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• W2000514078 abstract "Abstract In this study, we have examined the transport characteristics of the wild-type lactose permease, single mutants in which Lys-319 was changed to asparagine or alanine or Glu-325 was changed to glutamine or alanine, and the corresponding double mutant strains. The wild-type and Asn-319 mutant showed high levels of lactose uptake, with K m values of 0.42 and 1.30 mm and V max values of 102.6 and 48.3 nmol of lactose/min/mg of protein, respectively. The Asn-319/Gln-325 strain had a normal K m of 0.36 mm and a moderate V max of 18.5 nmol of lactose/min/mg of protein. By comparison, the single E325Q strain had a normal K m of 0.27 mm but a very defective V max of 1.3 nmol of lactose/min/mg of protein. A similar trend was observed among the alanine substitutions at these positions, although the V max values were lower for the Ala-319 mutations. When comparing theV max values between the single position 325 mutants with those of the double mutants, these results indicate that neutral 319 mutations substantially alleviate a defect inV max caused by neutral 325 mutations. With regard to H+/lactose coupling, the wild-type permease is normally coupled and can transport lactose against a gradient. The position 325 single mutants showed no evidence of H+transport with lactose or thiodigalactoside (TDG) and were unable to facilitate uphill lactose transport. The single Asn-319 mutant and double Asn-319/Gln-325 mutant were able to transport H+upon the addition of lactose or TDG. In addition, both of these strains catalyzed a sugar-dependent H+ leak that inhibited cell growth in the presence of TDG. These two strains were also defective in uphill transport, which may be related to their sugar-dependent leak pathway. Based on these and other results in the literature, a model is presented that describes how the interactions among several ionizable residues within the lactose permease act in a concerted manner to control H+/lactose coupling. In this model, Lys-319 and Glu-325 play a central role in governing the ability of the lactose permease to couple the transport of H+ and lactose." @default.
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• W2000514078 date "1999-02-01" @default.
• W2000514078 modified "2023-10-01" @default.
• W2000514078 title "A K319N/E325Q Double Mutant of the Lactose Permease Cotransports H+ with Lactose" @default.
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• W2000514078 doi "https://doi.org/10.1074/jbc.274.7.4074" @default.
• W2000514078 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9933600" @default.
• W2000514078 hasPublicationYear "1999" @default.
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