- Tytuł:
- Isotope effects on enzymatic and nonenzymatic reactions of phosphorothioates
- Autorzy:
-
Catrina, I.
Czyryca, P.
Hengge, A. - Powiązania:
- https://bibliotekanauki.pl/articles/146931.pdf
- Data publikacji:
- 2002
- Wydawca:
- Instytut Chemii i Techniki Jądrowej
- Tematy:
-
alkaline phosphatase
isotope effect
phosphoryl transfer
phosphorothioate
thio effect - Opis:
- Kinetic isotope effects have been measured for the aqueous hydrolysis reactions of p-nitrophenyl phosphorothioate (pNPPT) and the diester ethyl p-nitrophenyl phosphorothioate, and for the alkaline phosphatase-catalyzed reaction with pNPPT. The results show that the transition states of the uncatalyzed reactions of the phosphorothioate mono- and diesters are very similar to those of the corresponding phosphate ester reactions. The secondary 18O nonbridge isotope effects in reactions of phosphate esters become more normal as the mechanism changes from dissociative, metaphosphate-like to associative, phosphorane-like. The opposite trend occurs in phosphorothioate esters, due to differences in the relative contributions of bond-order changes and bending modes to this isotope effect. The KIEs for the alkaline phosphatase-catalyzed reaction of pNPPT are most consistent with a tight, triester-like transition state, probably a result of perturbations resulting from the larger size of sulfur that lead to a nucleophile attack angle that is unfavorable for an in-line process with a loose transition state.
- Źródło:
-
Nukleonika; 2002, 47,suppl.1; 17-23
0029-5922
1508-5791 - Pojawia się w:
- Nukleonika
- Dostawca treści:
- Biblioteka Nauki
Artykuł