Substrate specificity of thymidine phosphorylase of E. coli: role of hydroxyl groups.
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.
Panova
Natalya G
NG
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
Alexeev
Cyril S
CS
Polyakov
Konstantin M
KM
Gavryushov
Sergei A
SA
Kritzyn
Anatoliy M
AM
Mikhailov
Sergey N
SN
D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D006860:Hydrogen Bonding; D007700:Kinetics; D013379:Substrate Specificity; D013939:Thymidine Phosphorylase / Q000378:metabolism*
D029968:Escherichia coli Proteins; D013939:Thymidine Phosphorylase