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.
Enzymes are proteins that catalyse (speed up) a reaction. They are very specific; enzymes will only bind a very specific molecule (or molecules containing a very specific chemical group). They normally have no effect on molecules that are not their substrate (the specific type of molecule they can interact with). Enzymes work because they have a specific shape and an 'active site'. The active site is the part of the enzyme that will bind its substrate and it may be charged in specific places so that it attracts and binds tightly to the substrate. Because the active site is the right shape and charge for the substrate, it can bind it efficiently and when it does this it causes the enzyme to change shape and catalyse a chemical reaction. Other molecules that are the wrong size, shape or charge will simply not fit into the active site or will be repelled, so the enzyme doesn't affect them. Some enzymes contain complex metal ions at their active site which help create the right conditions to bind the substrate, by adding a certain charge in a certain place. Enzymes can be 'fooled' by molecules of a very similar size, shape and charge as their normal substrate. Many toxins work in this way, by being similar to a certain molecule that the enzyme normally binds to. The toxins cause a problem because they are slightly different from the actual substrate and so don't react but just occupy the active site permanently or until they fall out. This means that the enzyme is useless.
Valence electrons are the electrons in an atom that are involved in chemical bonding. These electrons are located in the outermost energy level of the atom and determine the atom's reactivity and ability to form bonds with other atoms.
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
A substrate doesn't 'know' anything. The interaction of enzymes with substrates depends on random collisions to take 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.
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.
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
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.