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. 2014 Feb 28;9(2):e89671. doi: 10.1371/journal.pone.0089671

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
Inline graphic 0.23 Inline graphic Autophosphorylation of D, forward reaction rate constant
Inline graphic 5.1×10−6 Inline graphic Autophosphorylation of D, backward reaction rate constant
Inline graphic 2.27×103 Inline graphic Phosphotransfer to E, forward reaction rate constant
Inline graphic 8.7×10−4 Inline graphic Phosphotransfer to E, backward reaction rate constant
Inline graphic 40.6×10−3 Inline graphic Dephosphorylation of EP by D
Inline graphic 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 Inline graphic DNA-binding of free EP, equilibrium dissociation constant
α 2.59×10−3 Inline graphic Affinity factor
ktr 1.06×104 Inline graphic Transcription rate constant
kz 21.74 Inline graphic Transcript degradation rate constant
Translation
ktl1 5.4 Inline graphic Translation rate constant of D
ktl2 162 Inline graphic Translation rate constant of E
ktl3 8.1×103 Inline graphic Translation rate constant of F
kd,F 4.8 11.4 4.8 Inline graphic Degradation rate constant of F
kd 0.2 Inline graphic Degradation rate constant of D and E
Potassium pools
kKdp 7.86×103 0.46×103 Inline graphic K+ uptake rate constant; given that Inline graphic at steady state and cell dry weight is DW = 2.8×10−13 g, one obtains an estimate of Inline graphic; in the literature we find Inline graphic [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 Inline graphic Maximum velocity of K+ uptake by Trk
KM,Trk 0.1 mM Half saturation constant of K+ uptake by Trk
Vmax,Ktr 0 400 Inline graphic 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 Inline graphic Maximum K+ release rate due to cell lysis
KM,lys 150 mM Half saturation constant of K+ release due to cell lysis
kbind 8 Inline graphic Binding rate constant of free K+
KM,free 250 mM
kdiss 7.81 Inline graphic 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 Inline graphic Maximum growth rate
kμ,2 1.43×10−3 1.52×10−3 1.57×10−3 Inline graphic Carrying capacity, inflection point of growth curve
Inline graphic 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.