In an enzyme-catalyzed reaction, the velocity of the reaction increases with increasing substrate concentration until the enzyme becomes saturated. At saturation, all active sites of the enzyme are occupied by substrate molecules, and the reaction reaches its maximum velocity (Vmax). Further increases in substrate concentration do not increase the velocity because there are no free active sites available.
This relationship is described by the Michaelis-Menten equation and is graphically represented by a hyperbolic curve, as shown in option (1).
Given below are two statements: one is labelled as Assertion A and the other is labelled as Reason R.
Assertion A : The potential (V) at any axial point, at 2 m distance(r) from the centre of the dipole of dipole moment vector
\(\vec{P}\) of magnitude, 4 × 10-6 C m, is ± 9 × 103 V.
(Take \(\frac{1}{4\pi\epsilon_0}=9\times10^9\) SI units)
Reason R : \(V=±\frac{2P}{4\pi \epsilon_0r^2}\), where r is the distance of any axial point, situated at 2 m from the centre of the dipole.
In the light of the above statements, choose the correct answer from the options given below :
The output (Y) of the given logic gate is similar to the output of an/a :