Structural requirements for phosphorylation of C4-leaf phosphoenolpyruvate carboxylase by its highly regulated protein-serine kinase. A comparative study with synthetic-peptide substrates and mutant target proteins

A family of synthetic peptides modelled after the highly conserved, N-terminal phosphorylation domain of C4 phosphoenolpyruvate carboxylase (PEPC) and a complementary set of recombinant mutant target proteins were exploited to investigate the local structural requirements for phosphorylation of this...

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Veröffentlicht in:Australian journal of plant physiology 1997, Vol.24 (4), p.443-449
Hauptverfasser: Li, B, Pacquit, V, Jiao, J, Duff, S.M.G, Maralihalli, G.B, Sarath, G, Condon, S.A, Vidal, J, Chollet, R
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Sprache:eng
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