Unit 3 Quiz Notes Flashcards
(14 cards)
Enzymes
Proteins that have certain shapes and are -vely charged in body and are catalysts
They work to reduce the activation energy to facilitate the reaction
Has a certain r group
enzyme graph
energy on the y axis
reaction progress on the x
write out reactants on one side
products on other side
in-between should be a bump for the activation energy (should be lower for enzyme)
induced fit
when the enzyme binds the substrate, the active site changes a little. this makes the catalysis faster
enzyme process ** see lesson 9 photo
1) substrate binds to active site
2) enzyme will do induced fit
3) substrate will reach an intermediate stage (all bonds are formed)
4) product will release
sodium potassium pump
sodium will bind inside, potassium will bind outside
ATPase will change structure and bind ATP
then the breakdown of ATP will release energy to allow the protein to do its job and pump out the Na and bring in the K
hemoglobin ** see lesson 9 for picture
(heme=prosthetic group, globin= protein subunit)
has 4 subunits with an iron cofactor and a prosthetic group of heme
** if there was no iron, hemoglobin would be floppy
cofactor
inorganic, has no carbon (can be a metal)
conenzyme
is organic, it has nonpermanent binding. Basically moves stuff around for an enzyme to bind to the substrate.
Prosthetic group
no amino acids in this, but it can be organic (heme)
Prosthetic groups are cofactors that bind tightly to proteins or enzymes.
irreversible inhibition
a substance with high affinity for the enzyme will bind and stay bound which means that you cannot do any function with the enzyme
ex. Sarin drug binds to acetylcholine esterase which means you cannot breakdown acetylcholine and then a muscle that contracts will not be able to contract back
reversible inhibition types
competitive and noncompetitive
competitive inhibition
reversible
- when there is another molecule that doesn’t fit into the substrate but competes with the substrate to bind to the enzyme
- it has lower affinity but it will still fit
noncompetitive inhibition
something that will bind to the allosteric site will change the shape of the active site which will effect how it binds
- Allosteric site binding can slow the enzyme or speed it up as well
allosteric site
another site that is not the active site where another susbtance can bind to influence the shape of the active site