because the competitive inhibitor stops the regular substrate from joining the enzyme. Its takes its place in the enzyme.
induced enzyme
A catalyst is a substance that accelerates a chemical reaction. It does this by lowering the activation energy necessary for that reaction to start. A catalyst is not a reactant or a product, and it does not get used up in a reaction. It is simply present with the reactants and the products and it does not change in a reaction. In an equation, it is correct to show the chemical formula for the catalyst in small characters above the "yield" arrow. The opposite of catalyst is inhibitor.
That depends on the chemicals present before the chemical reaction and sometimes the conditions under which the chemical reaction occurred.
When an enzyme binds to the appropriate substrate, subtle changes in the active site occur. This alteration of the active site is known as an induced fit.Induced fit enhances catalysis, as the enzyme converts substrate to product.Release of the products restores the enzyme to its original form. The enzyme can repeat this reaction over and over, as long as substrate molecules are present.
Oddly phased question in my opinion. Vmax is only effected by the amount of enzyme present in the reaction. Substrate concentration has zero effect on Vmax. There for I believe the answer in no. {Enzyme concentration is responsible for this}
No! A substrate is a reagent in a chemical reaction. Catalyse is the verb form of catalyst; a catalyst is a chemical species that participates in lowering the energy barrier of a chemical reaction and allow a reaction to occur more rapidly. A catalyst is not consumed in a reaction and therefore only a small amount of catalyst is required in any reaction (if required at all), whereas a substrate must be present in the proper stoichiometric amount to allow a reaction to proceed as it is consumed.
yes, it does. if there is more substrate present, the net reaction will go to the right. but if more prdouct accumulates, the reaction will slow down and eventually begin to move to the left
Generally, if you increase a reagent and there is no increase in the reaction, then it is limited by the amount of another reagent present. For example, a mole of Sodium Hydrogen Carbonate will react with a mole of Acetic Acid. However, doubling the Acetic acid will not result in a greater reaction because it is limited by the amount of Sodium Hydrogen Carbonate present.
Substrate is present
There are a number of factors that can influence how efficiently a certain enzyme can catalyse a reaction: the amount of substrate present, whether there are chemicals present that inhibit enzymes by either binding to their active site or cofactor site, the amount of enzymes present...
The bind in the active site.
In vitro, Temperature, pH and other factors leading to degradation or suboptimal activity affect enzymatic activity. All enzymes are not created equal, each enzyme functions its best at different optimal conditions.
add more substrate. The rate of the reaction drops when the enzyme no longer has a maximum number of substrate molecules to interact with. Above the maximum substrate concentration, the rate will not be increased by adding more substrate; the enzyme is already working as fast as it can. An enzyme can catalyze a certain number of reactions per second, and if there is not sufficient substrate present for it to work at its maximum velocity, the rate will decrease. Therefore, to keep the enzyme working at its maximum, you must add more substrate.
Your question makes absolutely no sense.
induced enzyme
The increase of enzyme concentration increase the rate of reaction. Given a fixed amount of substrates, it means that the substrates will be digested faster as there are more enzymes to do the work. Substrate concentration, temperature, and pH value of the surrounding where the enzymes work on also affects the rate.