Metal dependence of the phosphate (oxygen)-water exchange reaction of Escherichia coli alkaline phosphatase. Kinetics followed by 31P(18O) NMR.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference15 articles.
1. PHOSPHATE INCORPORATION INTO ALKALINE PHOSPHATASE OF E. COLI
2. Free energy of hydrolysis of the phosphoryl-enzyme intermediate in alkaline phosphatase-catalyzed reactions
3. The Rate of Formation and Decomposition of Phosphoryl-phosphatase (Escherichia coli)
4. Negative cooperativity and half of the sites reactivity. Alkaline phosphatases of Escherichia coli with Zn2+, Co2+, Cd2+ , Mn2+ and Cu2+ ions in the active sites
5. 31P NMR of alkaline phosphatase
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1. Isotope-Edited FTIR of Alkaline Phosphatase Resolves Paradoxical Ligand Binding Properties and Suggests a Role for Ground-State Destabilization;Journal of the American Chemical Society;2011-07-13
2. 31P NMR correlation maps of 18O/16O chemical shift isotopic effects for phosphometabolite labeling studies;Journal of Biomolecular NMR;2011-05-25
3. Arginine Coordination in Enzymatic Phosphoryl Transfer: Evaluation of the Effect of Arg166 Mutations in Escherichia coli Alkaline Phosphatase;Biochemistry;2008-07-01
4. Phosphate diester hydrolysis promoted by new Cu(II) alkoxide complexes;Inorganic Chemistry Communications;2007-02
5. Detection of17O-tagged phosphate by31P MRS: A method with potential for in vivo studies of phosphorus metabolism;Magnetic Resonance in Medicine;2007
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