PMID:9610360

Citation	Groche, D, Becker, A, Schlichting, I, Kabsch, W, Schultz, S and Wagner, AF (1998) Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site. Biochem. Biophys. Res. Commun. 246:342-6
Abstract	Three metallo forms of peptide deformylase (PDF, EC 3.5.1.31) of Escherichia coli were prepared and crystallized (space group C2, diffraction limit 1.9 A) for initiating the X-ray structure determination of the metal center in correlation with the catalytic functionality of this enzyme. The native Fe2+ containing enzyme species was directly isolated from overproducing bacteria by using catalase as a buffer additive, which stabilizes the catalytic activity against oxidative destruction. The Ni2+ containing form, which is oxygen-insensitive, was obtained by metal exchange with free Ni2+ and found to be catalytically equally effective (kcat/KM = 10(5) M-1 s-1 for N-formyl-Met-Ala). The Zn2+ form, prepared from the apoenzyme or by displacement of bound Ni2+ by free Zn2+, proved virtually inactive.
Links	PubMed Online version:10.1006/bbrc.1998.8616
Keywords	Amidohydrolases/chemistry; Amidohydrolases/isolation & purification; Amidohydrolases/metabolism; Binding Sites; Catalase; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Iron/chemistry; Kinetics; Nickel/chemistry; Oxidation-Reduction; Zinc/chemistry
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