Subtopic: Nature of Enzyme action
Enzyme-Substrate Interaction
- 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.