Optimal Activity (37°C, pH 7.0)
Rate: 0.0 reactions/s
Molecules have ideal kinetic energy. Complementary substrates fit into the specific active sites, forming Enzyme-Substrate Complexes and rapidly yielding products.
Triangle Enzyme & Substrate
Round Enzyme & Substrate
Square Enzyme & Substrate
Non-Matching Substrate
Click canvas to inject extra substrates
Products Formed
0
Total catalyzed molecules
Reaction Rate
0.0/s
Rolling 3-sec average
Active Complexes
0
E-S bound right now
Functional Enzymes
6
/ 6
(0 Denatured)
Intact active site shape
Rate vs. Temperature
100% EfficiencyGradual rise with kinetic energy up to ~37°C, followed by a steep drop as heat breaks bonds and denatures the active site.
Rate vs. pH Level
100% EfficiencyBell-shaped curve centered at the enzyme's optimum pH. Excess H⁺ or OH⁻ ions disrupt ionic bonds in the active site.
37°C
Controls molecular kinetic energy & thermal vibration
0°C (Freezing)
37°C (Body)
100°C (Boiling)
pH 7.0
Alters H⁺ / OH⁻ ion concentration & active site charges
1.0 (Strong Acid)
7.0 (Neutral)
14.0 (Strong Base)
34 Molecules
Low Concentration
High Saturation
📘 Biology Revision Notes
- Active Site & Specificity: Each enzyme has a uniquely shaped 3D pocket (active site). Only substrates with a complementary shape can bind (Lock-and-Key & Induced Fit).
- Enzyme-Substrate Complex: When a matching substrate binds, the enzyme lowers activation energy, breaking or joining bonds to form Products. The enzyme is unchanged and reused!
- Denaturation (High Temp / Extreme pH): Excessive heat or extreme pH breaks hydrogen and ionic bonds holding the protein's 3D shape. The active site warps permanently—substrates can no longer fit!