scholarly journals Role of Sucrose-Phosphate Synthase in Sucrose Metabolism in Leaves

1992 ◽  
Vol 99 (4) ◽  
pp. 1275-1278 ◽  
Author(s):  
Steven C. Huber ◽  
Joan L. Huber
Keyword(s):  
Sucrose Phosphate Synthase ◽  
Sucrose Metabolism ◽  
Sucrose Phosphate ◽  
Phosphate Synthase

scholarly journals Sucrose metabolism in cold-stored potato tubers with decreased expression of sucrose phosphate synthase

1998 ◽  
Vol 21 (3) ◽  
pp. 285-299 ◽  
Author(s):  
K.-P. Krause ◽  
L. Hill ◽  
R. Reimholz ◽  
T. Hamborg Nielsen ◽  
U. Sonnewald ◽  
...  
Keyword(s):  
Sucrose Phosphate Synthase ◽  
Sucrose Metabolism ◽  
Potato Tubers ◽  
Sucrose Phosphate ◽  
Phosphate Synthase

scholarly journals Cloning, Expression and Genetic Transformation of Sucrose Phosphate Synthase (Sps) Gene in Saccharum Spontaneum L.

2017 ◽  
Vol 59 (2) ◽  
pp. 7-15
Author(s):  
Yun-Wei Zhang ◽  
Yun-Zhuan Zhou ◽  
Hai-Bo Lu ◽  
Deng-Yu Zheng ◽  
Yan-Hua Huang
Keyword(s):  
Sucrose Phosphate Synthase ◽  
Saccharum Spontaneum ◽  
Reading Frame ◽  
Acid Protein ◽  
Significant Difference ◽  
Key Enzyme ◽  
Young Leaves ◽  
Sucrose Phosphate ◽  
Phosphate Synthase

AbstractSucrose phosphate synthase (SPS) is a key enzyme catalyzing sucrose metabolism in plants. In this study, we isolated the SPS cDNA from Saccharum spontaneum and designated as SsSPS (GenBank accession no. MF398541). The full-length of SsSPS cDNA was 4153-bp with an opening reading frame (ORF) of 3132 nucleotides, which encoded a 1043-amino acid protein. The nucleotide sequences alignment showed that it had 98%, 97% and 87% homology with S. officinarum, Setaria italica and Lolium perenne, respectively. Moreover, the SsSPS was detected to express in leaf and stem tissues of S. spontaneum and exhibited a predominant expression in the stem tissue. However, there was no significant difference in the expression level of SsSPS between young leaves and mature ones. Additionally, we generated transgenic S. spontaneum using Agrobacterium-mediated transformation. Our data will provide a valuable foundation for further study of the potential role of SPS in plants.

scholarly journals Sucrose Metabolism and Purification and Characterization of Sucrose Synthase from Lycopersicon esculentum var. cerasiforme Fruit

HortScience ◽  
1997 ◽  
Vol 32 (3) ◽  
pp. 491E-491
Author(s):  
Md. Shahidul Islam ◽  
S. Khan ◽  
T. Matsui
Keyword(s):  
Lycopersicon Esculentum ◽  
Sucrose Synthase ◽  
Enzymatic Reaction ◽  
Sucrose Phosphate Synthase ◽  
Acid Invertase ◽  
Sucrose Metabolism ◽  
Cherry Tomato ◽  
Fructose 2 ◽  
Sucrose Phosphate ◽  
Phosphate Synthase

Sucrose metabolism was followed in developing fruit of domesticated cherry tomato (Lycopersicon esculentum var. cerasiforme Alef.). The high amounts of reducing sugars were consistently linked to high soluble acid invertase (EC 3.2.1.26), whereas sucrose synthase (EC 2.4.1.13) followed the same pattern of sucrose levels and reached a peak of activity during early stage of maturation and then decreased to near nil. In comparison, sucrose phosphate synthase (EC 2.4.1.14) activity remain relatively constant throughout development. Thus, sucrose synthase and acid invertase, rather than sucrose phosphate synthase, are the critical enzymes regulating sucrose accumulation in tomatoes. Cultivated cherry tomato sucrose synthase (UDP-glucose: D-fructose 2-glucosyltransferase) was purified to homogeneity by ammonium sulfate precipitation, anion exchange chromatography on DEAE-Toyopreal 650, and gel filtration on Sephadex G-200. Further purification to homogeneity resulted from a single band from SDS-PAGE. The enzyme was identified as a homotetramer with a total molecular mass of 370 kDa and subunits of 92 kDa. The enzyme showed maximum activity for the cleavage and synthesis of sucrose was at pH 7.0 and 8.0, respectively, and the optimum temperature was 40°C in both directions for HEPES-KOH buffer. The enzymatic reaction followed typical Michaelis–Menten kinetics, with the following parameters: Km (fructose),7.4; Km (UDP-glucose), 0.2612; Km (sucrose), 33.24; Km (UDP), 0.0946. The enzyme was very sensitive to inhibition by heavy metals.

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