List of top Biochemistry Questions on Enzyme kinetics asked in GATE XL

Match the anti-nutritional factor in Column I with their corresponding activity given in Column II.
Column IColumn II
(P) Lectin 1 Total amount of produced by autotrophs energy
(Q) Stachyose  2Chelates with divalent cations and reduces their bio-availability 
(R) Phytate 3Inhibits trypsin and chymotrypsin 
(S) Knuitz type inhibitor 4Hemagglutination 
An enzyme-catalyzed conversion of a substrate at 298 K proceeds by a Michaelis-Menten mechanism. The Lineweaver-Burk plot for the analysis of the experimental data has an intercept along the y-axis of 0.357 mmol\(^{-1}\) dm\(^{3}\) s and a slope of 2.10 s. The correct Michaelis constant for the reaction is ______ (rounded off to 2 decimal places).
An enzyme-catalyzed conversion of a substrate at 298 K proceeds by a Michaelis-Menten mechanism. The Lineweaver-Burk plot for the analysis of the experimental data has an intercept along the y-axis of 0.357 mmol\(^{-1}\) dm\(^{3}\) s and a slope of 2.10 s. The correct Michaelis constant for the reaction is ______ (rounded off to 2 decimal places).
The action of which class of enzyme inhibitors can be reversed by adding an excess of substrate?
The half-maximal velocity of an enzyme catalyzed reaction was found at a substrate concentration of \(0.5 \times 10^{-6} \, \text{M}\). This enzyme follows Michaelis-Menten kinetics. In the presence of a competitive inhibitor, the half-maximal velocity was found at a substrate concentration of \(1.5 \times 10^{-6} \, \text{M}\). Given that the enzyme-inhibitor pair has a dissociation constant of \(2 \times 10^{-7} \, \text{M}\), the concentration of the competitive inhibitor in \(\mu M\), rounded off to one place of decimal, was ______.
Consider the following enzyme catalyzed reaction:
where \( E \) is enzyme, \( S \) is substrate, \( ES \) is enzyme-substrate complex, and \( P \) is product. The CORRECT statement(s) for the above reaction is/are