A Ca(2+)-dependent protein kinase phosphorylates phosphoenolpyruvate carboxylase in maize. |
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| Authors: | N Ogawa S Okumura K Izui |
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| Institution: | Department of Chemistry, Faculty of Science, Kyoto University, Japan. |
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| Abstract: | In C4 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 Ca2+. These results suggest that PEPC-PK is Ca(2+)-dependent in contrast with previous observations by other research groups. |
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