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Provoked changes in cellular calcium controlled protein phosphorylation and activity of quinate:NAD + oxidoreductase in carrot cells
Author(s) -
Graziana Annick,
Ranjeva Raoul,
Boudet Alain M.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80522-5
Subject(s) - egta , nad+ kinase , oxidoreductase , biochemistry , calcium , calmodulin , chemistry , enzyme , phosphorylation , biology , organic chemistry
Quinate:NAD + oxidoreductase activity decreased when carrot cell‐suspension cultures were supplemented with the Ca 2+ ‐ionophore, A‐23187 and EGTA. The protein phosphorylation pattern changed as judged by autoradiography. The loss in enzyme activity was correlated with the Ca 2+ efflux. Addition of Ca 2+ to protein extracts in combination with calmodulin or not had no effect. Initial quinate:NAD + oxidoreductase activity was partially recovered only after preincubation with ATP‐Mg 2+ and Ca 2+ . The reactivation was abolished by EGTA or fluphenazine. It is concluded that cellular Ca 2+ controls the enzyme activity by affecting its degree of phosphorylation in vivo.