Abstract:Die Amidothiophosphonsäuren (III) werden durch basische Hydrolyse ihrer Chloride (I) über ihre K‐Salze (II) hergestellt und elementaranalytisch, IR‐ sowie NMR‐spektroskopisch, aber auch durch chemische Methoden charakterisiert.
“…Studies indicate that the thiono−thiolo equilibrium lies far on the side of the thiono form in phosphonothioic acids (in which a carbon−phosphorus bond is present). In compounds where only phosphorus−oxygen bonds are present (Figure b) more of the thiolo form is typically present, depending upon the solvent. − 2 The thiono and thiolo tautomers of phosphonothioic acids (a) and phosphorothioic acids (b). The thiono−thiolo equilibrium lies far to the left phosphonothioic acids (a).…”
Section: Introductionmentioning
confidence: 99%
“…In compounds where only phosphorusoxygen bonds are present (Figure 2b) more of the thiolo form is typically present, depending upon the solvent. [17][18][19] The preparation of some of the compounds shown required the development of some new synthetic meth-odology. The majority of the thiophosphonic acids (1S-6S) were synthesized as previously described.…”
Phosphorothioates, analogues of phosphate esters in which a sulfur replaces an oxygen atom in the phosphoryl group, are competent surrogate substrates for a number of phosphatases. In some cases the thio analogues show similar binding (as estimated by K(m)) while other phosphatases show quite different K(m) values for phosphate compared to phosphorothioate esters. On this basis it was hypothesized that there might be different inhibitory tendencies by the nonhydrolyzable analogues, phosphonothioic acids compared with phosphonic acids. A series of phosphonothioic acids and corresponding phosphonic acids were synthesized and their inhibitory properties were compared toward human placental and E. coli alkaline phosphatases, the protein-tyrosine phosphatase from Yersinia, and the serine/threonine protein phosphatases PP2C and lambda. Sulfur substitution for oxygen gives the phosphonothioic acids pK(a) values that are close to those of phosphate esters, in contrast to the higher pK(a) values typical of phosphonic acids. Despite different steric requirements and differences in charge distribution in the anions of phosphonothioic acids compared with phosphonic acids, it was found that, with some exceptions, differences in inhibitory properties were modest.
“…Studies indicate that the thiono−thiolo equilibrium lies far on the side of the thiono form in phosphonothioic acids (in which a carbon−phosphorus bond is present). In compounds where only phosphorus−oxygen bonds are present (Figure b) more of the thiolo form is typically present, depending upon the solvent. − 2 The thiono and thiolo tautomers of phosphonothioic acids (a) and phosphorothioic acids (b). The thiono−thiolo equilibrium lies far to the left phosphonothioic acids (a).…”
Section: Introductionmentioning
confidence: 99%
“…In compounds where only phosphorusoxygen bonds are present (Figure 2b) more of the thiolo form is typically present, depending upon the solvent. [17][18][19] The preparation of some of the compounds shown required the development of some new synthetic meth-odology. The majority of the thiophosphonic acids (1S-6S) were synthesized as previously described.…”
Phosphorothioates, analogues of phosphate esters in which a sulfur replaces an oxygen atom in the phosphoryl group, are competent surrogate substrates for a number of phosphatases. In some cases the thio analogues show similar binding (as estimated by K(m)) while other phosphatases show quite different K(m) values for phosphate compared to phosphorothioate esters. On this basis it was hypothesized that there might be different inhibitory tendencies by the nonhydrolyzable analogues, phosphonothioic acids compared with phosphonic acids. A series of phosphonothioic acids and corresponding phosphonic acids were synthesized and their inhibitory properties were compared toward human placental and E. coli alkaline phosphatases, the protein-tyrosine phosphatase from Yersinia, and the serine/threonine protein phosphatases PP2C and lambda. Sulfur substitution for oxygen gives the phosphonothioic acids pK(a) values that are close to those of phosphate esters, in contrast to the higher pK(a) values typical of phosphonic acids. Despite different steric requirements and differences in charge distribution in the anions of phosphonothioic acids compared with phosphonic acids, it was found that, with some exceptions, differences in inhibitory properties were modest.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
