Substrate specificity of Escherichia coli thymidine phosphorylase.
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.
Panova
N G
NG
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991, Russia. natasha@eimb.ru
Alexeev
C S
CS
Kuzmichov
A S
AS
Shcheveleva
E V
EV
Gavryushov
S A
SA
Polyakov
K M
KM
Kritzyn
A M
AM
Mikhailov
S N
SN
Esipov
R S
RS
Miroshnikov
A I
AI
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
D009705:Nucleosides; D013939:Thymidine Phosphorylase; D013936:Thymidine