Table 1. Optimized parameters of the mathematical Kdp model.
Parameter name | Value | Units | Description | ||
Wild type | E. coli RH010 | E. coli RH010/pKT84 | |||
Two-component system | |||||
0.23 | Autophosphorylation of D, forward reaction rate constant | ||||
5.1×10−6 | Autophosphorylation of D, backward reaction rate constant | ||||
2.27×103 | Phosphotransfer to E, forward reaction rate constant | ||||
8.7×10−4 | Phosphotransfer to E, backward reaction rate constant | ||||
40.6×10−3 | Dephosphorylation of EP by D | ||||
520 | mM | Inhibition of autophosphorylation of D by free K+ | |||
Transcription | |||||
K | 4×104 | 1.2×104 | 6×104 | 1 | Equilibrium binding constant of σ-factor and RNA polymerase to DNA |
KE | 5.32×10−2 | DNA-binding of free EP, equilibrium dissociation constant | |||
α | 2.59×10−3 | Affinity factor | |||
ktr | 1.06×104 | Transcription rate constant | |||
kz | 21.74 | Transcript degradation rate constant | |||
Translation | |||||
ktl1 | 5.4 | Translation rate constant of D | |||
ktl2 | 162 | Translation rate constant of E | |||
ktl3 | 8.1×103 | Translation rate constant of F | |||
kd,F | 4.8 | 11.4 | 4.8 | Degradation rate constant of F | |
kd | 0.2 | Degradation rate constant of D and E | |||
Potassium pools | |||||
kKdp | 7.86×103 | 0.46×103 | K+ uptake rate constant; given that at steady state and cell dry weight is DW = 2.8×10−13 g, one obtains an estimate of ; in the literature we find [56] | ||
KM,Kdp | 3.83 | 4 | mM | Half saturation constant of K+ uptake; literature value for Kdp: KM = 2 µM | |
KI,Kdp | 100 | 0 | mM | Inhibition of K+ uptake by free K+ | |
Vmax,Trk | 36.5 | Maximum velocity of K+ uptake by Trk | |||
KM,Trk | 0.1 | mM | Half saturation constant of K+ uptake by Trk | ||
Vmax,Ktr | 0 | 400 | Maximum velocity of K+ uptake by KtrAB | ||
KM,Ktr | 0 | 5×10−2 | mM | Half saturation constant of K+ uptake by KtrAB; | |
Vmax,lys | 1×10−2 | 2×10−2 | 1×10−2 | Maximum K+ release rate due to cell lysis | |
KM,lys | 150 | mM | Half saturation constant of K+ release due to cell lysis | ||
kbind | 8 | Binding rate constant of free K+ | |||
KM,free | 250 | mM | |||
kdiss | 7.81 | Dissociation rate constant of bound K+ | |||
τ | 0 | 0.35 | 0 | h | “Delay” constant for intracellular K+ exchange |
Growth | |||||
kμ,1 | 0.54 | 0.59 | 0.54 | Maximum growth rate | |
kμ,2 | 1.43×10−3 | 1.52×10−3 | 1.57×10−3 | Carrying capacity, inflection point of growth curve | |
6 | 1 | 6 | 1 | Determines maximum steepness of growth curve |
The experimental data for the wild type, the RH010 mutant and the RH010/pKT84 mutant cannot be reproduced using a single set of parameters. The Table lists the values of each parameter used to describe the dynamics of each strain.