Interaction of F1-ATPase and its inhibitor peptide. Effect of dinitrophenol, nucleotides and anions

Int J Biochem. 1988;20(9):983-7. doi: 10.1016/0020-711x(88)90185-1.

Abstract

1. ATPase natural inhibitor interacted in a mixed non-competitive manner with compounds affecting hydrolytic activity. 2. Ka's for DNP, HCO3- and free ATP, and Ki's for SCN- and ADP became smaller as inhibitor peptide concentration increased, reflecting an increase in affinity of F1-ATPase for these compounds induced by the peptide. 3. Activators increased the peptide inhibitory effect, whereas inhibitors decreased it. 4. A two-step model for the peptide-enzyme interaction is suggested in which ATP hydrolysis is a key factor.

MeSH terms

  • 2,4-Dinitrophenol
  • ATPase Inhibitory Protein
  • Adenosine Diphosphate / pharmacology
  • Animals
  • Anions / pharmacology*
  • Bicarbonates / pharmacology
  • Cattle
  • Dinitrophenols / pharmacology*
  • Mitochondria, Liver / drug effects
  • Mitochondria, Liver / enzymology
  • Nucleotides / pharmacology*
  • Proteins / metabolism*
  • Proton-Translocating ATPases / metabolism*
  • Rats
  • Sodium Cyanide / pharmacology

Substances

  • Anions
  • Bicarbonates
  • Dinitrophenols
  • Nucleotides
  • Proteins
  • Adenosine Diphosphate
  • Proton-Translocating ATPases
  • Sodium Cyanide
  • 2,4-Dinitrophenol