SpeciÂficiÂty: Each enzyme (E) has a speÂcifÂic subÂstrate (S) bindÂing site withÂin its strucÂture.
Enzyme-SubÂstrate ComÂplex (ES): The bindÂing site facilÂiÂtates the forÂmaÂtion of a highÂly reacÂtive, tranÂsient (short-lived) ES comÂplex.
Enzyme-ProdÂuct ComÂplex (EP): The ES comÂplex tranÂsiÂtions into an EP comÂplex.
ProdÂuct ForÂmaÂtion and Enzyme RegenÂerÂaÂtion: The EP comÂplex disÂsoÂciÂates, yieldÂing the product(s) â„— and regenÂerÂatÂing the unchanged enzyme (E).
OverÂall ReacÂtion: E + S ⇌ ES → EP → E + P
ImporÂtance of ES ForÂmaÂtion: CruÂcial for the catÂalytÂic activÂiÂty of the enzyme.
Catalytic Cycle of Enzyme Action (Step-by-Step)
1. SubÂstrate BindÂing:
The subÂstrate molÂeÂcule encounÂters the enzyme.
The subÂstrate fits specifÂiÂcalÂly into the enzyme’s active site.
Two modÂels explain this interÂacÂtion:
Lock and Key ModÂel: The subÂstrate perÂfectÂly fits the pre-existÂing active site of the enzyme, like a key in a lock.
Induced Fit ModÂel: SubÂstrate bindÂing trigÂgers a conÂforÂmaÂtionÂal change in the enzyme’s shape, allowÂing the enzyme to snugÂly fit around the subÂstrate, maxÂiÂmizÂing interÂacÂtion and staÂbiÂlizÂing the tranÂsiÂtion state. This is the curÂrentÂly favored modÂel.
2. CatalÂyÂsis (Bond BreakÂing and ProdÂuct ForÂmaÂtion):
The active site, now in close proxÂimÂiÂty to the subÂstrate, facilÂiÂtates the breakÂing of chemÂiÂcal bonds withÂin the subÂstrate.
This bond breakÂing leads to the forÂmaÂtion of the enzyme-prodÂuct comÂplex (EP).
The chemÂiÂcal transÂforÂmaÂtion of the subÂstrate occurs at this stage.
3. ProdÂuct Release and Enzyme RegenÂerÂaÂtion:
The enzyme releasÂes the newÂly formed product(s) â„— from its active site.
The enzyme returns to its origÂiÂnal conÂforÂmaÂtion.
The free enzyme is now availÂable to bind with anothÂer subÂstrate molÂeÂcule and repeat the catÂalytÂic cycle. This ensures the enzyme can catÂalyze mulÂtiÂple reacÂtions.