Binding of phosphate and sulfate anions by purine nucleoside phosphorylase from E. coli: ligand-dependent quenching of enzyme intrinsic fluorescence
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,Biochemistry,Biophysics
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1. Single tryptophan Y160W mutant of homooligomeric E. coli purine nucleoside phosphorylase implies that dimers forming the hexamer are functionally not equivalent;Scientific Reports;2021-05-27
2. Crystallographic snapshots of ligand binding to hexameric purine nucleoside phosphorylase and kinetic studies give insight into the mechanism of catalysis;Scientific Reports;2018-10-18
3. A synergistic effect of phosphate, pH and Phe159 substitution on the formycin A association to the E. coli purine nucleoside phosphorylase;Biochimie;2018-05
4. Helicobacter pyloripurine nucleoside phosphorylase shows new distribution patterns of open and closed active site conformations and unusual biochemical features;The FEBS Journal;2018-02-26
5. 1,N6-ethenoadenine and other Fluorescent Nucleobase Analogs as Substrates for Purine-Nucleoside Phosphorylases: Spectroscopic and Kinetic Studies;Current Pharmaceutical Design;2018-02-16
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