Km value is defined as:
In the electron transport chain (ETC), which enzyme does cyanide inhibit?
Enzymes of glycolysis are found in:
Which glycogen storage disease also presents as a lysosomal storage disease?
What is the classification of the Y chromosome?
What are digestive enzymes classified as?
Which enzyme is primarily associated with the reduction of NADP+ to NADPH in the pentose phosphate pathway?
Which isoenzyme of lactate dehydrogenase (LDH) is predominantly elevated in liver injury?
What is the specific activity of an enzyme?
Which of the following pairs of compounds has the highest standard reduction potential?
NEET-PG 2012 - Biochemistry NEET-PG Practice Questions and MCQs
Question 21: Km value is defined as:
- A. Substrate concentration at Vmax/2 (Correct Answer)
- B. Substrate concentration at which reaction rate is maximum
- C. Substrate concentration at Vmax
- D. Substrate concentration at which enzyme activity is optimal
Explanation: ***Substrate concentration at Vmax/2*** - The **Michaelis constant (Km)** is defined as the **substrate concentration** at which the reaction velocity is **half of the maximum velocity (Vmax/2)**. - It reflects the **affinity of an enzyme for its substrate**; a lower Km indicates higher affinity. *Substrate concentration at which reaction rate is maximum* - The **maximum reaction rate (Vmax)** is achieved when the enzyme is **saturated with substrate**, meaning all active sites are occupied. - Km specifically refers to the substrate concentration needed to reach **half of this maximum rate**, not the maximum rate itself. *Substrate concentration at Vmax* - At **Vmax**, the enzyme is fully saturated with substrate, and the reaction rate cannot increase further by adding more substrate. - The **Km value** is a measure related to the **efficiency of substrate binding** at conditions below saturation, specifically at half Vmax. *Substrate concentration at which enzyme activity is optimal* - **Optimal enzyme activity** is generally influenced by factors such as **pH and temperature**, which affect the enzyme's structure and catalytic efficiency. - Km is specifically related to the **substrate concentration** required to achieve a specific reaction rate, not the overall optimal environmental conditions for the enzyme.
Question 22: In the electron transport chain (ETC), which enzyme does cyanide inhibit?
- A. Complex II (Succinate dehydrogenase)
- B. Cytochrome c oxidase (Complex IV) (Correct Answer)
- C. Complex I (NADH dehydrogenase)
- D. Complex III (Cytochrome bc1 complex)
Explanation: ***Cytochrome c oxidase (Complex IV)*** - Cyanide binds to the **ferric iron (Fe3+)** in the heme a3 component of cytochrome c oxidase, blocking the final transfer of electrons to oxygen. - This inhibition effectively halts the entire **electron transport chain** and **oxidative phosphorylation**, leading to rapid cellular energy depletion. *Complex I (NADH dehydrogenase)* - While other toxins can inhibit Complex I (e.g., rotenone, amytal), **cyanide specifically targets Complex IV**. - Inhibition here prevents the entry of electrons from **NADH** into the ETC, but it's not cyanide's primary site of action. *Complex III (Cytochrome bc1 complex)* - Complex III is involved in transferring electrons from **ubiquinol** to cytochrome c, but it is not directly inhibited by cyanide. - Antimycin A is a well-known inhibitor of Complex III. *Complex II (Succinate dehydrogenase)* - Complex II directly receives electrons from **succinate** in the citric acid cycle and passes them to ubiquinone, bypassing Complex I. - Cyanide does not inhibit Complex II; inhibitors of this complex include malonate.
Question 23: Enzymes of glycolysis are found in:
- A. Cytosol (Correct Answer)
- B. Cell membrane
- C. Mitochondria
- D. Ribosomes
Explanation: ***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.
Question 24: Which glycogen storage disease also presents as a lysosomal storage disease?
- A. Von Gierke's disease
- B. McArdle's disease
- C. Andersen's disease
- D. Pompe's disease (Correct Answer)
Explanation: ***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.
Question 25: What is the classification of the Y chromosome?
- A. Metacentric
- B. Submetacentric (Correct Answer)
- C. Acrocentric
- D. None of the options
Explanation: ***Submetacentric*** - The **Y chromosome** is classified as submetacentric because its **centromere** is located off-center, resulting in two arms of unequal length. - The short arm (Yp) is smaller than the long arm (Yq), but not as disproportionate as in acrocentric chromosomes. - The **X chromosome** is also submetacentric, making both sex chromosomes belong to this category. *Metacentric* - A **metacentric chromosome** has its **centromere** located in the middle, resulting in two arms of approximately equal length. - Examples include chromosomes 1, 3, 16, 19, and 20, which have nearly equal arm ratios unlike the Y chromosome. *Acrocentric* - An **acrocentric chromosome** has its **centromere** located very close to one end, creating one very short arm and one very long arm. - The five acrocentric human chromosomes are **13, 14, 15, 21, and 22**, which possess satellite DNA and nucleolar organizing regions (NORs) on their short arms. - The **Y chromosome is NOT acrocentric** despite historical confusion; it has a more centrally positioned centromere than true acrocentric chromosomes. *None of the options* - This option is incorrect because the Y chromosome has a specific and well-established classification as **submetacentric** based on its centromere position and arm ratio.
Question 26: What are digestive enzymes classified as?
- A. Hydrolases (Correct Answer)
- B. Oxidoreductases
- C. Transferases
- D. Ligases
Explanation: ***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.
Question 27: Which enzyme is primarily associated with the reduction of NADP+ to NADPH in the pentose phosphate pathway?
- A. G6PD (Correct Answer)
- B. APDH
- C. α-keto glutarate dehydrogenases
- D. None of the options
Explanation: ***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.
Question 28: Which isoenzyme of lactate dehydrogenase (LDH) is predominantly elevated in liver injury?
- A. LDH-3
- B. LDH-5 (Correct Answer)
- C. LDH-1
- D. LDH-2
Explanation: ***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.
Question 29: What is the specific activity of an enzyme?
- A. Enzyme units per mg of protein (Correct Answer)
- B. Concentration of substrate transformed per minute
- C. Enzyme units per mg of substrate
- D. Limit of enzyme per gram of substrate
Explanation: ***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.
Question 30: Which of the following pairs of compounds has the highest standard reduction potential?
- A. NADH/NAD+
- B. Succinate/Fumarate
- C. Ubiquinone/Ubiquinol
- D. Fe³⁺/Fe²⁺ (Correct Answer)
Explanation: ***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.