TABLE 1.

List of parameter values deduced from independent experiments and literature sources

Parameters	Description	Value	Units
α1	Degradation rate of Pel proteina	4.94 × 10−2	h−1
α2	Degradation rate of KdgR proteina	3.47 × 10−2	h−1
β2	Maximum rate of synthesis of KdgRb	7.00 × 10−2	μm·h−1
Km	Michaelis-Menten constant for Pel·PGA complexa	6.8	mm
Kd3	Equilibrium dissociation constant for KdgR2·KDG2 complexc	0.4	mm
kcat	Rate constant of the enzymatic Pel reactions in purified conditionsd	6 × 104	min−1

^a The weight-characterized Michaelis-Menten constant K_M = 1.2 g/liter has been measured in independent experiments as reported in this paper. From this value, one deduces the molar Michaelis-Menten constant K_m = K_M/P, where P is the molecular weight of the galacturonate (p = 176 Da) (30). For a theoretical discussion of the relation between K_M and K_m, see also supplemental material (Section 3).

^b Using the estimate that the number of KdgR₂ molecules measured during the growth phase is about 700 molecules/bacteria.

^c Approximately 0.4 mm of KDG is required for a dissociation of 50% KdgR operator complexes (16). Let us note that the molecular weight of KDG (C₆O₆H₁₀) is 178 Da, which is close to that of the galacturonate residue (176 Da).

^d The k_cat of the five major Pel enzymes were measured in purified conditions, as reported in Ref. 30.