Inactivation of enolase with tetranitromethane

Acta Biochim Pol. 1980;27(3-4):365-70.


1. All 20 tyrosyl residues of enolase from human and pig muscle were nitrated with tetranitromethane in mild conditions; 2-phosphoglycerate and magnesium ions decreased the rate of reaction. 2. Inactivation took place in two steps: (a), nitration of 6 - 10 tyrosine residues of enolase decreased the activity by about 20%, without affecting Km value, molecular weight of pH dependence; (b) on nitration of 12 tyrosyl residues, inactivation was nearly complete, with concomitant profound changes in the enzyme properties. 2-Phosphoglycerate and magnesium ions present together protected significantly against inactivation. 3. The results suggest that the activity of enolase is dependent on intactness of tyrosyl residues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Humans
  • Kinetics
  • Methane / analogs & derivatives*
  • Muscles / enzymology*
  • Phosphopyruvate Hydratase / antagonists & inhibitors*
  • Swine
  • Tetranitromethane / pharmacology*
  • Tyrosine


  • Tyrosine
  • Phosphopyruvate Hydratase
  • Tetranitromethane
  • Methane