PMID:9883883

Citation	Sundaram, AK, Howe, DL, Sheflyan, GY and Woodard, RW (1998) Probing the potential metal binding site in Escherichia coli 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (phenylalanine-sensitive). FEBS Lett. 441:195-9
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.
Links	PubMed
Keywords	3-Deoxy-7-Phosphoheptulonate Synthase/chemistry; 3-Deoxy-7-Phosphoheptulonate Synthase/genetics; 3-Deoxy-7-Phosphoheptulonate Synthase/metabolism; Base Sequence; Binding Sites; DNA Primers; Escherichia coli/enzymology; Kinetics; Metals/metabolism; Molecular Probes; Mutagenesis, Site-Directed; Phenylalanine/pharmacology
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