct forms of the same enzyme

Answer

Physically same forms of different enzymes

Answer

Forms of same enzyme that catalyze different reactions

Answer

Forms of different enzyme that catalyze same reactions

Question 5

What coenzyme is required by gulonate dehydrogenase for its activity?

Accepted Answer

NAD

Answer

FAD

Answer

FMN

Answer

NADP

Question 6

What are digestive enzymes classified as?

Accepted Answer

Hydrolases

Answer

Oxidoreductases

Answer

Transferases

Answer

Ligases

Question 7

Which cofactor is primarily associated with the activity of glutamate dehydrogenase?

Accepted Answer

NAD+

Answer

FAD

Answer

FMN

Answer

FADH2

Question 8

Which of the following best describes the difference between glucokinase and hexokinase?

Accepted Answer

Glucokinase has higher Km for glucose compared to hexokinase.

Answer

Glucokinase is not inhibited by glucose-6-phosphate unlike hexokinase.

Answer

Glucokinase has a low affinity for glucose.

Answer

Glucokinase activity increases with glucose concentration while hexokinase remains saturated.

Question 9

Apoenzyme is ?

Accepted Answer

Protein moiety

Answer

Organic cofactor

Answer

Inactive enzyme component

Answer

Non-protein component required for enzyme activity

Question 10

Selenocysteine is associated with ?

Accepted Answer

Deiodinase

Answer

Carbonic anhydrase

Answer

Catalase

Answer

Transferase

Enzymes — MCQs

Enzymes — MCQs

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