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What happens to an allosteric enzyme when the concentration of substrate around the molecule increases?
Wiki User
∙ 15y ago
THE ANSWER IS B (IT INCREASES IT'S PROCESSING CAPACITY) JUST DID THE TEST the answer is definitely B
Wiki User
∙ 15y ago
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How do allosteric regulation and competitive inhibition compare?
A competitive inhibition and allosteric regulation both involves an inhibitor molecule binding to the enzyme at a different area. The difference between the two is that allosteric inhibitors are modulator molecules which bind somewhere besides the catalytic activity.
The molecule on which an enzyme acts is called an?
The substance on which enzymes act are called substrates.
The specificity of an enzyme is due to its active siteThe active site is a shape only a certain?
An enzyme's active site will bind with only a specific substrate. Any other kind of substrate will be rejected by the active site.
An allosteric receptor embedded in a cell membrane will change shape only?
when a signal molecule fits the shape of the receptor
The substance acted upon by an enzyme is called its?
A substrate is the substance acted upon by an enzyme. The enzyme substrate complex is when an enzyme molecule combines with its substrates.
The particular region of an enzyme molecule that combines with the substrate it acts upon is called what?
The area where a molecule other than substrate can attach is called the allosteric site.
What is found in allosteric enzymatic regulation?
An allosteric enzyme is one in which the activity of the enzyme can be controlled by the biniding of a molecule to the "allosteric site". This really just means somewhere other than the active site. Thus allosteric control of an enzyme can be classed in two ways. A positive allosteric modification is the binding of a molecule to the enzyme which increase the rate of reaction. Sort of like catalysing the catalysing effect of an enzyme. Obviously the opposite is true of negative allosteric modification. A good example for this is the activity of phosphofructokinase, which is promoted by a high AMP concentration, and inhibited by a high ATP concentration. This should make sense if you think about the action of a kinase etc.
What happens during allosteric inhibition?
Allosteric (noncompetitive) inhibition results from a change in the shape of the active site when an inhibitor binds to an allosteric site. When this occurs the substrate cannot bind to its active site due to the fact that the active site has changed shape and the substrate no longer fits. Allosteric activation results when the binding of an activator molecule to an allosteric site causes a change in the active site that makes it capable of binding substrate.
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.
How are enzymes affected by concentration levels?
Higher concentration will mean that there is a higher probability that the substrate will find the enzyme. There will be a point though that you will start seeing dimishing returns as the concentration is sufficient for every enzyme molecule to have a substrate all the time.
Is hemoglobin allosteric?
Yes, Hemoglobin (Hb) is allosteric - it is also cooperative, which is a related but separate phenomenon. An allosteric protein has binding sites for effectors that can alter binding of another molecule or substrate. These effectors can be positive or negative. Hemoglobin has many negative effectors, which cause it to release the O2 that it is carrying. These include 2,3, Bisphosphoglycerate, Carbon Dioxide, and H+ (low pH).
Where is the substrate that binds to an enzyme?
A substrate molecule needs to interact with the enzyme's active center (known as "active site") for the enzyme mediated catalytic conversion of substrate into product. Some times, this could or may bind to a second site of an enzyme named, "allosteric site" that would not form the product.
How do allosteric regulation and competitive inhibition compare?
A competitive inhibition and allosteric regulation both involves an inhibitor molecule binding to the enzyme at a different area. The difference between the two is that allosteric inhibitors are modulator molecules which bind somewhere besides the catalytic activity.
What is substrate molecule?
Is a molecule upon which an enzyme acts. e.g. hydrogen peroxide is the substrate for the enzyme catalase
Who does the substrate work on enzyme action?
The substrate is the molecule(s) that an enzyme works on
Why does a higher concentration make a reaction go faster?
When the concentration of a solution increases, the particles are moving quicker as they have more energy. This results in more collisions between the substrate and the solution, thus resulting in an increased rate of reaction. Even if the particles are moving at the same speed, with a higher concentration, there is a higher probability of colliding with another reactant molecule rather than a solvent molecule.
What is a true substrate?
It acts as a reactant. In a chemical reaction A substrate is a molecule that is reacted on by enzymes.
