Dunno. But this is pretty cool. But if i search the question, i obvioudly don't know it, so why would i be given an optionto answer it?
"The reaction rate is lowered" Sorry, I don't believe that you are correct. From what I understand having an overabundance of substrate and an enzyme there will be a constant rate. As long as the concentration of enzyme stays the same, adding more substrate molecules should not affect the initial rate of reaction but this optimum rate will continue for a longer period of time as there is more substrate to react with. THUS the rate will not be changed directly but the length of the reaction will.
The rate of enzyme reaction is increased when the substrate concentration is also increased. However, when it reaches the maximum velocity of reaction, the reaction rate remains constant.
If there is a lower substrate concentration, the rate of activity will decrease also, as the enzyme does not have as much substrate to react with.
it slows down the reaction time of the enzyme because there are too many substrates bumping into each other and make it harder for them to bind to the enzymes.
The rate of the reaction increases.
The binding of an enzyme and a substrate forms an enzyme-substrate complex. It lowers the activation energy of a chemical reaction
NO. The enzyme acts on the substrate. The substrate is the chemical/compound being altered by the action of the enzyme. They are NOT the same.
The Michaelis constant (Km) is a means of characterising an enzyme's affinity for a substrate. The Km in an enzymatic reaction is the substrate concentration at which the reaction rate is half its maximum speed. Thus, a low Km value means that the enzyme has a high affinity for the substrate (as a "little" substrate is enough to run the reaction at half its max speed). This is only true for reactions where substrate is limiting and the enzyme is NOT allosteric.
Generally in an enzyme-catalyzed reaction, the reactant is called the substrate, which in association with the enzyme forms the product.
Vmax is the maxim initial velocity (Vo) that an enzyme can achieve. Initial velocity is defined as the catalytic rate when substrate concentration is high, enough to saturate the enzyme, and the product concentration is low enough to neglect the rate of the reverse reaction. Therefore, the Vmax is the maximum catalytic rate that can be achieved by a particular enzyme. Km is determined as the substrate concentration at which 1/2 Vmax is achieved. This kinetic parameter therefore importantly defines the affinity of the substrate for the enzyme. These two parameters for a specific enzyme defines: Vmax - the rate at which a substrate will be converted to product once bound to the enzyme. Km - how effectively the enzyme would bind he substrate, hence affinity.
A for Plato users
It doesn't
It doesn't
The rate of enzyme reaction is increased when the substrate concentration is also increased. However, when it reaches the maximum velocity of reaction, the reaction rate remains constant.
Increasing enzyme concentration increases the number of collisions between the enzyme molecules and the substrate molecules. This increases the number of successful collisions and the number of enzyme-substrate complexes. Therefore the reaction rate is increased as well and enzyme activity is promoted.
false
At low concentration of substrate , rate of enzyme action is directly proportional to conc. of substrate .
B. it increases its processin capacity
As the substrate concentration increases so does the reaction rate because there is more substrate for the enzyme react with.
it is a type of enzyme.
To find out how enzyme concentration affects the activity of the enzyme you must:vary the concentration of the enzyme, by preparing different concentrations (keeping the volume of solution the same)keep the temperature, substrate concentration and pH constantmeasure the activity of the enzyme at each concentrationHow the enzyme activity is measured will depend on the specific enzyme involved.You need to have plenty of substrate (excess substrate) so it doesn't run out during the experiment.In this type of experiment, the enzyme activity is the dependent variable, the temperature, pH and substrate concentration are control variables and the enzyme concentration is the independent variable.
False