Modulating Enzyme Catalysis through Mutations Designed to Alter Rapid Protein Dynamics.
Zoi, Ioanna; Suarez, Javier; Antoniou, Dimitri; Cameron, Scott A; Schramm, Vern L; Schwartz, Steven D.
J Am Chem Soc
; 138(10): 3403-9, 2016 Mar 16.
Artigo em Inglês | MEDLINE | ID: mdl-26927977
Inverse enzyme isotope effects in human purine nucleoside phosphorylase with heavy asparagine labels.
Catalytic site cooperativity in dimeric methylthioadenosine nucleosidase.
Inhibition and structure of Toxoplasma gondii purine nucleoside phosphorylase.
Purine nucleoside phosphorylase activity decline is linked to the decay of the trimeric form of the enzyme.
Site-Selective Ribosylation of Fluorescent Nucleobase Analogs Using Purine-Nucleoside Phosphorylase as a Catalyst: Effects of Point Mutations.
Isotope-specific and amino acid-specific heavy atom substitutions alter barrier crossing in human purine nucleoside phosphorylase.
Catalytic-site design for inverse heavy-enzyme isotope effects in human purine nucleoside phosphorylase.
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Computer Simulations Reveal Substrate Specificity of Glycosidic Bond Cleavage in Native and Mutant Human Purine Nucleoside Phosphorylase.
Thermodynamics of the Purine Nucleoside Phosphorylase Reaction Revealed by Computer Simulations.