Proteins - Lecture Ten Flashcards
How does an enzyme catalyse a reaction?
1
Q
Covalent catalysis
A
Involves the formation of a reactive, short-lived intermediate, which is covalently attached to the enzyme, this often involves s nucleophilic attack
2
Q
Ionisation
A
May be part of the activation to the transition state
3
Q
Acid-base catalysis
A
Groups need to be in correct ionisation state for catalytic mechanism to proceed
4
Q
Histidine in acid-base catalysis
A
Histidine is particularly suitable to these types of reactions and depending on the environment of the active site His can donate or accept a proton
5
Q
Catalytic triad
A
Comprises serine, histidine and aspartic acid
6
Q
Oxyanion hole
A
Stabilises tetrahedral intermediate, and is where the oxygen sits in the final product
