Send to

Choose Destination
See comment in PubMed Commons below
Biochem Biophys Res Commun. 1993 Apr 30;192(2):597-602.

Biotransformation of pravastatin sodium (I). Mechanisms of enzymic transformation and epimerization of an allylic hydroxy group of pravastatin sodium.

Author information

  • 1Analytical and Metabolic Research Laboratories, Sankyo Co., Ltd., Tokyo, Japan.

Erratum in

  • Biochem Biophys Res Commun 1993 Aug 31;195(1):504.


One of the major metabolites, R-416(3'alpha-OH), of pravastatin sodium(PV, 6'beta-OH), and a minor metabolite, R-418 (6'alpha-OH), were produced in rat liver cytosol in the presence of adenosine 3'-phosphate 5'-phosphosulfate as a cofactor. The reactions were inhibited by the inhibitors for sulfotransferases, and 18OH was introduced to the 3'alpha- and 6'alpha-positions of R-416 and R-418, respectively, by incubation with H2 18O. These results strongly suggested that PV was metabolically activated by sulfation at the 6'beta-hydroxy group by sulfotransferases, followed by nucleophilic attack of hydroxy anions at the 3'alpha- or 6'alpha-position, to give R-416 or R-418, respectively.

[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk