EC Number   |
General Information |
Reference |
|---|
    3.1.3.37 | evolution |
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 |
749507 |
| 3.1.3.37 | 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 |
-, 751470 |
| 3.1.3.37 | metabolism |
Sedoheptulose-1,7-bisphosphatase is a key enzyme in the photosynthetic carbon reduction cycle, i.e. Calvin cycle |
-, 716913 |
| 3.1.3.37 | 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 |
748559 |
| 3.1.3.37 | more |
active-site residue are Asp33, Glu57, Glu100, Thr102, Tyr131, Lys134, Arg176, Arg178, Asp198, Asp200, and Glu225 |
749507 |
| 3.1.3.37 | more |
enzyme-overexpressing Nicotiana tabacum plants show greater carbon assimilation and electron transport rates compared to non-transfected plants, phenotype, overview |
714630 |
| 3.1.3.37 | physiological function |
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 |
749507 |
| 3.1.3.37 | 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 |
751838 |
| 3.1.3.37 | 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 |
-, 750140 |
| 3.1.3.37 | 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 |
-, 730578 |
