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

Biochem Biophys Res Commun. 1993 Apr 30;192(2):597-602. doi: 10.1006/bbrc.1993.1457.

Abstract

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.

MeSH terms

  • Animals
  • Biotransformation
  • Cytosol / enzymology
  • Cytosol / metabolism*
  • Liver / enzymology
  • Liver / metabolism*
  • Male
  • Pravastatin / chemistry
  • Pravastatin / metabolism*
  • Rats
  • Rats, Sprague-Dawley

Substances

  • Pravastatin