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Phosphorylation of Serine-15 of Maize Leaf Sucrose Synthase (Occurrence in Vivo and Possible Regulatory Significance)
Experiments were conducted to determine whether sucrose synthase (SuSy) was phosphorylated in the elongation zone of maize (Zea mays L.) leaves. The approximately 90-kD subunit of SuSy was… Expand
Membrane association of sucrose synthase: changes during the graviresponse and possible control by protein phosphorylation
Sucrose synthase (SuSy) plays an important role in sucrose degradation and occurs both as a soluble and as a membrane‐associated enzyme in higher plants. We show that membrane association can vary in… Expand
Reversible light/dark modulation of spinach leaf nitrate reductase activity involves protein phosphorylation.
- J. Huber, S. Huber, W. H. Campbell, M. Redinbaugh
- Chemistry, Medicine
- Archives of biochemistry and biophysics
- 1 July 1992
Spinach (Spinacia oleracea L.) leaf nitrate reductase (NADH:NR;NADH:nitrate oxidoreductase, EC 184.108.40.206) activity was found to rapidly change during light/dark transitions. The most rapid and dramatic… Expand
Sucrose phosphate synthase and sucrose accumulation at low temperature.
The influence of growth temperature on the free sugar and sucrose phosphate synthase content and activity of spinach (Spinacia oleracea) leaf tissue was studied. When plants were grown at 25 degrees… Expand
The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14‐3‐3 protein
The inhibitor protein (IP) that inactivates spinach leaf NADH:nitrate reductase (NR) has been identified for the first time as a member of the eukaryotic 14‐3‐3 protein family based on three lines of… Expand
Role of sucrose-phosphate synthase in sucrose metabolism in leaves.
Sucrose is formed in the cytoplasm of leaf cells from triose phosphates exported from the chloroplast. Flux control is shared among key enzymes of the pathway, one of which is sucrose-phosphate… Expand
Biological significance of divalent metal ion binding to 14-3-3 proteins in relationship to nitrate reductase inactivation.
In this report we address two questions regarding the regulation of phosphorylated nitrate reductase (pNR; EC 220.127.116.11) by 14-3-3 proteins. The first concerns the requirement for millimolar… Expand
Protein phosphorylation as a mechanism for regulation of spinach leaf sucrose-phosphate synthase activity.
Studies were conducted to determine whether protein phosphorylation may be a mechanism for regulation of spinach (Spinacia oleracea L.) leaf sucrose-phosphate synthase (SPS), shown previously to be… Expand
14‐3‐3 proteins associate with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform‐specific manner and reduce dephosphorylation of Ser‐543 by endogenous protein…
- M. Bachmann, J. Huber, G. S. Athwal, K. Wu, R. Ferl, S. Huber
- Biology, Medicine
- FEBS letters
- 25 November 1996
Three lines of evidence indicate that the 14‐3‐3 proteins that inactivate the phosphorylated form of spinach leaf NADH:nitrate reductase (NR) bind to the enzyme at the regulatory phosphorylation site… Expand
Phosphorylated nitrate reductase and 14-3-3 proteins. Site of interaction, effects of ions, and evidence for an amp-binding site on 14-3-3 proteins.
The inactivation of phosphorylated nitrate reductase (NR) by the binding of 14-3-3 proteins is one of a very few unambiguous biological functions for 14-3-3 proteins. We report here that serine and… Expand