Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.4.1.14 (SPS)
 813 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Rate of net CO2 exchange and activities of the key enzymes of fru-2,6-P2, sucrose and starch synthesis and levels of certain intermediates of Calvin cycle were determined in Brassica pods at different stages of their development. The rate of net CO2 exchange, activities of FBPase, UDPG-pyrophosphorylase and SPS, and the contents of 3-PGA, DHAP, RuBP and UDPG increased up to day 21 after anthesis followed by a continuous decrease thereafter. However the content of fru-6-P started decreasing only after 28 days of anthesis. Changes in the levels of fru-2,6-P2 were closely associated with the changes in F6P 2-kinase activity rather than with F2,6-P2ase activity. Similarly, activities of ADPG-pyrophosphorylase and ADPG-starch synthetase closely followed the pattern of starch accumulation in pod tissues. These observations suggest that during the early phase of pod development (up to 21 days after anthesis), which is also the active phase for pod photosynthesis, carbon is mainly utilised for sucrose synthesis and that during the later phase of pod development (from day 21 to 42 after anthesis), there is shift in metabolic path of carbon from sucrose to starch.
 ...
PMID:Photosynthetic carbon reduction cycle metabolites and enzymes of sucrose and starch biosynthesis in developing Brassica pods. 814 70

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 (32)P-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 Mg(2+) in the assay from 10 to 2 mM. Under likely physiological conditions (pH 7.0 and 2 mM Mg(2+)), 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-1,6P(2) > 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.
 ...
PMID:Regulation of a plant SNF1-related protein kinase by glucose-6-phosphate. 1080 57