



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).
Match the LIST I (Enzyme) with LIST II (Catabolic Products)
| LIST-I | LIST-II | ||
|---|---|---|---|
| (Enzyme) | (Catabolic Products) | ||
| A | \(\beta\)-galactosidase | III | Galactose + glucose |
| B | Lecithinase | I | Choline + H$_3$PO$_4$ + fat |
| C | Urease | IV | CO$_2$ + NH$_3$ |
| D | Lipase | II | Glycerol + fatty acids |
What is Microalbuminuria ?
The output (Y) of the given logic implementation is similar to the output of an/a …………. gate.