The gluconate metabolism in Escherichia coli involves duplicate activities of transport and phosphorylation for gluconate. In both cases, these activities can be differentiated in vitro by their different affinities for the substrate. In addition, the two gluconokinases can be differentiated by their heat sensitivities. The technique of continuous culture was used to investigate the influence of the growth rate on this metabolism in an E. coli HfrG6 strain during gluconate-limited growth under conditions of high and low oxygen concentrations. The transport and phosphorylation for gluconate, induced when the cells are cultivated in media with gluconate were differently influenced by the culture dilution rate. These activities were induced under the two conditions investigated; however, the low affinity transport system for gluconate and the thermosensitive gluconokinase were not detected under conditions of high and low oxygen concentrations, respectively. The induction of the dehydratase was favoured under conditions of low oxygen concentration. The experimental data suggest that induction and repression work together to regulate the levels of these activities during gluconate-limited growth conditions. Furthermore, that an effector molecule distinct from gluconate might be involved in the induction of the dehydratase.