TABLE 2.

Parameters for E. coli used in Figs. 2–4 and variables used in the model

Parameter (i = 1,2)	Description	Value used	Reference
kSi	Maximum rate of synthetase i	100 s−1	(Pedersen et al., 1978)
kR	kcat of translation	20 s−1	(Bremer and Dennis, 1987)
kai	See Appendix A	106 M−1s−1	(Schomburg et al., 2002)
KSi	Dissociation constant of deacylated tRNA i and synthetase i	10−6 M	(Schomburg et al., 2002)
Ki	Feedback inhibition constant for aai	10−4 M	(Chassagnole et al., 2001b; Neidhardt et al., 1996)
KRi	Km for ternary complex i in protein synthesis	10−6 M	(Pavlov and Ehrenberg, 1996)
t0i	Total concentration of tRNA for amino acid i	10−5 M	(Dong et al., 1996)
[Si]	Total concentration of aminoacyl-tRNA synthetase i	10−6 M	(Pedersen et al., 1978)
r	Ribosome concentration	1.67 × 10−5 M	(Bremer and Dennis, 1987; Donachie and Robinson, 1987)
fi	Usage frequency of amino acid i in protein synthesis	0.05	(Dong et al., 1996)
Variables	Description
xi	Concentration of free amino acid i
yi	Concentration of ternary complex i
ti	Concentration of deacylated tRNA i
ki	Uninhibited amino acid i synthesis rate
si	Normalized uninhibited synthesis rate of amino acid i
	Normalized inhibited synthesis rate of amino acid i
JR	Total flow of amino acid into proteins
Jmax	Maximal flow of amino acid into proteins
v	Average translation rate per ribosome
vmax	Maximal translation rate per ribosome
γ	Fraction of RelA bound to the ribosome

We estimate the experimental values to be correct with sufficient accuracy to allow for the analytical approximations in Table 1.