title: Towards new thymidine phosphorylase/PD-ECGF inhibitors based on the transition state of the enzyme reaction.
abstract: Computational studies have been conducted to built a closed form of TPase and to characterize the transition state of the phosphorylisis reaction catalyzed by TPase. The results obtained point to a crucial role of His-85 and the O2 of thymine in the catalysis. This modelled transition state forms the basis for the design of new TPase inhibitors.
authors.affiliation: Instituto de Química Médica (C.S.I.C.), Madrid, Spain. empriego@iqm.csic.es
authors.forename: E M
authors.initials: EM
authors.lastname: Priego
authors.forename: J
authors.initials: J
authors.lastname: Mendieta
authors.forename: F
authors.initials: F
authors.lastname: Gago
authors.forename: J
authors.initials: J
authors.lastname: Balzarini
authors.forename: E
authors.initials: E
authors.lastname: De Clercq
authors.forename: M J
authors.initials: MJ
authors.lastname: Camarasa
authors.forename: M J
authors.initials: MJ
authors.lastname: Pérez-Pérez
mesh_terms: D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D006639:Histidine; D007700:Kinetics; D011487:Protein Conformation; D013939:Thymidine Phosphorylase / Q000037:antagonists & inhibitors* / Q000737:chemistry*; D013941:Thymine
chemical_list: D004791:Enzyme Inhibitors; D006639:Histidine; D013939:Thymidine Phosphorylase; D013941:Thymine