Catalytic-site design for inverse heavy-enzyme isotope effects in human purine nucleoside phosphorylase.
Harijan, Rajesh K; Zoi, Ioanna; Antoniou, Dimitri; Schwartz, Steven D; Schramm, Vern L.
Proc Natl Acad Sci U S A
; 114(25): 6456-6461, 2017 06 20.
Artigo em Inglês | MEDLINE | ID: mdl-28584087
Inverse enzyme isotope effects in human purine nucleoside phosphorylase with heavy asparagine labels.
Isotope-specific and amino acid-specific heavy atom substitutions alter barrier crossing in human purine nucleoside phosphorylase.
Modulating Enzyme Catalysis through Mutations Designed to Alter Rapid Protein Dynamics.
Catalytic site cooperativity in dimeric methylthioadenosine nucleosidase.
Femtosecond dynamics coupled to chemical barrier crossing in a Born-Oppenheimer enzyme.
Atomic detail of chemical transformation at the transition state of an enzymatic reaction.
Tri-Cyclic Nucleobase Analogs and their Ribosides as Substrates of Purine-Nucleoside Phosphorylases. II Guanine and Isoguanine Derivatives.
Distortional binding of transition state analogs to human purine nucleoside phosphorylase probed by magic angle spinning solid-state NMR.
Site-Selective Ribosylation of Fluorescent Nucleobase Analogs Using Purine-Nucleoside Phosphorylase as a Catalyst: Effects of Point Mutations.
Neutron structures of the Helicobacter pylori 5'-methylthioadenosine nucleosidase highlight proton sharing and protonation states.