Inhibition of the proton pumping ATPases of yeast and oat root plasma membranes by dicyclohexylcarbodiimide.
The inhibition of the proton-pumping ATPases of yeast and oat root plasma membranes by dicyclohexylcarbodiimide (DCCD) can be correlated with the covalent incorporation of the inhibitor. Full inhibition of the yeast enzyme required the incorporation of about 1 mol DCCD/mol of the ATPase polypeptide of 100 kDa. A kinetic study of the interaction of DCCD with the yeast and oat ATPases indicates a second-order rate constant of about 500 M-1 min-1 and a stoichiometry of 1 mol DCCD/mol of enzyme, in agreement with the amount of DCCD incorporated by the yeast enzyme. It is proposed that DCCD reacts with a single carboxylic group present in a hydrophobic region of these proton-pumping ATPases and which could participate in proton binding and transport.
D000595:Amino Acid Sequence; D001665:Binding Sites; D002234:Carbodiimides / Q000494:pharmacology*; D002462:Cell Membrane / Q000201:enzymology*; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology*; D002523:Edible Grain / Q000201:enzymology; D007700:Kinetics; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors*; D012441:Saccharomyces cerevisiae / Q000201:enzymology
D002234:Carbodiimides; D004024:Dicyclohexylcarbodiimide; D006180:Proton-Translocating ATPases