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What happens when increasing the substrate concentration when there is less substrate than enzyme?

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?


What happens if the enzyme concentration is low?

An enzyme can overcome the presence of a competitive inhibitor by increasing the substrate concentration The reaction rate falls direct propartional to the concentration fall (which is the result of that same reaction). This is called 'first order reaction rate'.


The effect of substrate concentration on the rate of reaction of h202 and catalase?

As the substrate concentration increases, so will the enzyme activity and hence there will be a quick reaction. however, only up to a certain point ( where, if you drew a graph of the reaction, the line will level off ) as all the active sites in the enzyme are occupied and the reaction cannot go any faster. Here more enzymes will be needed to speed up the reaction.


What is the Effect of dilution on enzyme activity?

At a high ion concentration, the ion interfere with the bonds between the side groups of the amino acids making up the enzyme (which is a protein). This causes the enzyme to lose its shape, called denaturation. If the enzyme loses its shape, it can no longer accept and react substrate, so the rate of enzyme activity decreases.


What does a lower substrate concentration signify in enzymatic reactions?

A lower substrate concentration in enzymatic reactions indicates that there is less of the molecule that the enzyme acts upon. This can affect the rate of the reaction, as enzymes require substrates to bind to and convert into products. With lower substrate concentrations, the reaction may proceed more slowly until more substrates are available for the enzyme to work on.


Describe the change in the rate of reaction when the enzyme concentration is increased?

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.


What is the unit of specificity constant?

The unit of specificity constant is typically expressed in units of M^(-1)·s^(-1) since it represents the efficiency of an enzyme in converting substrate to product per unit time for a given substrate concentration. The lower the value of the specificity constant, the less efficient the enzyme is at converting substrate to product.


Competitive inhibitors and how they work?

Inhibitors are substances that alter the activity of enzymes by combining with them in a way that influence the binding of substrate and/or its turnover number. Many inhibitors are substances that structurally resemble their enzyme's substrate but either do not react or react very slowly compared to substrate.There are two kinds of inhibitors: a) competitive inhibitors (those compete directly with a normal substrate for an enzyme-binding site), and b) uncompetitive inhibitors (these bind directly to the enzyme-substrate complex but not to the free enzyme).


What does increased Vmax suggest?

An increase in Vmax suggests an increase in the maximum rate of an enzymatic reaction, indicating an enhancement in the enzyme's catalytic activity. This could be due to factors such as increased enzyme concentration, enzyme efficiency, or substrate availability. An increased Vmax can also indicate a higher affinity between the enzyme and substrate.


What happens to the rate of enzyme reaction when you increase the enzyme concentration?

As the enzyme concentration increases, the rate of reaction will increase because there are many more enzymes present to aid break down the substrate. However, a point will be reached when no matter how much enzyme is present, the reaction will not occur any quicker. This is equilibrium. This happens because all the substrate is being broken down by the exact same amount of enzyme, so enzymes will be present which have no substrate to break down.


What causes the enzymes active site to change shape?

When too much of a certain compound is made, the compound attaches to a separate site called allosteric site. When attached to the allosteric site, it changes the active site's shape and prevents any more to be made.


Where does a noncompetitive inhibitor bind in relation to the enzyme-substrate complex?

A noncompetitive inhibitor binds to the enzyme at a location other than the active site, which is where the substrate normally binds. This binding changes the shape of the enzyme, making it less effective at catalyzing the reaction with the substrate.