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Regulation of spinach leaf sucrose-phosphate synthase by multisite phosphorylation


, : Regulation of spinach leaf sucrose-phosphate synthase by multisite phosphorylation. Current Topics in Plant Biochemistry and Physiology 9: 329-343

Following an introduction covering light modulation of chloroplast enzymes and the 2 soluble cytosolic enzymes, PEPCase and sucrose-phosphate synthase (SPS), the latter being the only enzyme in the sucrose formation pathway recognized to be light modulated, mechanisms of light modulation of SPS are outlined.

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Related references

Huber J.L.; Huber S.C., 1990: Multisite phosphorylation of spinach leaf sucrose phosphate synthase. Plant Physiology (Rockville) 93(1 SUPPL): 18

Huber, J.L.; Huber, S.C.; Nielsen, T.H., 1989: 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 light-dark regulated by some type of covalent mod...

Toroser, D.; Huber, S.C., 1999: Phosphorylation dependent regulation and interaction of spinach leaf UDP-Glucose pyrophosphorylase with 14-3-3 proteins and sucrose-phosphate synthase. Plant Biology (Rockville) : 139

Doehlert D.C.; Huber S.C., 1983: Regulation of spinach spinacia oleracea leaf sucrose phosphate synthase by glucose 6 phosphate inorganic phosphate and ph. Sucrose phosphate synthase was partially purified from spinach leaves and the effects and interactions among G-6-P, Pi and pH were investigated. G-6-P activated sucrose phosphate synthase and the concentration required for 50% of maximal activatio...

Huber, J.L.; Huber, S.C., 1992: Site-specific serine phosphorylation of spinach leaf sucrose-phosphate synthase. We recently reported [Huber, Huber & Nielsen (1989) Arch. Biochem. Biophys. 270, 681-690] that spinach (Spinacia oleracea L.) sucrose-phosphate synthase (SPS; EC 2.4.1.14) was phosphorylated in vivo when leaves were fed [32P]Pi. In vitro the e...

Doehlert, D.C.; Huber, S.C., 1983: Regulation of Spinach Leaf Sucrose Phosphate Synthase by Glucose-6-Phosphate, Inorganic Phosphate, and pH. Sucrose phosphate synthase was partially purified from spinach leaves and the effects and interactions among glucose-6-P, inorganic phosphate (Pi), and pH were investigated. Glucose-6-P activated sucrose phosphate synthase and the concentration re...

Doehlert, D.C.; Huber, S.C., 1983: Regulation of spinach leaf sucrose phosphate synthase by glucose-6-phosphate, inorganic phosphate, and pH. Sucrose phosphate synthase was partially purified from spinach leaves and the effects and interactions among glucose-6-P, inorganic phosphate (Pi), and pH were investigated. Glucose-6-P activated sucrose phosphate synthase and the concentration re...

Huber, S.; Huber, J., 1991: In vitro phosphorylation and inactivation of spinach leaf sucrose-phosphate synthase by an endogenous protein kinase. (1) Partially purified preparations of spinach (Spinacia oleracea L.) leaf sucrose-phosphate synthase (SPS) contain an endogenous protein kinase that phosphorylates and inactivates the enzyme with [gamma-32P]ATP. (2) The kinetic effect of phosphor...

Doehlert D.C.; Huber S.C., 1985: The role of sulfhydryl groups in the regulation of spinach leaf sucrose phosphate synthase. The activation of spinach leaf sucrose phosphate synthase by glucose 6-phosphate (Glc6P) was labile in the absence of dithiothreitol, whereas enzyme activity in the absence of activator remained stable. The loss of regulation by Glc6P proceeded mo...

Huber S.C.; Huber J.L., 1991: Regulation of maize leaf sucrose phosphate synthase by protein phosphorylation. Studies were conducted to determine the potential for regulation of maize leaf sucrose-phosphate synthase (SPS) by protein phosphorylation. Highly activated enzyme, in desalted crude leaf extracts prepared from illuminated leaves, was inactivated...