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evolution
Thermosynechococcus vestitus
the FBP/SBPase found in Thermosynechococcus elongatus is a type II FBPase, a member of the larger Li+-sensitive phosphatase superfamily. It shares 80% sequence identity with the Synechocystis sp. PCC 6803 FBP/SBPase
malfunction
overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase (BiBPase) alters the carbon partitioning to extracellular carbohydrate. It induces carbohydrate partitioning which is significantly different from that in the wild-type and more towards extracellular carbohydrate and less towards glycogen. The activities of aldolase and ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) are enhanced by overexpression of BiBPase compared to wild-type, while glucose 6-phosphate dehydrogenase activity is decreased. Overexpression of BiBPase leads to enhanced cell size and photosynthetic O2 evolution. Overexpression of BiBPase in Synechococcus sp. PCC 7002 confers faster growth under elevated [CO2] and light conditions, but not under conditions where the amount of either light or CO2 is limiting
malfunction
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overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase (BiBPase) alters the carbon partitioning to extracellular carbohydrate. It induces carbohydrate partitioning which is significantly different from that in the wild-type and more towards extracellular carbohydrate and less towards glycogen. The activities of aldolase and ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) are enhanced by overexpression of BiBPase compared to wild-type, while glucose 6-phosphate dehydrogenase activity is decreased. Overexpression of BiBPase leads to enhanced cell size and photosynthetic O2 evolution. Overexpression of BiBPase in Synechococcus sp. PCC 7002 confers faster growth under elevated [CO2] and light conditions, but not under conditions where the amount of either light or CO2 is limiting
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malfunction
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overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase (BiBPase) alters the carbon partitioning to extracellular carbohydrate. It induces carbohydrate partitioning which is significantly different from that in the wild-type and more towards extracellular carbohydrate and less towards glycogen. The activities of aldolase and ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) are enhanced by overexpression of BiBPase compared to wild-type, while glucose 6-phosphate dehydrogenase activity is decreased. Overexpression of BiBPase leads to enhanced cell size and photosynthetic O2 evolution. Overexpression of BiBPase in Synechococcus sp. PCC 7002 confers faster growth under elevated [CO2] and light conditions, but not under conditions where the amount of either light or CO2 is limiting
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metabolism
Sedoheptulose-1,7-bisphosphatase is a key enzyme in the photosynthetic carbon reduction cycle, i.e. Calvin cycle
metabolism
the enzyme is involved in the Calvin-Benson-Bassham cycle, the main pathway to fix atmospheric CO2 and store energy in carbon bonds, forming the precursors of most primary and secondary metabolites necessary for life
metabolism
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Sedoheptulose-1,7-bisphosphatase is a key enzyme in the photosynthetic carbon reduction cycle, i.e. Calvin cycle
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physiological function
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the C3 cycle enzyme sedoheptulose-1,7 bisphosphatase exerts strong metabolic control over ribulose-5-phosphate regeneration at light saturation
physiological function
expression of sedoheptulose-1,7-bisphosphatase in Dunaliella bardawil leads to larger cell size, enhanced photosynthetic activity, increased total organic carbon content and improved glycerol production
physiological function
Thermosynechococcus vestitus
bifunctional enzyme FBP/SBPase is unique in that it catalyses two separate reactions in the Calvin cycle, both of which are catalysed by separate enzymes in plants. The reactions catalysed by FBP/SBPase are important for Calvin cycle flux, as indicated by their high predicted metabolic control coefficients
physiological function
construction of transgenic Arabidopsis thaliana plants with altered combinations of sedoheptulose 1,7-bisphosphatase (SBPase), fructose 1,6-bisphosphate aldolase (FBPA) and glycine decarboxylase-H protein (GDC-H). Increasing the levels of the three corresponding proteins, either independently or in combination, significantly increases the quantum efficiency of photosystem PSII. Lines over-expressing SBPase and FBP display an increase in the maximum efficiency of CO2 fixation. The co-expression of GDC-H with SBPase and FBPA results in a cumulative positive impact on leaf area and biomass
physiological function
expression of enzyme in Euglena gracilis cells to enhance its photosynthetic activity. The cell volume of the transgenic cell line is significantly larger than that of wild-type cells under normal growth conditions and the photosynthetic activity is significantly higher than that of wild type under high light and high CO2, resulting in enhanced biomass production. The accumulation of paramylon is increased. Transgenic cell lines grown under high light and high CO2 and placed on anaerobiosis show approximately 13- to 100fold higher productivity of wax esters than in wild-type cells
physiological function
in transgenic plants overexpressing SBPase, photosynthetic rates are increased and in parallel an increase in sucrose and starch accumulation is evident. Total biomass and leaf area are increased in SBPase sense plants, and are reduced in SBPase antisense plants compared with wild-type. Under chilling stress, tomato plants with increased SBPase activity are more chilling tolerant due to reduced electrolyte leakage, increased photosynthetic capacity, and elevated RuBP regeneration rate and quantum efficiency of photosystem II
physiological function
methyl jasmonate and dark induce senescence in detached tomato leaves and concomitantly downregulate the expression and reduce SBPase activity. Mutagenesis of SBPase leads to senescence-associated characteristics in mutant plants, including loss of chlorophyll, repressed photosynthesis, increased membrane ion leakage, and enhanced transcript abundance of senescence-associated genes
physiological function
overexpression of BiBPase enhances growth, cell size, and photosynthetic O2 evolution, and coordinately upregulates enzymes in the Calvin Benson cycle including RuBisCO and fructose-1,6-bisphosphate aldolase. Overexpression downregulates enzymes in respiratory carbon metabolism including glucose-6-phosphate dehydrogenase. The content of glycogen is significantly reduced while the soluble carbohydrate content is increased
physiological function
overexpression of SBPase and Rubisco in order to improve photosynthesis. An increase in SBPase and Rubisco contents by 82-102% and 20-30%, respectively, doesnot increase CO2 assimilation rate under the conditions of high irradiance and different CO2 partial pressures. Overproduction and antisense suppression of SBPase does not greatly affect CO2 assimiation at high CO2 concentration
physiological function
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expression of sedoheptulose-1,7-bisphosphatase in Dunaliella bardawil leads to larger cell size, enhanced photosynthetic activity, increased total organic carbon content and improved glycerol production
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physiological function
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expression of enzyme in Euglena gracilis cells to enhance its photosynthetic activity. The cell volume of the transgenic cell line is significantly larger than that of wild-type cells under normal growth conditions and the photosynthetic activity is significantly higher than that of wild type under high light and high CO2, resulting in enhanced biomass production. The accumulation of paramylon is increased. Transgenic cell lines grown under high light and high CO2 and placed on anaerobiosis show approximately 13- to 100fold higher productivity of wax esters than in wild-type cells
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additional information
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enzyme-overexpressing Nicotiana tabacum plants show greater carbon assimilation and electron transport rates compared to non-transfected plants, phenotype, overview
additional information
Thermosynechococcus vestitus
active-site residue are Asp33, Glu57, Glu100, Thr102, Tyr131, Lys134, Arg176, Arg178, Asp198, Asp200, and Glu225