0
Does the enzyme pick up another substrate that fits since it was deformed from the allosteric site?
Wiki User
∙ 12y ago
I have an enzyme with activity 218 u/mg enzyme, How can I pick up 0.12 u/ml enzyme?
Wiki User
∙ 12y ago
Add your answer:
Earn +20 pts
What can effect how the enzyme and substrate come together?
Shape of substrate, shape of the enzyme, Competitive, noncompetitive and allosteric inhibitors.
What would be unlikely to contribute to the substrate specificity of an enzyme?
The allosteric site is distinct from the active site, and does not affect the substrate specificity of the enzyme
What happens to an allosteric enzyme when the concentration of substrate around the?
B. it increases its processin capacity
In an allosteric enzyme the homotropic effect is seen when?
Ahh... A fine question. The answer: When a substrate acts as an effector there are homotropic effects. The substrate binds to the active site and induces allosteric-like effects.
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.
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.
Why does adding additional substrate overcome competitive but not noncompetitive inhibition?
A competitive inhibitor competes with the substrate to bind to the active site while a noncompetitive inhibitor binds to an allosteric site of the enzyme (one other than the active site). Thus no amount of substrate can overcome or in a sense interfere with the inhibitors binding to an allosteric site.
Does Allosteric regulation depends on inhibitors binding to the active site of enzymes?
Of course. That is the meaning of ' noncompetitive inhibitor. ' It does not compete with the substrate at the active site but inhibits enzyme activity at the allosteric ( other site ) site.
What blocks enzyme activity by binding to allosteric site of an enzyme causing the enzyme's active site to change shape?
An allosteric inhibitor stops enzyme activity by binding to an allosteric site and causing the conformation of the enzyme to change.
What happens to an allosteric enzyme when the concentration of substrate around the molecule increases?
THE ANSWER IS B (IT INCREASES IT'S PROCESSING CAPACITY) JUST DID THE TEST the answer is definitely B
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.
