The nature of microsomal monooxygenase inhibition by cimetidine

Biochem Pharmacol. 1986 Jul 1;35(13):2157-61. doi: 10.1016/0006-2952(86)90586-1.

Abstract

A kinetic investigation of the inhibitory effect of cimetidine on the O-dealkylation of 7-ethoxyresorufin by rat liver microsomes has yielded linear Lineweaver-Burk plots which intersect in the second quadrant. Though technically compatible with non-competitive inhibition, the results are shown to be readily explained by the more realistic molecular concept of competitive inhibition by invoking the involvement of cytochrome P-450 isoenzymes with widely different KI values. Microsomal monooxygenase heterogeneity is also shown to provide a plausible explanation of other published results signifying the departure of chloramphenicol and phenacetin from the concept of competitive inhibition despite competition with substrate for the active-site haem group of cytochrome P-450.

MeSH terms

  • Animals
  • Binding Sites
  • Binding, Competitive
  • Cimetidine / pharmacology*
  • Cytochrome P-450 Enzyme System
  • Heme / metabolism
  • Isoenzymes / metabolism
  • Kinetics
  • Male
  • Mathematics
  • Microsomes, Liver / enzymology*
  • Oxazines / metabolism
  • Oxygenases / antagonists & inhibitors*
  • Rats
  • Rats, Inbred Strains

Substances

  • Isoenzymes
  • Oxazines
  • Heme
  • ethoxyresorufin
  • Cimetidine
  • Cytochrome P-450 Enzyme System
  • Oxygenases