title: [Phosphorus-containing inhibitors of penicillin acylase. 3. Inhibition of Escherichia coli penicillin acylase by phosphonate analogs of substrates].
abstract: Phosphonic analogues of penicillin acylase substrates are found to be selective reversible competitive inhibitors of the enzyme from E. coli (EC 3.5.1.11). The mode of binding of the inhibitors to the enzyme and the influence of the stereoelectronic parameters of the phosphonic inhibitors on their affinity to the enzyme are discussed.
authors.forename: V A
authors.initials: VA
authors.lastname: Solodenko
authors.forename: V N
authors.initials: VN
authors.lastname: Tserniuk
authors.forename: V P
authors.initials: VP
authors.lastname: Kukhar'
mesh_terms: D001667:Binding, Competitive / Q000502:physiology; D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D063065:Organophosphonates / Q000494:pharmacology*; D010399:Penicillin Amidase / Q000037:antagonists & inhibitors*; D010758:Phosphorus / Q000032:analysis*
chemical_list: D063065:Organophosphonates; D010758:Phosphorus; D010399:Penicillin Amidase
vernacular_title: Fosforsoderzhashchie ingibitory penitsillinatsilazy. 3. Ingibirovanie penitsillinatsilazy Escherichia coli fosfonatnymi analogami substratov.