Key result
Conservative amino acid changes in the catalytic center of Ca2+-ATPase preserved function, whereas nonconservative changes disrupted it, and specific mutations abolished phosphoenzyme formation.
Population
Rabbit fast twitch muscle Ca2+-ATPase
Design
Preclinical
Authors
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Does not support clinical SERCA targeting; leaves open relevance of these residues to human cardiac disease.
Conservative amino acid changes in the catalytic center of sarcoplasmic reticulum Ca2+-ATPase preserve function, while nonconservative changes and specific mutations in the nucleotide-binding domain disrupt it.
Maruyama et al. (1989) studied this question. Amino acid mutations in the catalytic center and nucleotide-binding domain of Ca2+-ATPase vs. Wild-type Ca2+-ATPase was evaluated on Ca2+ transport activity and autophosphorylation with ATP or Pi. Conservative amino acid changes in the catalytic center of Ca2+-ATPase preserved function, whereas nonconservative changes disrupted it, and specific mutations abolished phosphoenzyme formation.
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