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http://purl.uniprot.org/citations/9610360http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9610360http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9610360http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/9610360http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/9610360http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1998.8616"xsd:string
http://purl.uniprot.org/citations/9610360http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1998.8616"xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/author"Becker A."xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/author"Becker A."xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/author"Schlichting I."xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/author"Schlichting I."xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/author"Kabsch W."xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/author"Kabsch W."xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/author"Schultz S."xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/author"Schultz S."xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/author"Groche D."xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/author"Groche D."xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/author"Wagner A.F."xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/author"Wagner A.F."xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/pages"342-346"xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/pages"342-346"xsd:string
http://purl.uniprot.org/citations/9610360http://purl.uniprot.org/core/title"Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site."xsd:string