santababyhere is another one
Lindsey,
Many enzymes exist in two states, an inactive and an active state.
Usually these states differ in the conformation, or three-dimensional shape,
of the enzyme. The balance between these two states provides a means for
regulating the activity of the enzyme, in effect, by turning it on or off.
Often the switch that controls which state the enzyme is in is provided
by a small molecule which binds to a receptor site somewhere on the surface
of the enzyme. Such a small molecule is called an allosteric effector. For
alpha-amylases from mammals, chloride ion is the allosteric effector. These
amylases have a binding site for chloride ion, which contains a positively
charged amino acid residue (lysine, which at physiological pH is in the
ammonium ion form). This positive charge assists binding of the negatively
charged chloride ion, and the size of the binding pocket excludes larger
negative ions.
Binding of chloride causes a conformational change to the amylase,
switching it to the more active state.
thought this was gonna be a poem or bars ngl