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).
A bob of heavy mass \(m\) is suspended by a light string of length \(l\). The bob is given a horizontal velocity \(v_0\) as shown in figure. If the string gets slack at some point P making an angle \( \theta \) from the horizontal, the ratio of the speed \(v\) of the bob at point P to its initial speed \(v_0\) is :