By Eric J. Toone

This publication covers important advances in enzymology, explaining the habit of enzymes and the way they are often applied to increase novel medicines, synthesize identified and novel compounds, and comprehend evolutionary strategies.

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The affinity of substrates for AcrB was estimated in two ways. First, the substrates were added as potential competitors in the fluorescent phospholipid efflux assay. This showed that conjugated bile acids, such as taurocholate, were the most effective inhibitors of phospholipid efflux. Second, the potential substrates were added in the proton efflux assay, and again taurocholate was the most effective in producing proton efflux among the compounds tested (Figure 8). These results fit the notion that the natural substrate for the AcrB pump are the bile salts, most of which exist in the conjugated form in the intestinal tract of higher animals.

Interestingly, when the assay was extended to cephalosporins that were clinically useful, such as cephalothin, cefamandole, and cephaloridine, kinetics with strong positive cooperativity was observed (Figure 5B). Although it is not clear why such kinetics were not observed with nitrocefin, we note that nitrocefin has a much lower Km value than that of these compounds. 9 Â 10À2 cm3 mgÀ1 sÀ1), although the Vmax for cephaloridine was 80 times higher than that for nitrocefin. The results on cephaloridine merit close attention for several reasons.

A similar situation was found more recently with the MFP MacA for the activation of an ABC efflux transporter MacB (30). Results obtained with streptomycin are shown in Figure 9. When streptomycin was added to the external medium, the drug is occupying a more alkaline compartment that is similar to the cytosol in intact cells. Under such a setup, we could not detect stimulation of proton efflux (curve 2); however, a strong stimulation was observed when streptomycin 30 HIROSHI NIKAIDO Figure 9. Proton flux assay of reconstituted AcrD with streptomycin.

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