(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. […]
Tag: csir enzymes kinetics PYQ
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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 […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
How Reaction Products Inhibit Enzyme Catalysis: Mechanisms and Impact
(DEC 2014) 59. Reaction products inhibit catalysis in enzymes by (1) covalently binding to the enzyme. (2) altering the enzyme structure (3) occupying the active site. (4) form a complex […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Selecting the Optimal Isozyme for Low Substrate Concentrations: Liver Enzyme Kinetics Explained
The correct answer is (1) A. Introduction Isozymes are enzyme variants catalyzing the same reaction but optimized for different tissue environments, frequently distinguished by their kinetic properties: the Michaelis constant (KmKm) […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Correcting Misconceptions in Enzyme Kinetics: Allosteric Behavior and Enzymatic Efficiency
(JUNE 2019) 57. Choose the INCORRECT statement from the following statements made for an enzyme- catalyzed reaction (1) The kinetic properties of allosteric enzyme do not diverge from Michaelis-Menten behaviour. […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Concerted Feedback Inhibition in Metabolic Pathways: Achieving Stoichiometric End Product Balance
The correct answer is (1) K inhibits F→G and L inhibits F→H; D→E is inhibited at equal amounts of K and L. Introduction Metabolic pathways often branch to produce multiple end […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Understanding Allosteric Regulation: Identifying Positive and Negative Effectors Through the Allosteric Constant LL
(DEC 2019 ASSAM) 55. An allosteric enzyme has two heterotropic effectors, X and Y. The allosteric constant, L for the enzyme in the absence of effector molecules is 180. For […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Understanding Negative Cooperativity in Multi-Subunit Enzymes: Mechanism and Implications
(DEC 2006) 54. If an enzyme obeying Hills reaction shows negative cooperativity. It means (1) Binding of substrate to any one site of multi-subunit enzyme decreases affinity for other substrate […]
