Eric J. Toone's Advances in Enzymology and Related Areas of Molecular PDF

By Eric J. Toone

ISBN-10: 0470638354

ISBN-13: 9780470638354

This booklet covers important advances in enzymology, explaining the habit of enzymes and the way they are often applied to improve novel medications, synthesize recognized and novel compounds, and comprehend evolutionary methods.

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Extra resources for Advances in Enzymology and Related Areas of Molecular Biology (Volume 77)

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The opening of the cleft is indicated approximately by the large red ellipse. AcrB residues corresponding to those MexD residues affecting the substrate specificity (81) (Phe610, Gln34, Glu89, and Thr676) are shown in space-filling models, as well as those that were shown to affect drug pumping by site-directed mutagenesis (88) (Phe664, Phe666, and Glu673). A, is shown by stick models (ciprofloxacin, yellow; nafcillin, green; ethidium, magenta; rhodamine 6G, salmon; and PheArg-b-naphthylamide, orange).

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.

Middlemiss and Poole (83) used a different approach and carried out an in vitro random mutagenesis of the mexB gene from P. aeruginosa. B), or Gly220 mutant in the “peg” that is inserted into the periplasmic domain of the neighboring protomer. The mutants that are significantly altered in the substrate specificity, in contrast, often contained alterations in the periplasmic domain, as expected. Among these, alterations of Ala618 and Arg716 22 HIROSHI NIKAIDO Figure 6. Large cleft of the AcrB periplasmic domain, seen from the outside.

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Advances in Enzymology and Related Areas of Molecular Biology (Volume 77) by Eric J. Toone

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