(FEB 2022-1) 25. The following statements are being made to define the Michaelis constant (KM). It is: A. Independent of enzyme concentration [E] and substrate concentration [S] B. Equal to […]
![(FEB 2022-1) 25. The following statements are being made to define the Michaelis constant (KM). It is: A. Independent of enzyme concentration [E] and substrate concentration [S] B. Equal to the dissociation constant when the [ES] complex dissociates more rapidly than product formation C. Equal to the dissociation constant when product formation is more rapid than [ES] complex dissociation D. An intrinsic property of an enzyme and does not depend on pH, temperature and ionic strength Which one of the following combination of statements is correct? (1) A and B only (2) A, B and D only (3) C and D only (4) A and D only](https://www.letstalkacademy.com/wp-content/uploads/2025/09/25.jpg)
Tag: csir enzymes kinetics PYQ
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CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Understanding Enzyme-Substrate Affinity: The Role of Michaelis Constant (Km)
(JUNE 2007) 24. If the Km of enzyme for substrate A is 1 x 10-6 and for substrate B is 4 x 10-8, it means (1) Enzyme has more affinity […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Identifying the Rate-Limiting Step in Multi-Enzyme Reactions Using Michaelis Constant (Km)
The correct answer is (4) B ⟶ C (Enzyme EB). Introduction Multistep biochemical pathways often involve several enzyme-catalyzed reactions, each with unique kinetic properties. The rate-limiting step determines the overall speed […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Michaelis-Menten Enzyme Kinetics: Understanding Km, kcat, and Their Relationships
The correct answer is (2) B and D. Introduction Michaelis-Menten kinetics is essential for understanding how enzymes catalyze biochemical reactions. Two critical parameters—Km (Michaelis constant) and kcat (turnover number)—describe how efficiently […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Clarifying Enzyme Kinetics and Inhibition: Correct Statements on Substrate Concentration and Reaction Velocity
(DEC 2019 ASSAM) 21. Following are statements on enzyme kinetics. Choose the correct statement. (1) Sufficiently high concentrations of substrate cannot completely relieve competitive inhibition. (2) Sufficiently high concentrations of […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Understanding Michaelis-Menten Equation: Key Assumptions and Rate-Limiting Step
(DEC 2011) 19. Michaelis and Menten derived their equation using which of the following assumption? (1) Rate limiting step in the reaction is the breakdown of ES complex to product […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Role of Restriction Endonucleases in Viral Defense and Impact of Enzyme Turnover Rate on Host Benefit
(JUNE 2011) 18. A researcher has isolated a restriction endonuclease that cleaves at only one specific 10 base pair site. A) Would this enzyme be useful in protecting cells from […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Roles of Coenzymes as Transient Chemical Group Carriers: Comprehensive Matching Guide
The correct answer is (2) A-(ii), B-(i), C-(iv), D-(iii). Introduction Coenzymes are vital non-protein molecules that partner with enzymes to catalyze a wide range of biological reactions. They often serve as […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Calculating Equilibrium Constant in Enzyme-Catalyzed Reaction with Rate Enhancement
The correct answer is (3) 10. Introduction Understanding the relationship between rate constants and equilibrium constants in enzyme-catalyzed reactions is critical in biochemistry. Enzymes accelerate reactions but do not alter their […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Calculating Equilibrium Constant in Enzyme-Catalyzed Reaction with Rate Enhancement
(NOV 2020-1) 15. The rate constant for conversion of a substrate into the product is 10-4 s-1, while the reverse rate constant 10-6 s-1. An enzyme enhance the rate of […]
