title: Substrate specificity of thymidine phosphorylase of E. coli: role of hydroxyl groups.
abstract: Substrate specificity of E. coli thymidine phosphorylase to pyrimidine nucleoside modified at 5'-, 3'-, and 2'-positions of sugar moiety has been studied. Equilibrium (K(eq)) and kinetics constants of phosphorolysis reaction of nucleosides were measured. The most important hydrogen bonds in enzyme-substrate complex have been determined.
authors.affiliation: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
authors.forename: Natalya G
authors.initials: NG
authors.lastname: Panova
authors.forename: Cyril S
authors.initials: CS
authors.lastname: Alexeev
authors.forename: Konstantin M
authors.initials: KM
authors.lastname: Polyakov
authors.forename: Sergei A
authors.initials: SA
authors.lastname: Gavryushov
authors.forename: Anatoliy M
authors.initials: AM
authors.lastname: Kritzyn
authors.forename: Sergey N
authors.initials: SN
authors.lastname: Mikhailov
mesh_terms: D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D006860:Hydrogen Bonding; D007700:Kinetics; D013379:Substrate Specificity; D013939:Thymidine Phosphorylase / Q000378:metabolism*
chemical_list: D029968:Escherichia coli Proteins; D013939:Thymidine Phosphorylase