(DEC 2013 GU) 69. If the product of an enzyme binds to the enzyme- substrate complex to exhibit its activity through a decrease in both Km and Vmax, this type […]
Category: CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
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CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Interpreting Enzyme Specificity Using Activity Profiles After Inhibitor and Heat Treatments
The correct answer is (3) Both X and Y are specific for the substrate, S. Introduction Substrate specificity is a key property for enzymes, defining their role in cellular metabolism and […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Lineweaver-Burk Plot Analysis for Km Determination in Reversible Non-Competitive Enzyme Inhibition
The correct answer is (1). Introduction Enzyme inhibition is a cornerstone of biochemistry and pharmacology, and visualizing its effects on kinetic parameters is essential. The Lineweaver-Burk double reciprocal plot provides a […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Non-Competitive Enzyme Inhibition: Effects on Kinetic Parameters VmaxVmax and KmKm
(JUNE 2002) 66. Which of following is true for non-competitive inhibition? (1) Increases Vmax (2) Decreases Vmax (3) Increases Km (4) Decreases Km The correct answer is (2) Decreases Vmax. Introduction […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Noncompetitive Enzyme Inhibition: Reaction Schemes, Mechanism, and Impact on Kinetics
The correct answer is (2) E+S ⇄ ES → E+P; ES+I ⇄ ESI. Introduction Noncompetitive inhibition is a fundamental model in enzyme kinetics, describing how inhibitors can reduce enzyme activity regardless […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Understanding Competitive Inhibition: How Substrate Concentration Overcomes Inhibition
(DEC 2001) 64. False statement of competitive inhibition is- (1) Structure same as substrate (2) Inhibits substrate binding (3) Binds to active site (4) Reaction cannot be favorably biased by […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Understanding Enzyme Inhibition: Why Competitive Inhibition Increases KmKm but Not VmaxVmax
(JUNE 2004) 63. During inhibition of enzyme action Vmax remains unchanged while Km is increased. Inhibition is- (1) Competitive (2) Non-competitive (3) Un-competitive (4) Allosteric The correct answer is (1) Competitive. […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Mechanism-Based (Suicide) Inhibition in Enzyme Catalysis: Penicillin’s Site of Action Explained
The correct answer is (2) K₂. Introduction Mechanism-based (suicide) inhibitors are among the most potent and specific enzyme inhibitors in biochemistry and pharmacology. Penicillin serves as a classical example, irreversibly inactivating […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Covalent Enzyme Modification and Transition State Analogs: Key Mechanisms in Enzyme Inhibition
The correct answer is (4) The given brominated compound binds to triose phosphate isomerase at the active site and covalently modifies a glutamic acid residue required for enzyme activity. Introduction Enzyme […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Enzyme Inhibition by Heavy Metals and Catalytic Activity of Monoclonal Antibodies: Clarifying Common Misconceptions
(DEC 2017) 60. Indicate the INCORRECT statement from the following: (1) Allosteric enzymes function through reversible noncovalent binding of allosteric modulators or effectors. (2) Monoclonal antibodies that catalyze hydrolysis of […]
