Scenario Presets
Click to loadSolution Concentrations
[Enzyme] Total
6
[Substrate] Initial / Free
30
[Competitive Inhibitor]
0
Mimics substrate shape; competes directly for the Active Site.
[Non-Competitive Inhibitor]
0
Binds Allosteric Site; changes Active Site conformation so substrate bounces off!
Interactive Visual Legend
Active Enzyme
V-Notch Active Site
Allosteric E-I
Warped Active Site
Substrate (S)
Fits V-Active Site
Products (P₁+P₂)
Catalyzed Output
Live Reaction Chamber
t = 0.0s
Select Mechanism to Inspect Up-Close:
Free [S]:
30
Products [P]:
0
Rate (V):
0.0 /s
Real-Time Enzyme State Breakdown
Free (E): 100%
E-S Complex: 0%
Comp Blocked (E-I): 0%
Allosteric (E-I): 0%
Product Formation vs. Time
Slope of line = Reaction Rate (V)
Michaelis-Menten Kinetics (V0 vs. [S])
Shows how inhibitors shift Vmax and apparent Km
Vmax: 100%
Km: 15
No Inhibitor
Normal Vmax, Km
Competitive
Same Vmax, ↑ Km
Non-Competitive
↓ Vmax, Same Km