(FEB 2022-1) 28. The enzyme alkaline phosphatase was tested for its catalytic activity using the substrate para- nitrophenylphosphate. The KM obtained was 10 mM and Vmax was 100umol/min. Which one […]
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CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Substrate Concentration for Half-Maximal Velocity: Understanding Michaelis Constant (Km)
(JUNE 2010) 27. Km for enzyme is equal to where (1) V0=Vmax (2) 2V0= Vmax (3) 4V0=Vmax (4) V0 = 2 Vmax The correct answer is (2) Introduction In enzymatic reactions, […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Understanding Michaelis Constant (Km) and Its Relationship with Substrate Concentration and Initial Velocity in Enzyme Kinetics
(JUNE 2004) 26. During an enzyme assay if the initial velocity Vo = 1/2 Vmax, then substrate concentration will be equal to (1) α Km (2) Km (3) 1/2 Km […]
![(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)
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Michaelis Constant (Km) Explained: Key Properties and Assumptions in Enzyme Kinetics
(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 […]
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
Steady-State Hypothesis in Enzyme Kinetics: Explanation and Key Assumptions
(DEC 2006) 20. The steady state hypothesis for enzyme suggest that (1) Rate of formation of ES complex is equal to rate of breakdown of ES complex (2) Rate 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 […]
