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Specific dicyclohexylcarbodiimide inhibition of the phospho enzyme plus water to enzyme plus inorganic phosphate reaction and atp inorganic phosphate exchange in sarcoplasmic reticulum atpase


, : Specific dicyclohexylcarbodiimide inhibition of the phospho enzyme plus water to enzyme plus inorganic phosphate reaction and atp inorganic phosphate exchange in sarcoplasmic reticulum atpase. Biochemistry 24(4): 1025-1029

Treatment of sarcoplasmic reticulum [from rabbits] ATPase with N,N'-dicyclohexylcarbodiimide is known to produce total inhibition of Ca binding and enzyme activity. Treatment with lower reagent:protein ratios produces selective inhibition of hydrolytic Pi [inorganic phosphate] cleavage, enzyme phosphorylation with Pi, and ATP .dblarw. Pi exchange, while Ca binding and enzyme phosphorylation with ATP remain largely unaffected. This specific inhibition is attributed to derivatization of residues which are normally involved in acid-base-assisted catalysis of the hydrolytic reaction and its reversal, but are not involved in Ca binding or in the mechanism of phosphoryl transfer from ATP to the enzyme. This specific inhibition is prevented by the presence of micromolar Ca during the incubation with the inhibitor, evidently through an allosteric effect of Ca binding on the catalytic site. Also the initial adducts formed between ATPase residues and N,N'-dicyclo[14C]carbodiimide undergo further degradation with release of radioactive product into the medium, while the protein residues remain inactivated probably by linkage with neighboring residues. Therefore, the stoichiometry of radioactive labeling underestimates the actual number of inactivated residues.

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