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Question 1

enzymes

Answer 1

made up of globular proteins
-active site which is specific due folding and bonding in tertiary structure
-intrecellular and extracellular

Question 2

lock and key model

Answer 2

enxymes act like a lock and the substrate fits like a key due to tertiary structure

Question 3

induced fit hypothesis

Answer 3

enzyme is the glove and the substrate is like your hand

enzyme active site is induced by substrate to become perfectly complementary

enzyme- substrate complex puts strains on the bonds causing lower activation enenrgy

Question 4

q10 formula

Answer 4

R2/R1
R1= rate of reaction at temperature
R2=rate of reaction at temperature +10c

Question 5

inhibitors

Answer 5

competitive:
similar to substrate and binds to active site
-forming enxyme-inhibitor complex
-to reverse use a high substrate concentration

Non-competitive:
bind onto the enzyme at the allosteric site
-causes actiive site to change

End product inhibitors:
controls reactions

Question 6

co enzyme and co factors

Answer 6

bind to the active site to make the substrate complementary to the enzyme

co enzymes are organic
co factors are inorganic(dont contain carbon)

Question 7

Prosthetic groups

Answer 7

type of cofactors but are permanently attached to the enzyme by non/covalent forces

Question 8

precursor activation

Answer 8

enzymes are activated by the binding of a cofactor causing a change in tertiary structure, allowing substrates to bind

-precursor protein (inactive enzyme) AKA apoenzyme is activated by the holoenzyme which is the cofactor