Describe how an allosteric regulator can regulate enzyme activity.

Explanation:

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.

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i got you i did it ya know what it is just needing to fill this in for a quick task!

osteogenesis imperfecta (oi) refers to a congenital ailment of bones. in the condition, the bones become brittle or fragile. this ailment is a general result of the defect or mutations in the genes (colia1 or colia2). this mutation results in imperfect collagen formation either in quantity or quality wise.  

there are eight kinds of oi defects, and each kind varies with certain distinctions in symptoms. the usual symptoms include frequent bone fractures, loss of hearing in infants, protruding eyes, discoloration of the white in the eyes, respiratory issues, loosening of the joints, short stature, and other symptoms.