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• W1979702489 startingPage "1249" @default.
• W1979702489 abstract "In the human placental glutathione transferase, Cys-47 possesses, at physiological pH values, a pKavalue of 4.2 and may exist as an ion pair with the protonated ɛ-amino group of Lys-54. Using site-directed mutagenesis we investigate spectral, kinetic, and structural properties of Cys-47 and Lys-54 mutants. The results shown indicate that the thiolate ion detected at 229 nm should be assigned exclusively to Cys-47. The contribution of Lys-54 to the activation of Cys-47 is assessed by the spectral properties of the K54A mutant enzyme. The induced cooperativity toward glutathione, as a consequence of mutation of Lys-54 to alanine, clearly parallels that observed for the Cys-47 mutant enzymes (see the preceding paper (Ricci, G., Lo Bello, M., Caccuri, A. M., Pastore, A., Nuccetelli, M., Parker, M. W., and Federici, G.(1995) J. Biol. Chem. 270, 1243-1248) and points out the importance of this electrostatic interaction in shaping the correct spatial arrangement for the binding of glutathione and in anchoring the flexible helix α 2. When this ion pair is disrupted, by mutation of either residue, the flexibility of this region could be greatly increased, causing helix α 2 to come in contact with the other subunit and generating a structural communication, which is the basis of the observed cooperativity. In the human placental glutathione transferase, Cys-47 possesses, at physiological pH values, a pKavalue of 4.2 and may exist as an ion pair with the protonated ɛ-amino group of Lys-54. Using site-directed mutagenesis we investigate spectral, kinetic, and structural properties of Cys-47 and Lys-54 mutants. The results shown indicate that the thiolate ion detected at 229 nm should be assigned exclusively to Cys-47. The contribution of Lys-54 to the activation of Cys-47 is assessed by the spectral properties of the K54A mutant enzyme. The induced cooperativity toward glutathione, as a consequence of mutation of Lys-54 to alanine, clearly parallels that observed for the Cys-47 mutant enzymes (see the preceding paper (Ricci, G., Lo Bello, M., Caccuri, A. M., Pastore, A., Nuccetelli, M., Parker, M. W., and Federici, G.(1995) J. Biol. Chem. 270, 1243-1248) and points out the importance of this electrostatic interaction in shaping the correct spatial arrangement for the binding of glutathione and in anchoring the flexible helix α 2. When this ion pair is disrupted, by mutation of either residue, the flexibility of this region could be greatly increased, causing helix α 2 to come in contact with the other subunit and generating a structural communication, which is the basis of the observed cooperativity." @default.
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• W1979702489 date "1995-01-01" @default.
• W1979702489 modified "2023-09-26" @default.
• W1979702489 title "Site-directed Mutagenesis of Human Glutathione Transferase P1-1" @default.
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• W1979702489 doi "https://doi.org/10.1074/jbc.270.3.1249" @default.
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