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A Ca(2+)-dependent protein kinase phosphorylates phosphoenolpyruvate carboxylase in maize.

作者信息

Ogawa N, Okumura S, Izui K

机构信息

Department of Chemistry, Faculty of Science, Kyoto University, Japan.

出版信息

FEBS Lett. 1992 May 4;302(1):86-8. doi: 10.1016/0014-5793(92)80291-n.

DOI:10.1016/0014-5793(92)80291-n
PMID:1587360
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.

摘要

相似文献

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