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

BMC Systems Biology

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

Description	Reaction^a	Eq7^b	k(s^-1)	K	Notes^c[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/[A_t].
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/[B_t].
Phosphotransfer	$A m + B ↔ K AB A m B → k AB A m + B P$	v _B1	3.2	0.281
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	$B P → k F B B B$	v _B2	0.35	-
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/[C_t].
Phosphotransfer	$A m + C ↔ K AC A m C → k AC A m + C P$	v _C1	650	0.36
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/[C_t].
Dephosphotransfer

^aSuperscript m denotes methylated form and superscript p denotes phosphorylated form.
^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).
^cTotal concentrations for the CheA-bound receptor complex ([A_t]), CheB ([B_t]) and CheY ([C_t]) are 5.0 μM [34], 2.27 μM [37] and 17.9 μM [34], respectively. Superscript exp denotes experimental measurement.

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