In: Chemistry
what are the strategies that enzymes use for catalysis (describe each below)
Acid-Base Catalysis
Covalent Catalysis
Metal ion Catalysis
Proximity and orientation effects
Solution
All of the following strategy are used by enzyme.
Acid-Base Catalysis
Covalent Catalysis
Metal ion Catalysis
Proximity and orientation effects
Acid-base catalysid:- functional groups in enzyme structure positioned to
donate proton act as avcid and to accept proton act as base.
it helps to avoid unstable charged intermediate in the reaction
Functional groups that acts as general acid-base
_Thiol group
-Carboxylic group
-Guanidine group
-imidazole group
covalent catalysis:- they accelarate the rate by transient formation of covalent enzyme substrate bond.
Covalent intermediate are mo reactive as they have lower activation energy.
Nucleophilic attack often involved in covalent catalysis.
Metal ion catalysi:- also known as prthestic group or metalloenzyme i.e Fe2+,Zn2+
Function
-Binding and orientation
-Redox reaction
-Shielding
All kinase enzymes require Mg2+ for activity.
proximity:- reaction between bound molecules does not require improbable collision between two molecules.
orientation:- reactant not only near each other on enzyme but they are oriented in optimal position to react.