NEET-PG 2012 - Biochemistry Practice Questions

Q: Enzymes of glycolysis are found in:

Cytosol. ***Cytosol*** - Glycolysis is a metabolic pathway that occurs in the **cytosol** of cells. - All the enzymes required for the conversion of glucose to pyruvate are freely dissolved in the **cytoplasm**. *Cell membrane* - The cell membrane is primarily involved in **regulating the passage of substances** into and out of the cell, as well as cell signaling. - Glycolytic enzymes are not associated with the cell membrane. *Mitochondria* - Mitochondria are the primary site of **oxidative phosphorylation** and the **citric acid cycle**, not glycolysis. - While pyruvate (the end product of glycolysis) moves into the mitochondria for further metabolism, the initial glycolytic steps do not occur there. *Ribosomes* - Ribosomes are responsible for **protein synthesis** (translation). - They do not contain enzymes for metabolic pathways like glycolysis.

Q: Which glycogen storage disease also presents as a lysosomal storage disease?

Pompe's disease. ***Pompe's disease*** - Also known as **glycogen storage disease type II**, it is caused by a deficiency of **acid alpha-glucosidase (GAA)**, a *lysosomal enzyme*. - This deficiency leads to the accumulation of **glycogen in lysosomes**, particularly affecting muscle tissue, thereby earning its classification as both a glycogen storage disease and a lysosomal storage disease. *Von Gierke's disease* - This is **glycogen storage disease type I** and is due to a deficiency in **glucose-6-phosphatase**. - It primarily affects the **liver and kidneys**, causing severe **hypoglycemia** and **lactic acidosis**, but it is not classified as a lysosomal storage disease. *McArdle's disease* - This is **glycogen storage disease type V**, caused by a deficiency in **muscle glycogen phosphorylase (myophosphorylase)**. - It manifests as **exercise intolerance** and muscle pain, but it does not involve lysosomal enzyme defects or glycogen accumulation in lysosomes. *Andersen's disease* - This is **glycogen storage disease type IV**, caused by a deficiency in the **glycogen branching enzyme**. - It leads to the formation of **abnormal glycogen structures**, primarily affecting the liver and causing early liver failure, but it is not a lysosomal storage disorder.

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 enzyme is primarily associated with the reduction of NADP+ to NADPH in the pentose phosphate pathway?

G6PD. ***G6PD*** - **Glucose-6-phosphate dehydrogenase (G6PD)** catalyzes the first committed step in the pentose phosphate pathway, converting **glucose-6-phosphate** to **6-phosphogluconolactone**. - This reaction involves the reduction of **NADP+ to NADPH**, making G6PD the primary enzyme for NADPH production in this pathway. *APDH* - **APDH (adenosine phosphosulfate reductase)** is involved in sulfur metabolism and has no direct role in the pentose phosphate pathway or NADPH production. - This enzyme primarily functions in prokaryotes for the **reduction of APS (adenosine 5'-phosphosulfate)**. *α-keto glutarate dehydrogenases* - **Alpha-ketoglutarate dehydrogenase** is a mitochondrial enzyme part of the **Krebs cycle**, converting **alpha-ketoglutarate to succinyl-CoA**. - This enzyme is crucial for ATP production and generates **NADH**, not NADPH, in its reaction. *None of the options* - This option is incorrect because **G6PD** is indeed the primary enzyme responsible for NADPH generation in the pentose phosphate pathway.

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 is the specific activity of an enzyme?

Enzyme units per mg of protein. ***Enzyme units per mg of protein*** - **Specific activity** is defined as the number of **enzyme units** (representing catalytic activity) per milligram of total protein in the sample. - It is a measure of **purity**, indicating the amount of active enzyme relative to other proteins in a preparation. - Formula: Specific activity = Units of enzyme activity / mg of total protein - Used to track enzyme purification progress during isolation procedures. *Concentration of substrate transformed per minute* - This describes the **reaction velocity** or rate of catalysis, but not the specific activity of the enzyme. - While related to enzyme activity, it does not normalize the activity to the amount of **total protein**. - This would be expressed as reaction rate or velocity (V), not specific activity. *Enzyme units per mg of substrate* - This is an incorrect formulation that confuses substrate with protein. - **Specific activity** is normalized to the amount of **protein** in the enzyme preparation, not the substrate. - This option represents a common misconception in enzyme kinetics terminology. *Limit of enzyme per gram of substrate* - This phrase does not correspond to any standard biochemical measure of enzyme activity or concentration. - It does not provide information about the **catalytic efficiency** or **purity** of the enzyme preparation. - The term "limit" is not used in the context of specific activity measurements.

Q: Which of the following pairs of compounds has the highest standard reduction potential?

Fe³⁺/Fe²⁺. ***Fe³⁺/Fe²⁺*** - The **Fe³⁺/Fe²⁺ couple** has a **standard reduction potential (E'0)** of **+0.77 V**, making it the highest among the given options. - A higher positive E'0 indicates a stronger tendency for the oxidized form to accept electrons and be reduced. *NADH/NAD+* - The **NADH/NAD+ couple** has a **standard reduction potential** of **-0.32 V**, indicating it is a strong reducing agent. - Its negative reduction potential means it readily donates electrons during metabolic processes. *Succinate/Fumarate* - The **succinate/fumarate couple** has a **standard reduction potential** of **+0.03 V**. - This pair is involved in the **TCA cycle**, where succinate is oxidized to fumarate, releasing electrons. *Ubiquinone/Ubiquinol* - The **ubiquinone/ubiquinol couple** has a **standard reduction potential** varying around **+0.05 to +0.10 V**, depending on the specific state. - It acts as a mobile electron carrier in the **electron transport chain**, accepting electrons from NADH and FADH2.

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: 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: Increased uric acid levels are seen in which glycogen storage disease ?

Type I (Von Gierke's disease). ***Type I (Von Gierke's disease)*** - In **Von Gierke's disease**, the deficiency of **glucose-6-phosphatase** leads to accumulation of glucose-6-phosphate in hepatocytes. - **Hyperuricemia** occurs due to: 1. **Increased purine degradation** - Metabolic stress leads to accelerated ATP breakdown and increased uric acid production 2. **Decreased renal excretion** - Lactic acidosis (from G6P → pyruvate → lactate) competitively inhibits uric acid secretion in renal tubules 3. **Enhanced purine synthesis** - Increased availability of ribose-5-phosphate from pentose phosphate pathway - Classic triad: **Hepatomegaly, hypoglycemia, and lactic acidosis with hyperuricemia** *Type II (Pompe disease)* - Caused by a deficiency of **acid alpha-glucosidase** (acid maltase), leading to glycogen accumulation in **lysosomes**. - Primarily affects the **heart**, **muscles**, and **liver**, but does not cause hyperuricemia. *Type IV (Andersen disease)* - Results from a deficiency of **glycogen branching enzyme**, leading to the formation of abnormal glycogen with long, unbranched chains. - Primarily affects the **liver** and **spleen**, causing cirrhosis and hepatic failure, but not hyperuricemia. *Type III (Cori disease)* - Caused by a deficiency of **glycogen debranching enzyme** (amylo-1,6-glucosidase), leading to abnormal accumulation of glycogen with short outer branches. - Presents with hepatomegaly, hypoglycemia, and muscle weakness, but **hyperuricemia is not a characteristic feature**.

Question 1

Enzymes of glycolysis are found in:

Accepted Answer

Cytosol

Answer

Cell membrane

Answer

Mitochondria

Answer

Ribosomes

Question 2

Which glycogen storage disease also presents as a lysosomal storage disease?

Accepted Answer

Pompe's disease

Answer

Von Gierke's disease

Answer

McArdle's disease

Answer

Andersen's disease

Question 3

What are digestive enzymes classified as?

Accepted Answer

Hydrolases

Answer

Oxidoreductases

Answer

Transferases

Answer

Ligases

Question 4

Which enzyme is primarily associated with the reduction of NADP+ to NADPH in the pentose phosphate pathway?

Accepted Answer

G6PD

Answer

APDH

Answer

α-keto glutarate dehydrogenases

Answer

None of the options

Question 5

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 6

What is the specific activity of an enzyme?

Accepted Answer

Enzyme units per mg of protein

Answer

Concentration of substrate transformed per minute

Answer

Enzyme units per mg of substrate

Answer

Limit of enzyme per gram of substrate

Question 7

Which of the following pairs of compounds has the highest standard reduction potential?

Accepted Answer

Fe³⁺/Fe²⁺

Answer

NADH/NAD+

Answer

Succinate/Fumarate

Answer

Ubiquinone/Ubiquinol

Question 8

Fluoroacetate inhibits?

Accepted Answer

Aconitase

Answer

Citrate synthase

Answer

Succinate dehydrogenase

Answer

Alpha-ketoglutarate dehydrogenase

Question 9

Glucose oxidase converts glucose to?

Accepted Answer

Gluconic acid

Answer

Glucuronic acid

Answer

Galactonic acid

Answer

Iduronic acid

Question 10

Increased uric acid levels are seen in which glycogen storage disease ?

Accepted Answer

Type I (Von Gierke's disease)

Answer

Type II (Pompe disease)

Answer

Type IV (Andersen disease)

Answer

Type III (Cori disease)

NEET-PG 2012 — Biochemistry