By Eric J. Toone
This e-book covers important advances in enzymology, explaining the habit of enzymes and the way they are often applied to increase novel medicinal drugs, synthesize recognized and novel compounds, and comprehend evolutionary procedures.
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Additional info for Advances in Enzymology and Related Areas of Molecular Biology (Volume 77)
Rather, AcrA could have activated the pumping activity of AcrB directly, in view of the fact that AcrD, a close homolog of AcrB, is activated in a reconstituted system by AcrA (64) (see below). To show more directly that AcrB functions as a proton/drug antiporter, the system was energized by using the valinomycin-induced efflux of Kþ , which was converted into an interior-acidic proton gradient in the presence of KCl. By measuring the intravesicular pH with a fluorescent, membrane-impermeable pH indicator pyranine, we confirmed that proton efflux occurred accompanying the pH-gradient-driven operation of the pump in the presence of substrates (67) (Figure 8).
4, implicating the protonation/ deprotonation of at least this Asp residue as a key step in the proton 38 HIROSHI NIKAIDO translocation pathway, and eventually, in generating conformational alterations in AcrB that leads to drug extrusion. IV. Mechanism of Drug Efflux A. MAIN SUBSTRATE-BINDING SITE The possible route of substrate binding and extrusion is suggested by the structure of the asymmetric trimer (103–105). In the binding protomer, the periplasmic domain contains an expanded binding pocket containing several aromatic and hydrophobic residues [Phe136, 178, 610, 615, 617, and 628; Val139 and 612; Ile277 and 626; and Tyr327 (104)].
This mutant pump has an altered specificity. It produces a stronger resistance to relatively small aromatic compounds such as levofloxacin, linezolid, and tetracycline, but the resistance to nonaromatic, bulky macrolides becomes weaker than in the parent protein. A). 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.
Advances in Enzymology and Related Areas of Molecular Biology (Volume 77) by Eric J. Toone