scholarly journals Kinetic Characterization of Spinach Leaf Sucrose-Phosphate Synthase

1982 ◽  
Vol 69 (5) ◽  
pp. 1027-1030 ◽  
Author(s):  
Jacob Amir ◽  
Jack Preiss
Keyword(s):  
Sucrose Phosphate Synthase ◽  
Kinetic Characterization ◽  
Spinach Leaf ◽  
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

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.

Purification, cloning and expression of spinach leaf sucrose-phosphate synthase in Escherichia coli

Planta ◽  
1993 ◽  
Vol 189 (2) ◽  
Author(s):  
U. Sonnewald ◽  
W.P. Quick ◽  
E. MacRae ◽  
K.-P. Krause ◽  
Mark Stitt
Keyword(s):  
Escherichia Coli ◽  
Sucrose Phosphate Synthase ◽  
Cloning And Expression ◽  
Spinach Leaf ◽  
Sucrose Phosphate ◽  
Phosphate Synthase

Characterization of a Maize Sucrose–phosphate Synthase Protein and Its Effect on Carbon Partitioning in Transgenic Rice Plants

1999 ◽  
Vol 2 (3) ◽  
pp. 172-177 ◽  
Author(s):  
Kiyomi Ono ◽  
Ken Ishimaru ◽  
Naohiro Aoki ◽  
Sakiko Takahashi ◽  
Kenjiroh Ozawa ◽  
...  
Keyword(s):  
Transgenic Rice ◽  
Sucrose Phosphate Synthase ◽  
Carbon Partitioning ◽  
Rice Plants ◽  
Transgenic Rice Plants ◽  
Sucrose Phosphate ◽  
Phosphate Synthase
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