scholarly journals NO3- Enhances the Kinase Activity for Phosphorylation of Phosphoenolpyruvate Carboxylase and Sucrose Phosphate Synthase Proteins in Wheat Leaves: Evidence from the Effects of Mannose and Okadaic Acid

1992 ◽  
Vol 99 (1) ◽  
pp. 344-347 ◽  
Author(s):  
Le Van Quy ◽  
M.-L. Champigny
Keyword(s):  
Okadaic Acid ◽  
Phosphoenolpyruvate Carboxylase ◽  
Kinase Activity ◽  
Sucrose Phosphate Synthase ◽  
Wheat Leaves ◽  
Sucrose Phosphate ◽  
Phosphate Synthase

scholarly journals Site-specific serine phosphorylation of spinach leaf sucrose-phosphate synthase

1992 ◽  
Vol 283 (3) ◽  
pp. 877-882 ◽  
Author(s):  
J L A Huber ◽  
S C Huber
Keyword(s):  
Okadaic Acid ◽  
Spinacia Oleracea ◽  
Sucrose Phosphate Synthase ◽  
Serine Phosphorylation ◽  
Spinacia Oleracea L ◽  
Spinach Leaf ◽  
Sucrose Phosphate ◽  
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 enzyme was phosphorylated and inactivated by using [gamma-32P]ATP. We now report that SPS is phosphorylated both in vivo and in vitro on serine residues. The protein is phosphorylated at multiple sites both in vivo and in vitro as indicated by two-dimensional peptide maps of the immunopurified SPS protein. After being fed with radiolabel, leaves were illuminated or given mannose (which activates the enzyme), in the presence or absence of okadaic acid. Feeding okadaic acid to leaves decreased the SPS activation state in the dark and light and in leaves fed mannose. Across all the treatments, the activation state of SPS in situ was inversely related to the labelling of two phosphopeptides (designated phosphopeptides 5 and 7). These two phosphopeptides are phosphorylated when SPS is inactivated in vitro with [gamma-32P]ATP, and thus are designated as regulatory (inhibitory) sites [Huber & Huber (1991) Biochim. Biophys. Acta 1091, 393-400]. Okadaic acid increased the total 32P-labelling of SPS and in particular increased labelling of the two regulatory sites, which explains the decline in activation state. In the presence of okadaic acid, two cryptic phosphorylation sites became labelled in vivo that were not apparent in the absence of the inhibitor. Overall, the results suggest that light/dark regulation of SPS activity occurs as a result of regulatory serine phosphorylation. Multiple sites are phosphorylated in vivo, but two sites in particular appear to regulate activity and dephosphorylation of these sites in vivo is sensitive to okadaic acid.

Regulation of sucrose-phosphate synthase in wheat (Triticum aestivum) leaves

2004 ◽  
Vol 31 (7) ◽  
pp. 685 ◽  
Author(s):  
Stephen J. Trevanion ◽  
C. Kate Castleden ◽  
Christine H. Foyer ◽  
Robert T. Furbank ◽  
W. Paul Quick ◽  
...  
Keyword(s):  
Triticum Aestivum ◽  
Feedback Inhibition ◽  
Sucrose Phosphate Synthase ◽  
High Light ◽  
Sucrose Synthesis ◽  
Short Term ◽  
Cereal Species ◽  
Wheat Leaves ◽  
Sucrose Phosphate ◽  
Phosphate Synthase

The regulation of sucrose-phosphate synthase (SPS, E.C. 2.4.1.14), a key enzyme of sucrose synthesis, was investigated in wheat (Triticum aestivum L.) leaves. Wheat SPS was activated in the light, with an increased affinity for its substrates and the activator glucose-6-phosphate, reduced sensitivity to inhibition by Pi, but no change in maximum catalytic activity. Based on these properties, assays to measure the total activity and activation state of the enzyme were established and validated using several different wheat cultivars, grown under different environmental conditions. As found in previous studies on other species, e.g. spinach, activation appeared to be linked to the prevailing rate of photosynthesis rather than light per se. Long-term exposure to higher light levels increased total SPS activity in the leaves, and some experiments indicated that this response could occur within 1 h of exposure of low-light-grown plants to high light. However, activation of pre-existing enzyme was a more common short-term response to high light. Wheat, like many important cereal species, stores a large amount of sucrose in its leaves. In contrast with spinach, which stores more starch in its leaves, accumulation of sucrose in wheat leaves did not lead to inactivation of SPS or inhibition of sucrose synthesis. In conclusion, the mechanisms linking the rates of sucrose synthesis and photosynthetic CO2 fixation in wheat leaves appear to be similar to those in other species, but the mechanisms involved in short-term feedback inhibition of sucrose synthesis by sucrose, found in starch-storing species, are lacking in wheat.

scholarly journals Comparative transcriptome analysis reveals key genes potentially related to organic acid and sugar accumulation in loquat

PLoS ONE ◽  
2021 ◽  
Vol 16 (4) ◽  
pp. e0238873
Author(s):  
Jun Yang ◽  
Jing Zhang ◽  
Xian-Qian Niu ◽  
Xue-Lian Zheng ◽  
Xu Chen ◽  
...  
Keyword(s):  
Organic Acids ◽  
Organic Acid ◽  
Fruit Development ◽  
Phosphoenolpyruvate Carboxylase ◽  
Sucrose Synthase ◽  
Sugar Content ◽  
Sucrose Phosphate Synthase ◽  
Sucrose Phosphate ◽  
Sucrose Cleavage ◽  
Phosphate Synthase

Organic acids and sugars are the primary components that determine the quality and flavor of loquat fruits. In the present study, major organic acids, sugar content, enzyme activities, and the expression of related genes were analyzed during fruit development in two loquat cultivars, ’JieFangZhong’ (JFZ) and ’BaiLi’ (BL). Our results showed that the sugar content increased during fruit development in the two cultivars; however, the organic acid content dramatically decreased in the later stages of fruit development. The differences in organic acid and sugar content between the two cultivars primarily occured in the late stage of fruit development and the related enzymes showed dynamic changes in activies during development. Phosphoenolpyruvate carboxylase (PEPC) and mNAD malic dehydrogenase (mNAD-MDH) showed higher activities in JFZ at 95 days after flowering (DAF) than in BL. However, NADP-dependent malic enzyme (NADP-ME) activity was the lowest at 95 DAF in both JFZ and BL with BL showing higher activity compared with JFZ. At 125 DAF, the activity of fructokinase (FRK) was significantly higher in JFZ than in BL. The activity of sucrose synthase (SUSY) in the sucrose cleavage direction (SS-C) was low at early stages of fruit development and increased at 125 DAF. SS-C activity was higher in JFZ than in BL. vAI and sucrose phosphate synthase (SPS) activities were similar in the two both cultivars and increased with fruit development. RNA-sequencing was performed to determine the candidate genes for organic acid and sugar metabolism. Our results showed that the differentially expressed genes (DEGs) with the greated fold changes in the later stages of fruit development between the two cultivars were phosphoenolpyruvate carboxylase 2 (PEPC2), mNAD-malate dehydrogenase (mNAD-MDH), cytosolic NADP-ME (cyNADP-ME2), aluminum-activated malate transporter (ALMT9), subunit A of vacuolar H+-ATPase (VHA-A), vacuolar H+-PPase (VHP1), NAD-sorbitol dehydrogenase (NAD-SDH), fructokinase (FK), sucrose synthase in sucrose cleavage (SS-C), sucrose-phosphate synthase 1 (SPS1), neutral invertase (NI), and vacuolar acid invertase (vAI). The expression of 12 key DEGs was validated by quantitative reverese transcription PCR (RT-qPCR). Our findings will help understand the molecular mechanism of organic acid and sugar formation in loquat, which will aid in breeding high-quality loquat cultivars.

Effects of canopy defoliation in the dark on the activity of sucrose phosphate synthase

1984 ◽  
Vol 34 (3) ◽  
pp. 247-252 ◽  
Author(s):  
Thomas W. Rufty ◽  
Steven C. Huber ◽  
Phillip S. Kerr
Keyword(s):  
Sucrose Phosphate Synthase ◽  
Sucrose Phosphate ◽  
Phosphate Synthase

scholarly journals Cloning and characterization of the Cerasus humilis sucrose phosphate synthase gene (ChSPS1)

PLoS ONE ◽  
2017 ◽  
Vol 12 (10) ◽  
pp. e0186650 ◽  
Author(s):  
Juan Wang ◽  
Junjie Du ◽  
Xiaopeng Mu ◽  
Pengfei Wang
Keyword(s):  
Sucrose Phosphate Synthase ◽  
Cerasus Humilis ◽  
Sucrose Phosphate ◽  
Phosphate Synthase

Control analysis of photosynthetic sucrose synthesis: assignment of elasticity coefficients and flux-control coefficients to the cytosolic fructose 1,6-bisphosphatase and sucrose phosphate synthase

1989 ◽  
Vol 323 (1216) ◽  
pp. 327-338 ◽  
Keyword(s):  
Sucrose Phosphate Synthase ◽  
Control Analysis ◽  
Sucrose Synthesis ◽  
Flux Control ◽  
Fructose 1,6 Bisphosphatase ◽  
Flux Control Coefficients ◽  
Sucrose Phosphate ◽  
Control Coefficients ◽  
Phosphate Synthase

The use of elasticity coefficients and flux-control coefficients in a quantitative treatment of control is discussed, with photosynthetic sucrose synthesis as an example. Experimental values for elasticities for the cytosolic fructose 1,6-bisphosphatase and sucrose phosphate synthase are derived from their in vitro properties, and from an analysis of the in vivo relation between fluxes and metabolite levels. An empirical factor α , describing the response of the fructose 2,6-bisphosphate regulator cycle to fructose 6-phosphate is described, and an expression is derived relating α to the elasticities of the enzymes involved in this regulator cycle. The in vivo values for elasticities and α are then used in a modified form of the connectivity theorem to estimate the flux control coefficients of the cytosolic fructose 1,6-bisphosphatase and sucrose phosphate synthase during rapid photosynthetic sucrose synthesis.

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