Table 4.
Fitting dataset
| Measurement (source) | Temperature (°C) | [KaiA] (μM) a | ATP | Time points | Phosphoform |
|---|---|---|---|---|---|
| Phosphorylation (this work) | 30 | 0.375, 0.75, 1.50, 3.00, 4.50, 6.00 | 10, 25, 100%b | 8 | U, T, D c |
| Dephosphorylation (Rust et al, 2011) | 30 | 1.4 | 5 mM | 21 | |
| ADP production (Terauchi et al, 2007) | 30 | 1.2 | 1 mM | 1 | N/A |
| KaiA on/off rates (Kageyama et al, 2006) | 25 | Variable | 1 mM | N/A | Likely U |
| KaiA dwell time (Mori et al, 2018) | 25–28 | 1.0 | N/A | N/A | T, S, D d |
a
We report here on the KaiA monomer concentration. However, since KaiA functions as a dimer, all KaiA concentration is divided by two in the models.
b
%ATP, defined as 100%[ATP]/([ATP] + [ADP]); total [ATP] + [ADP] is held constant at 5 mM.
c
The conservation of mass constraint implies that one of the four phosphoforms is not a free state variable. We have chosen the S phosphoform to be the constrained state variable.
d
Phosphomimetic mutants.