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Volume 272, Number 48, Issue of November 28, 1997 pp. 30244-30253
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Mutation Lys⁷⁵⁸  Ile of the Sarcoplasmic Reticulum Ca²⁺-ATPase Enhances Dephosphorylation of E₂P and Inhibits the E₂ to E₁Ca₂ Transition

(Received for publication, June 26, 1997, and in revised form, September 8, 1997)

From the Department of Physiology, University of Aarhus, DK-8000 Aarhus C, Denmark

The highly conserved lysine residue Lys⁷⁵⁸ in the fifth stalk segment of the sarcoplasmic reticulum Ca²⁺-ATPase was substituted with either isoleucine or arginine by site-directed mutagenesis. The substitution with arginine was without significant effects on Ca²⁺-ATPase function, whereas multiple changes of functional characteristics were observed with the Lys⁷⁵⁸  Ile mutant. These included insensitivity of ATPase activity to the calcium ionophore A23187, an alkaline shift of the pH dependence of ATPase activity, reduced maximum molecular turnover rate and steady-state phosphorylation level, reduced apparent affinities for Ca²⁺ and inorganic phosphate, as well as increased sensitivity to inhibition by vanadate. Analysis of the partial reaction steps of the enzyme cycle traced these changes to two steps. The rate of dephosphorylation of the ADP-insensitive phosphoenzyme intermediate (E₂P) was increased, irrespective of variations of pH, K⁺, Ca²⁺, and dimethyl sulfoxide concentration. In addition, the rate of conversion of the dephosphoenzyme with low Ca²⁺ affinity (E₂) to the Ca²⁺-bound form activated for phosphorylation (E₁Ca₂) was reduced in the mutant, and the ATP-induced rate enhancement of this step required higher ATP concentrations in the mutant compared with the wild type.

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