Benzil, a potent activator of microsomal epoxide hydrolase in vitro

Eur J Biochem. 1980 Dec;112(3):643-8. doi: 10.1111/j.1432-1033.1980.tb06129.x.

Abstract

Benzil was found to be a very potent activator of microsomal epoxide hydrolase activity (measured with styrene oxide as substrate) in vitro. The activating effect was uncompetitive and benzil causes approximately ninefold increases in both the apparent V and the apparent Km of the enzyme(s). The half-maximal effect on activity was obtained as a 0.3 mM concentration of benzil. The activating effect obtained with benzil was found to be very specific, since a variety of structurally related compounds had little or no effect on microsomal epoxide hydrolase activity. In order to obtain indications for the existence of more than one microsomal epoxide hydrolase the effect of benzil on this activity from rats induced with phenobarbital, 3-methylcholanthrene, 2-acetylaminofluorene, trans-stilbene oxide, and benzil was tested. The differences observed were minor.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aldehydes / pharmacology*
  • Animals
  • Chalcone / analogs & derivatives
  • Chalcone / pharmacology
  • Chalcones
  • Enzyme Activation / drug effects
  • Epoxide Hydrolases / metabolism*
  • Hydrogen-Ion Concentration
  • Kinetics
  • Male
  • Metyrapone / pharmacology
  • Microsomes, Liver / enzymology*
  • Phenylglyoxal / analogs & derivatives
  • Phenylglyoxal / pharmacology*
  • Rats
  • Solvents
  • Structure-Activity Relationship

Substances

  • Aldehydes
  • Chalcones
  • Solvents
  • chalcone epoxide
  • Chalcone
  • Epoxide Hydrolases
  • Phenylglyoxal
  • benzil
  • Metyrapone