enzyme catalyze the biochemical reactions by lowering their activation energy. An enzyme which take part in such reaction wont be lost or gained any chemical structure and it would be the same after the reaction.
At low concentration of substrate , rate of enzyme action is directly proportional to conc. of substrate .
Because you will still have the same number of enzymes inhibited. For example, you have 20 enzymes and 10 non-competitive inhibitors. Regardless of substrate concentration, at any one time, there will only be 10 enzymes available to accept a substrate. Increasing the substrate concentration does not affect this.
In an allosteric enzyme, the homotropic effect occurs when the substrate acts as a ligand and binds to the active site, influencing the enzyme's activity. This binding can either enhance or inhibit the enzyme's function, depending on the specific enzyme and substrate involved.
The effect of substrate concentration on enzyme activity is characterized by an initial increase in reaction rate as substrate concentration rises, leading to more frequent enzyme-substrate collisions. However, this relationship reaches a saturation point where all active sites of the enzyme molecules are occupied, resulting in a maximum reaction rate known as Vmax. Beyond this saturation point, further increases in substrate concentration do not enhance enzyme activity, as the enzymes are already working at their maximum capacity. Thus, enzyme activity is dependent on substrate concentration up to a certain threshold, after which it plateaus.
A lone electron pair can significantly affect a molecule's geometry and reactivity. It can cause distortion in the molecular shape due to repulsion with bonding pairs of electrons, often leading to angles that deviate from idealized geometries. Additionally, lone pairs can participate in hydrogen bonding and influence the molecule's polarity, affecting its physical and chemical properties.
Kishorkumar Ratilal Shah has written: 'Radiation induced chemical bonding' -- subject(s): Effect of radiation on, Materials, Chemical bonds, Ceramic to metal bonding
For the enzyme to work, its particles must collide with the particles of the substrate. The more particles there are per unit volume, the more frequent the collisions will be. Thus changing the concentration of either chemical will have the same effect.
Basically there are two types of chemical bonding- Ionic bonding and covalent bonding, their sub classes include coordinate covalent bonding , metallic bonding and secondary type of bonding includes Hydrogen bonding , Vander waal's bonding, Dipole-Dipole interaction and London's dispersion effect.
The use of substrate in Field Effect Transistors is for it to serve as insulating material between the gate and the source.
At low concentration of substrate , rate of enzyme action is directly proportional to conc. of substrate .
Temperature, pH, substrate concentration
Basically there are two types of chemical bonding- Ionic bonding and covalent bonding, their sub classes include coordinate covalent bonding , metallic bonding and secondary type of bonding includes Hydrogen bonding , Vander waal's bonding, Dipole-Dipole interaction and London's dispersion effect.
A substrate doesn't 'know' anything. The interaction of enzymes with substrates depends on random collisions to take effect.
Stops substrate from getting to the active site
Because you will still have the same number of enzymes inhibited. For example, you have 20 enzymes and 10 non-competitive inhibitors. Regardless of substrate concentration, at any one time, there will only be 10 enzymes available to accept a substrate. Increasing the substrate concentration does not affect this.
In an allosteric enzyme, the homotropic effect occurs when the substrate acts as a ligand and binds to the active site, influencing the enzyme's activity. This binding can either enhance or inhibit the enzyme's function, depending on the specific enzyme and substrate involved.
It slows down or even stop the enzymatic activity because it compete the actove site of the enzymes with substrate and its effect can be reduced by concentrating the concentration of substrate or add more subatrate therefore more substrate are compete with the inibitors