AP BIO -- CH 8.5 [REGULATION OF
ENZYME ACTIVITY EXAM QUESTIONS
AND ANSWERS
allosteric site - ANSWER-A site on an enzyme other than the active site, to which a
specific substance binds, thereby changing the shape and activity of the enzyme.
where do activating or inhibting regulatory molecules usually bind? - ANSWER-to an
allosteric site where subunits join
what does the binding of an activator stabilize? - ANSWER-active (proper) shape of
enzyme
what does the binding of an inhibitor stabilize? - ANSWER-inactive (incorrect) form
of enzyme by keeping enzyme from performing function
does a shape change in 1 allosteric subunit change all of the subunits? - ANSWER-
yes
cooperativity - ANSWER-amplifies the response of enzymes to substrates
Why is cooperativity allosteric? - ANSWER-when the active site is filled, the active
site changes and once the substrate leaves the active site the active site will go back
to previous shape before the substrate was in it
hemoglobin is made of 4 subunits each with a...
how does the attraction for O2 increase in hemoglobin? - ANSWER-O2 binding site /
more O2 binding sites are filled
feedback inhibition - ANSWER-metabolic pathway is switched off by the inhibitory
binding of its end product to an enzyme that acts early in the pathway
what is a benefit of feedback inhibition? - ANSWER-prevents cell from making too
much of the end product than necessary and wastes the chemical resources until
there are none left
how does the end product act as an inhibitor in feedback inhibition? - ANSWER-end
product binds to allosteric site instead of active site and is used up by the cell and
cannot produce anymore
3 things that increase efficiency of metabolic processes - ANSWER-1) enzymes
grouping into complexes
2) enzymes being used in membranes
3) enzymes in organelles
what do the molecules that regulate enzyme activity most nearly resemble? -
ANSWER-reversible noncompetitive inhibitors
ENZYME ACTIVITY EXAM QUESTIONS
AND ANSWERS
allosteric site - ANSWER-A site on an enzyme other than the active site, to which a
specific substance binds, thereby changing the shape and activity of the enzyme.
where do activating or inhibting regulatory molecules usually bind? - ANSWER-to an
allosteric site where subunits join
what does the binding of an activator stabilize? - ANSWER-active (proper) shape of
enzyme
what does the binding of an inhibitor stabilize? - ANSWER-inactive (incorrect) form
of enzyme by keeping enzyme from performing function
does a shape change in 1 allosteric subunit change all of the subunits? - ANSWER-
yes
cooperativity - ANSWER-amplifies the response of enzymes to substrates
Why is cooperativity allosteric? - ANSWER-when the active site is filled, the active
site changes and once the substrate leaves the active site the active site will go back
to previous shape before the substrate was in it
hemoglobin is made of 4 subunits each with a...
how does the attraction for O2 increase in hemoglobin? - ANSWER-O2 binding site /
more O2 binding sites are filled
feedback inhibition - ANSWER-metabolic pathway is switched off by the inhibitory
binding of its end product to an enzyme that acts early in the pathway
what is a benefit of feedback inhibition? - ANSWER-prevents cell from making too
much of the end product than necessary and wastes the chemical resources until
there are none left
how does the end product act as an inhibitor in feedback inhibition? - ANSWER-end
product binds to allosteric site instead of active site and is used up by the cell and
cannot produce anymore
3 things that increase efficiency of metabolic processes - ANSWER-1) enzymes
grouping into complexes
2) enzymes being used in membranes
3) enzymes in organelles
what do the molecules that regulate enzyme activity most nearly resemble? -
ANSWER-reversible noncompetitive inhibitors
