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פותח על ידי קלירמאש פתרונות בע"מ -
Regulation of a plant SNF1-related protein kinase by glucose-6-phosphate
Year:
2000
Authors :
פלאוט, צבי
;
.
Volume :
123
Co-Authors:
Toroser, D., U. States Department of Agriculture, Agricultural Research Service, North Carolina State University, Raleigh, NC 27695-7631, United States
Plaut, Z., U. States Department of Agriculture, Agricultural Research Service, North Carolina State University, Raleigh, NC 27695-7631, United States, Dept. of Environmental Physiology, Agricultural Research Organization, P.O. Box 6, Bet-Dagan, 50250, Israel
Huber, S.C., U. States Department of Agriculture, Agricultural Research Service, North Carolina State University, Raleigh, NC 27695-7631, United States
Facilitators :
From page:
403
To page:
411
(
Total pages:
9
)
Abstract:
One of the major protein kinases (PK(III)) that phosphorylates serine-158 of spinach sucrose-phosphate synthase (SPS), which is responsible for light/dark modulation of activity, is known to be a member of the SNF1-related family of protein kinases. In the present study, we have developed a fluorescence-based continuous assay for measurement of PK(III) activity. Using the continuous assay, along with the fixed-time-point 32P-incorporation assay, we demonstrate that PK(III) activity is inhibited by glucose-6-phosphate (Glc-6-P). Relative inhibition by Glc-6-P was increased by decreasing pH from 8.5 to 5.5 and by reducing the concentration of Mg2+ in the assay from 10 to 2 mM. Under likely physiological conditions (pH 7.0 and 2 mM Mg2+), 10 mm Glc-6-P inhibited kinase activity approximately 70%. Inhibition by Glc-6-P could not be ascribed to contaminants in the commercial preparations. Other metabolites inhibited PK(III) in the following order: Glc-6-P > mannose-6-P, fructose-1,6P2 > ribose-5-P, 3-PGA, fructose-6-P. Inorganic phosphate, Glc, and AMP were not inhibitory, and free Glc did not reverse the inhibition by Glc-6-P. Because SNF1-related protein kinases are thought to function broadly in the regulation of enzyme activity and gene expression, Glc-6-P inhibition of PK(III) activity potentially provides a mechanism for metabolic regulation of the reactions catalyzed by these important protein kinases.
Note:
Related Files :
biochemical pathway
enzyme activity
enzyme inhibition
pH
Plants
protein kinase
עוד תגיות
תוכן קשור
More details
DOI :
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
23743
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:02
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Scientific Publication
Regulation of a plant SNF1-related protein kinase by glucose-6-phosphate
123
Toroser, D., U. States Department of Agriculture, Agricultural Research Service, North Carolina State University, Raleigh, NC 27695-7631, United States
Plaut, Z., U. States Department of Agriculture, Agricultural Research Service, North Carolina State University, Raleigh, NC 27695-7631, United States, Dept. of Environmental Physiology, Agricultural Research Organization, P.O. Box 6, Bet-Dagan, 50250, Israel
Huber, S.C., U. States Department of Agriculture, Agricultural Research Service, North Carolina State University, Raleigh, NC 27695-7631, United States
Regulation of a plant SNF1-related protein kinase by glucose-6-phosphate
One of the major protein kinases (PK(III)) that phosphorylates serine-158 of spinach sucrose-phosphate synthase (SPS), which is responsible for light/dark modulation of activity, is known to be a member of the SNF1-related family of protein kinases. In the present study, we have developed a fluorescence-based continuous assay for measurement of PK(III) activity. Using the continuous assay, along with the fixed-time-point 32P-incorporation assay, we demonstrate that PK(III) activity is inhibited by glucose-6-phosphate (Glc-6-P). Relative inhibition by Glc-6-P was increased by decreasing pH from 8.5 to 5.5 and by reducing the concentration of Mg2+ in the assay from 10 to 2 mM. Under likely physiological conditions (pH 7.0 and 2 mM Mg2+), 10 mm Glc-6-P inhibited kinase activity approximately 70%. Inhibition by Glc-6-P could not be ascribed to contaminants in the commercial preparations. Other metabolites inhibited PK(III) in the following order: Glc-6-P > mannose-6-P, fructose-1,6P2 > ribose-5-P, 3-PGA, fructose-6-P. Inorganic phosphate, Glc, and AMP were not inhibitory, and free Glc did not reverse the inhibition by Glc-6-P. Because SNF1-related protein kinases are thought to function broadly in the regulation of enzyme activity and gene expression, Glc-6-P inhibition of PK(III) activity potentially provides a mechanism for metabolic regulation of the reactions catalyzed by these important protein kinases.
Scientific Publication
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