title: Substrate specificity of Escherichia coli thymidine phosphorylase.
abstract: Substrate specificity of Escherichia coli thymidine phosphorylase to thymidine derivatives modified at 5' -, 3' -, and 2' ,3' - positions of the sugar moiety was studied. Equilibrium and kinetic constants (K(m), K(I), k(cat)) of the phosphorolysis reaction have been determined for 20 thymidine analogs. The results are compared with X-ray and molecular dynamics data. The most important hydrogen bonds in the enzyme-substrate complex are revealed.
authors.affiliation: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991, Russia. natasha@eimb.ru
authors.forename: N G
authors.initials: NG
authors.lastname: Panova
authors.forename: C S
authors.initials: CS
authors.lastname: Alexeev
authors.forename: A S
authors.initials: AS
authors.lastname: Kuzmichov
authors.forename: E V
authors.initials: EV
authors.lastname: Shcheveleva
authors.forename: S A
authors.initials: SA
authors.lastname: Gavryushov
authors.forename: K M
authors.initials: KM
authors.lastname: Polyakov
authors.forename: A M
authors.initials: AM
authors.lastname: Kritzyn
authors.forename: S N
authors.initials: SN
authors.lastname: Mikhailov
authors.forename: R S
authors.initials: RS
authors.lastname: Esipov
authors.forename: A I
authors.initials: AI
authors.lastname: Miroshnikov
mesh_terms: D019943:Amino Acid Substitution; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D015394:Molecular Structure; D009705:Nucleosides / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013936:Thymidine / Q000378:metabolism*; D013939:Thymidine Phosphorylase / Q000737:chemistry* / Q000378:metabolism
chemical_list: D009705:Nucleosides; D013939:Thymidine Phosphorylase; D013936:Thymidine