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• W2017781609 abstract "The active site residues of the proposed metal binding site of DAH 7-P synthase (phe) were probed by site-directed mutagenesis of C61 to glycine and serine, H64 to glycine, and with the double mutant C61H/H64C. While C61S and C61H/ H64C were inactive, both C61G and H64G were active. All mutants, regardless of enzymatic activity, bound one equivalent of Fe2+ per monomeric unit. Even though C61 and H64 were shown not to be metal ligands for the DAH 7-P synthase (phe), they may provide some of the backbone interactions/secondary structural elements necessary to properly form the metal binding pocket." @default.
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• W2017781609 date "1998-12-18" @default.
• W2017781609 modified "2023-09-26" @default.
• W2017781609 title "Probing the potential metal binding site in<i>Escherichia coli</i>3-deoxy-<scp>d</scp>-<i>arabino</i>-heptulosonate 7-phosphate synthase (phenylalanine-sensitive)" @default.
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• W2017781609 doi "https://doi.org/10.1016/s0014-5793(98)01545-2" @default.
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