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Probing the SERCA1a sarcoplasmic reticulum Ca2+-ATPase phosphorylation-site mutant D351E with inorganic phosphate BJMBR
Carreira,A.C.O.; Bastos,C.M.V.; Verjovski-Almeida,S..
The expression of sarcoplasmic reticulum SERCA1a Ca2+-ATPase wild-type and D351E mutants was optimized in yeast under the control of a galactose promoter. Fully active wild-type enzyme was recovered in yeast microsomal membrane fractions in sufficient amounts to permit a rapid and practical assay of ATP hydrolysis and phosphoenzyme formation from ATP or Pi. Mutant and wild-type Ca2+-ATPase were assayed for phosphorylation by Pi under conditions that are known to facilitate this reaction in the wild-type enzyme, including pH 6.0 or 7.0 at 25ºC in the presence of dimethylsulfoxide. Although glutamyl (E) and aspartyl (D) residue side chains differ by only one methylene group, no phosphoenzyme could be detected in the D351E mutant, even upon the addition of...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Phosphorylation site mutant; Catalytic site; Yeast expression system; Saccharomyces cerevisiae; P-type ATPase.
Ano: 2007 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2007001000004
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