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A Ca 2+ ‐dependent protein kinase phosphorylates phosphoenolpyruvate carboxylase in maize
Author(s) -
Ogawa Noriyuki,
Okumura Satoru,
Izui Katsura
Publication year - 1992
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(92)80291-n
Subject(s) - phosphoenolpyruvate carboxylase , protein kinase a , biochemistry , egta , phosphorylation , dephosphorylation , myosin light chain kinase , chemistry , kinase , calmodulin , protein phosphorylation , biology , calcium , enzyme , phosphatase , organic chemistry
In C 4 plants the activity of phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31) is regulated by phosphorylation/dephosphorylation which is mediated by light/dark signals. The study using protein kinase inhibitors showed that the inhibition pattern of maize PEPC‐protein kinase (PEPC‐PK) is similar to that of myosin light chain kinase, a Ca 2+ ‐calmodulin‐dependent PK. The kinase activity was also inhibited by EGTA and the inhibition was relieved by Ca 2+ . These results suggest that PEPC‐PK is Ca 2+ ‐dependent in contrast with previous observations by other research groups.