Unit 2 Enzyme Regulations

Question 1

What are the ways to regulate enzymes?

Answer 1

1. limit the production of the enzyme
   -make no more
2. inhibit the action of enzyme:
   2.1: competitive inhibitor
   2.2: non-competitive inhibitor
   2.3: feedback inhibition

Question 2

What is the point of enzyme regulation?

Answer 2

to slow down chemical reactions in the body –>to control cellular activities

Question 3

what are inhibitors?

Answer 3

molecules that bind to enzymes to slow them down (decrease activity)

Question 4

Explain the difference between competitive vs non-competitive inhibition.

Answer 4

Competitive inhibition:
-inhibitor binds to active site
-blocks substrate

non-competitive (allosteric inhibition):
-binds to allosteric site (literally anywhere else on the enzyme other than the active site)
-changes shape of active site (functional group reaction blah blah blah)

Question 5

Explain the difference between Allosteric activators vs allosteric inhibitors

Answer 5

allosteric activators:
-binds to allosteric site
-changes shape of active site(functional group and such) (allosteric effect)
-allows substrate to bond to enzyme
-increases affinity enzyme has for substrate
-like –> love

allosteric inhibitors:
-binds to allosteric site
-changes shape of active site(functional group and such) (allosteric effect)
-doesn’t allow substrate to bond to enzyme
-lowers affinity enzyme has for substrate
-like –> hate

Question 6

what is feedback inhibition?

Answer 6

-prosses to regulate enzyme activity

1. substrate bind to active site
2. enzyme catalyzes reaction
3. product is produced
4. so much product is made that it attaches to allosteric site
5. product binded to enzyme is now a non-competitive inhibitor –> stopes the substrate from binding to the active sight
6. as product is used, less bind to enzyme and allow more substrate to bind to active site

ex.
-ATP
-amino acids
-cholesteral

Question 7

what is the difference between feedback inhibition vs precursor activation?

Answer 7

feedback inhibition:
lowers affinity between substrate and enzyme
(allosteric effect)

precursor activation:
Increases affinity between substrate and enzyme
(idk what precursor actually is lol)

Question 8

What is the difference between cofactors vs coenzymes?

Answer 8

cofactors:
-inorganic, non-protien group (metals)
-binds to enzyme
-contain active site
-saddle

coenzymes:
-organic
-assist enzymes with their tasks
-ex. shuttle molecules (transport stuff from one enzyme to another)
-assistant