Section 6.5: Binding Modes of Enzymatic Catalysis

Measurements have shown that the chemical effects of enzymatic catalysis only account for increases of around 10 to 100 over the uncatalyzed rate
The remainder of the rate increase is due to binding effects. There are two main types of binding effects that have been identified in enzyme catalysis:
- The proximity effect, which brings about a reduction of entropy
- Stabilization of transition state (perhaps the most important contributor to rate acceleration)
In addition to these, we'll also consider some related issues, including weak binding of substrates to enzyme, transition state analogs and catalytic antibodies