Enzyme kinetic parameters
Michaelis constants KM, turnover numbers kcat and catalytic efficiencies kcat/KM of several enzymes, as used on the catalysis bench.
| Carbonic anhydrase | CO₂ | 0.008 | 6.0 × 10⁵ | 7.5 × 10⁷ |
|---|---|---|---|---|
| Penicillinase (β-lactamase) | benzylpenicillin | 5.0 × 10⁻⁵ | 2000 | 4.0 × 10⁷ |
| Chymotrypsin | acetyl-L-tryptophanamide | 0.005 | 100 | 20000 |
| Lysozyme | hexa-N-acetylglucosamine | 6.0 × 10⁻⁶ | 0.5 | 83000 |
KM depends on the substrate and conditions; kcat is the maximum turnover number listed in the source.