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Table 3 Experimental data for the kinetic parameters of E. coli chemotaxis

From: Understanding system dynamics of an adaptive enzyme network from globally profiled kinetic parameters

    Description

    Reactiona

Eq7b

k(s-1)

K

Notesc[Reference]

Receptor Complex Demethylation

B P + A m ↔ K BA B P A m → k BA B P + A

v A2

1.2

0.08

k exp = 1.2 s-1[46] and K exp = 0.39 μ M [46]; k BA  = k exp and K BA  = K exp/[At].

CheB

A m + B ↔ K AB A m B → k AB A m + B P

v B1

3.2

0.281

k exp = 3.2 s-1[37] and K exp = 1.405 μ M [37]; k AB  = k exp and K AB  = K exp/[Bt].

Phosphotransfer

CheB

B P → k F B B B

v B2

0.35

-

k exp = 0.7 s-1 at 35°C, or 0.35 s-1 at 25°C [47]; k FBB  = k exp .

Dephosphotransfer

CheY

A m + C ↔ K AC A m C → k AC A m + C P

v C1

650

0.36

k exp = 650 s-1[48] and K exp = 6.5 μ M [48]; k AC  = k exp and K AC  = K exp/[Ct].

Phosphotransfer

CheY

F C + C P ↔ K F C C F C C P → k F C C F C + C

v C2

30

0.006

k exp = 650 s-1[34] and K exp = 0.1 μ M [34]; k FCC  = k exp and K FCC  = K exp/[Ct].

Dephosphotransfer

     
  1. aSuperscript m denotes methylated form and superscript p denotes phosphorylated form.
  2. bEach biochemical reaction is equivalent to the process of activation (v n1 ) or deactivation (v n2 ) (n = A, B, and C) as indicated in the NFBLB model (see equation (7) in Methods).
  3. cTotal concentrations for the CheA-bound receptor complex ([At]), CheB ([Bt]) and CheY ([Ct]) are 5.0 μM [34], 2.27 μM [37] and 17.9 μM [34], respectively. Superscript exp denotes experimental measurement.