title: Binding causes the remote [5'-3H]thymidine kinetic isotope effect in human thymidine phosphorylase.
abstract: The remote 5'-3H V/K kinetic isotope effect (KIE) observed in human thymidine phosphorylase (6.1%) is significantly larger than can be explained by the reaction chemistry. One hypothesis connects the 5'-3H KIE in purine nucleoside phosphorylase to that enzyme's SN1 transition state. The transition state of thymidine phosphorylase, however, is an SN2 nucleophilic displacement. Here we report equilibrium binding isotope effects sufficiently large to explain the presence of this substantial KIE in thymidine phosphorylase.
authors.affiliation: Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, USA.
authors.forename: Matthew R
authors.initials: MR
authors.lastname: Birck
authors.forename: Vern L
authors.initials: VL
authors.lastname: Schramm
mesh_terms: D001667:Binding, Competitive; D002384:Catalysis; D006801:Humans; D007554:Isotopes; D007700:Kinetics; D015394:Molecular Structure; D011485:Protein Binding; D013936:Thymidine / Q000737:chemistry*; D013939:Thymidine Phosphorylase / Q000378:metabolism*; D014316:Tritium / Q000737:chemistry
chemical_list: D007554:Isotopes; D014316:Tritium; D013939:Thymidine Phosphorylase; D013936:Thymidine