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• W2001737752 startingPage "6140" @default.
• W2001737752 abstract "Prolidases are dipeptidases specific for cleavage of Xaa‐Pro dipeptides. Pyrococcus furiosus prolidase is a homodimer having one Co‐bound dinuclear metal cluster per monomer with one tightly bound Co(II) site and the other loosely bound ( K d 0.24 mM). To identify which Co site is tight‐binding and which is loose‐binding, site‐directed mutagenesis was used to modify amino acid residues that participate in binding the Co1 (E‐313 and H‐284), the Co2 site (D‐209) or the bidentate ligand (E‐327). Metal‐content, enzyme activity and CD‐spectra analyses of D209A‐, H284L‐, and E327L‐prolidase mutants show that Co1 is the tight‐binding and Co2 the loose‐binding metal center." @default.
• W2001737752 created "2016-06-24" @default.
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• W2001737752 date "2005-10-11" @default.
• W2001737752 modified "2023-10-13" @default.
• W2001737752 title "Characterization of the dinuclear metal center of<i>Pyrococcus furiosus</i>prolidase by analysis of targeted mutants" @default.
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• W2001737752 doi "https://doi.org/10.1016/j.febslet.2005.09.086" @default.
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