-transparent.png){kind=logo}
[18O]Adenosine 5'-O-phosphorothioate-O-p-nitrophenyl ester was prepared by saponification of the bis (-O,O-p-nitrophenyl ester) with K18OH. Only the diastereoisomer with the Rp configuration si a substrate for snake venom phosphodiesterase. The asymmetrically labeled [18O]adenosine 5'-O-phosphorothioate formed in this reaction was converted enzymatically to [18O]adenosine 5'-(1-thiodiphosphate) with the Sp configuration. The position of the 18O label, either bridging [1,2-mu-18O] or nonbridging [1-18O] was then determined. The results show that the reaction catalyzed by snake venom phosphodiesterase takes place with retention of configuration at phosphorus. This indicates that the hydrolysis proceeds via a covalent nucleotide enzyme intermediate.
P M Burgers, and
F Eckstein, and
D H Hunneman
January 1966,
Comptes rendus de l'Academie Bulgare des sciences : sciences mathematiques et naturelles,
P M Burgers, and
F Eckstein, and
D H Hunneman
November 1981,
The Biochemical journal,
P M Burgers, and
F Eckstein, and
D H Hunneman
January 1969,
FEBS letters,
P M Burgers, and
F Eckstein, and
D H Hunneman
January 1970,
Biokhimiia (Moscow, Russia),
P M Burgers, and
F Eckstein, and
D H Hunneman
November 1957,
Nature,
P M Burgers, and
F Eckstein, and
D H Hunneman
January 1975,
Molekuliarnaia biologiia,
P M Burgers, and
F Eckstein, and
D H Hunneman
March 1987,
Carcinogenesis,
P M Burgers, and
F Eckstein, and
D H Hunneman
February 1964,
Biochimica et biophysica acta,
P M Burgers, and
F Eckstein, and
D H Hunneman
May 2020,
Biomolecules,
P M Burgers, and
F Eckstein, and
D H Hunneman
January 1974,
Methods in enzymology,
