Characterization of the substrate specificity of sucrose-phosphate synthase protein kinase

Robert W. McMichael, Jan Kochansky, Robert R. Klein, Steven C. Huber

Research output: Contribution to journalArticle

Abstract

Sucrose-phosphate synthase (SPS; EC 2.4.1.14) is regulated by reversible protein phosphorylation. When the enzyme is phosphorylated it is inactivated and can be reactivated by removal of phosphate. The major regulatory phosphorylation site is known to be Ser158 in the spinach-leaf enzyme, and two protein kinase activities have been resolved chromatographically which phosphorylate SPS at this site in vitro. In this report, we use a set of synthetic peptide substrate analogs based on the phosphorylation site sequence, and a set of Escherichia coli-expressed 26-kDa fragments of spinach SPS which contain the site, to identify the recognition elements that target the two protein kinases to Ser158. The major recognition element consists of basic residues at P-3 and P-6 relative to the phosphorylated serine. Comparison of the spinach enzyme amino-acid sequence with two other plant species show conservation of these amino acids and implies that these signals are also conserved. We also present evidence that glucose-6-phosphate is not only an allosteric activator of SPS but also an inhibitor of SPS-protein kinase per se, thereby allowing it to act at both levels of SPS regulation.

Original languageEnglish (US)
Pages (from-to)71-75
Number of pages5
JournalArchives of Biochemistry and Biophysics
Volume321
Issue number1
DOIs
StatePublished - Jan 1 1995

Keywords

  • Protein kinase
  • Recognition elements
  • Regulatory phosphorylation
  • Synthetic peptides

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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