scholarly journals Sucrose Phosphate Synthase, a Key Enzyme for Sucrose Biosynthesis in Plants

1991 ◽  
Vol 96 (2) ◽  
pp. 473-478 ◽  
Author(s):  
Jean-Michel Bruneau ◽  
Ann C. Worrell ◽  
Bernard Cambou ◽  
Danielle Lando ◽  
Toni A. Voelker
2019 ◽  
Vol 6 (1) ◽  
pp. 130
Author(s):  
Suwinda Fibriani ◽  
Inyana Dwi Agustien ◽  
Widhi Dyah Sawitri ◽  
Bambang Sugiharto

Genetic Transformation and Expression of Sucrose Phosphate Synthase Mutant in Tomato Plant ABSTRACTSucrose phosphate synthase (SPS) is a key enzyme responsible for sucrose biosynthesis. In its regulation, SPS activity is modulated by an allosteric effector glucose-6-phosphate (G6P) suggested to have an ability to bind SPS N-terminus domain. To understand the role of N-terminus in regulating SPS, the SPS gene was mutated with the deletion of N-terminus domain (∆N-SPS). The ∆N-SPS gen was transformed into tomato plants with 5% transformation efficiency. Three transgenic tomato plant 4.20, 5.5.1, and 5.10 were obtained and confirmed by PCR analysis. Transgenic tomato expression was characterized by enzymatic analysis. Result showed that the G6P allosteric regulation in transgenic ∆N-SPS had lost and the SPS activity increased by 2-fold compared to non-transgenic plant. This showed that N-terminus domain-deleted SPS could be actively expressed in plant. Keywords: enzyme, genetic transformation, N-terminus domain deletion, sucrose phosphate synthase, tomato ABSTRAKSucrose phosphate synthase (SPS) merupakan enzim kunci yang bertanggung jawab dalam sintesis sukrosa. Dalam regulasinya, aktifitas SPS dipengaruhi oleh alosterik efektor glukosa-6-fosfat (G6P) yang diduga dapat berikatan pada domain N-terminus SPS. Untuk mengetahui peran N-terminus pada regulasi SPS, dilakukan mutasi SPS dengan penghilangan domain N-terminus (∆N-SPS). Gen ∆N-SPS diinsersi pada tanaman tomat melalui transformasi genetik dengan efisiensi transformasi 5%. Tiga tanaman transgenik tomat (event4.20; 5.5.1; dan 5.10) didapatkan dan positif terkonfirmasi melalui analisis PCR. Ekspresi mutan dikarakterisasi melalui analisis enzimatik. Hasil menunjukkan bahwa tanaman tomat transgenik ∆N-SPS tidak dipengaruhi regulasi alosterik G6P dan aktifitas SPS 2 kali lipat lebih tinggi daripada tanaman bukan transgenik. Ini menunjukkan bahwa SPS dengan delesi domain N-terminus dapat terekspresi aktif pada tanaman.  Kata Kunci: delesi domain N-terminus, enzim, sucrose phosphate synthase, tomat, transformasi genetik 


2013 ◽  
Vol 347 (1) ◽  
pp. 43-51 ◽  
Author(s):  
Sergey Y. But ◽  
Valentina N. Khmelenina ◽  
Alexander S. Reshetnikov ◽  
Yuri A. Trotsenko

Plants ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 200 ◽  
Author(s):  
Risky Mulana Anur ◽  
Nurul Mufithah ◽  
Widhi Dyah Sawitri ◽  
Hitoshi Sakakibara ◽  
Bambang Sugiharto

Sucrose phosphate synthase (SPS) is a key enzyme in sucrose synthesis, which controls sucrose content in plants. This study was designed to examine the efficacy of the overexpression of SoSPS1 gene on sucrose accumulation and carbon partitioning in transgenic sugarcane. The overexpression of SoSPS1 gene increased SPS activity and sucrose content in transgenic sugarcane leaves. More importantly, the overexpression enhanced soluble acid invertase (SAI) activity concomitant with the increase of glucose and fructose levels in the leaves, whereas sucrose synthase activity exhibited almost no change. In the stalk, a similar correlation was observed, but a higher correlation was noted between SPS activity and sugar content. These results suggest that SPS overexpression has both direct and indirect effects on sugar concentration and SAI activity in sugarcane. In addition, SPS overexpression resulted in a significant increase in plant height and stalk number in some transgenic lines compared to those in non-transgenic control. Taken together, these results strongly suggest that enhancing SPS activity is a useful strategy for improving sugarcane yield.


2017 ◽  
Vol 59 (2) ◽  
pp. 7-15
Author(s):  
Yun-Wei Zhang ◽  
Yun-Zhuan Zhou ◽  
Hai-Bo Lu ◽  
Deng-Yu Zheng ◽  
Yan-Hua Huang

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.


2006 ◽  
Vol 33 (6) ◽  
pp. 605 ◽  
Author(s):  
C. P. L. Grof ◽  
C. T. E. So ◽  
J. M. Perroux ◽  
G. D. Bonnett ◽  
R. I. Forrester

Sucrose-phosphate synthase (SPS) is a key enzyme in the pathway of sucrose synthesis. Five different gene families encoding SPS have been reported in the Poaceae [Castleden CK, Aoki N, Gillespie VJ, MacRae EA, Quick WP, Buchner P, Foyer CH, Furbank RT, Lunn JE (2004) Evolution and function of the sucrose-phosphate synthase gene families in wheat and other grasses. Plant Physiology 135, 1753–1764]. Expression of the five families in leaf and stem tissues of Saccharum spp. at different stages of development was determined by quantitative real-time PCR. The type B and C families of SPS genes were predominantly expressed in both immature and mature leaves, whereas the two subfamilies making up the type D family were expressed at similar levels in all tissues examined. In the type A family, expression was lowest in leaves and increased from the meristem region down to internode 7 of the stem.


2002 ◽  
Vol 29 (5) ◽  
pp. 569 ◽  
Author(s):  
Rui Zhou ◽  
Richard C. Sicher ◽  
Bruno Quebedeaux

Sucrose-phosphate synthase (SPS) from mature apple (Malus domestica Borhk. cv. Gala) leaves was purified 34-fold to a final specific activity of 15.3 μmol mg–1 protein h–1. The enzyme showed hyperbolic saturation kinetics for both fructose-6-phosphate (F6P) (Km= 0.36 mM) and uridine-5′-diphosphoglucose (UDPG) (Km = 6.49 mM). Glucose-6-phosphate (G6P) was found to be an activator of apple SPS, and the activation was dependent upon the F6P concentration. At a concentration of 2 mM, G6P significantly decreased the Km for F6P and increased SPS activity. However, higher concentrations of G6P did not further stimulate SPS activity. In contrast to SPS from other plant species, inorganic phosphate (Pi) had little or no inhibitory effect on apple SPS. The apple leaf enzyme was inhibited 7–10% by 10 mM Pi when F6P concentrations were in the range of 2–10 mM. We observed that sorbitol-6-phosphate, an intermediate metabolite in sorbitol biosynthesis, was a competitive inhibitor of SPS with a Ki of 1.83 mM. Sorbitol-6-phosphate also inhibited G6P activation of SPS. Our results suggest that sucrose biosynthesis may be altered by the products of sorbitol biosynthesis in apple leaves.


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