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• W2101318753 abstract "In order to investigate the role of tryptophan residues on the activity of inorganic pyrophosphatase [EC 3.6.1.1, PPiase], several lines of experiments were carried out. Methylenediphosphonate (PCP) was found to be a competitive inhibitor for PPiase and its Ki value was found to be 1.1×10−3 M at pH 6.0. The ORD curve of PPiase-Mg2+PCP complex showed the decrease of the depth of trough at 233 mμ and apparent change of the Cotton effect around 290 mμ in shape comparing with the ORD curve of PPiase. The CD curve of PPiase-Mg2+PCP complex showed a slight blue shift of negative CD band around 290 mμ from that of PPiase. The difference spectrum between PPiase and PPiase bound with Mg2+PCP had a negative peak at 300 mμ indicating the possible participation of tryptophan residues for enzyme-inhibitor complex. These results suggested that the environment around some tryptophan residues was changed by the binding with Mg2+PCP. About one mole of tryptophan residue of PPiase was oxidized by NBS at pH 6.0–6.5 with simultaneous loss of the enzymatic activity. The rate of NBS oxidation was suppressed by the presence of Mg2+PCP. PPiase which was oxidized with NBS lost its Cotton effect around 290 mμ. These experiments described above showed that the tryptophan residue has an important role on the enzymatic activity. The fluorescence emission spectrum of PPiase excited by 295 mμ light was found to have maximum at 330 mμ and the maximum was shifted to 350 mμ in 6M guanidine-HCl. The pH dependence of fluorescence emission maximum indicated that at pH 6.0–7.5 where most of our experiments were carried out, the amount of tryptophan residues exposed to the solvent was minimum. Solvent perturbation difference spectra of PPiase in the presence and absence of Mg2+PCP using ethylene glycol as a perturbant, gave two peaks at 285 mμ and 278 mμ and a shoulder at 295 mμ. By comparing Δε at peak positions with those of N-acetyltyrosinamide and N-acetyltryptophan, it was suggested that about 10 residues of tyrosine and 2.5 residues of tryptophan were exposed to the solvent in the absence of Mg2+PCP, and that 5 residues of tyrosine and 1.4 residues of tryptophan were exposed in the presence of Mg2+PCP." @default.
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• W2101318753 date "1972-01-01" @default.
• W2101318753 modified "2023-09-25" @default.
• W2101318753 title "Studies on the Tryptophan Residues of Yeast Inorganic Pyrophosphatase in Relation to the Enzymatic Activity" @default.
• W2101318753 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a129743" @default.
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