Table 1.

Kinetic, calorimetric parameters of the enzymes and chemical reactions studied

	KM (mM)	kcat (s−1) ×104	ΔH (kJ mol−1)	α(m2) × 10−16
Catalase	62	5.8	−100	10 (9.6–11)
Urease	3	1.7	−59.6	4.5 (3.8–5.3)
Alkaline phosphatase	1.6	1.4	−43.5	16 (14–18)
Triose phosphate isomerase	1.8	1.3	−3.00	−2.5 (−6.1–1.1)

The Michaelis constant K_M and maximum turnover number k_cat are obtained from the fit to a Michaelis–Menten curve for the reaction rate as a function of substrate concentration (Extended Data Fig. 1). Values are in agreement with the ones from the supplier (Sigma) and found in the literature^17–20. ΔH is the enthalpy of the chemical reaction measured in bulk; values are reported in the literature for catalase³⁰, urease¹, triose phosphate isomerase²² and measured by isothermal titration calorimetry for alkaline phosphatase (see Extended Data Fig. 2). α is the coefficient of proportionality between the diffusion coefficient and the reaction rate, in parentheses is the 95% confidence interval.