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Merck

R0878

Sigma-Aldrich

D-Ribulose 1,5-bisphosphate sodium salt hydrate

≥90% (TLC)

Sinónimos:

D-erythro-2-Pentulose, 1,5-bis(dihydrogen phosphate), D-Ribulose 1,5-diphosphate, RuDP

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About This Item

Fórmula empírica (notación de Hill):
C5H12O11P2 · xNa+ · yH2O
Número de CAS:
Peso molecular:
310.09 (anhydrous free acid basis)
UNSPSC Code:
12352201
NACRES:
NA.28

biological source

synthetic (inorganic)

Quality Level

assay

≥90% (TLC)

form

powder

impurities

≤16% water (Karl Fischer)

color

white

solubility

water: ~50 g/L

cation traces

Na: 17.1-24.6% (dry basis)

storage temp.

−20°C

InChI

1S/C5H12O11P2/c6-3(1-15-17(9,10)11)5(8)4(7)2-16-18(12,13)14/h3,5-6,8H,1-2H2,(H2,9,10,11)(H2,12,13,14)/t3-,5-/m1/s1

InChI key

YAHZABJORDUQGO-NQXXGFSBSA-N

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Application


  • Bio-Inspired Microreactors Continuously Synthesize Glucose Precursor from CO(2) with an Energy Conversion Efficiency 3.3 Times of Rice.: This study leverages D-Ribulose 1,5-bisphosphate sodium salt hydrate in bio-inspired microreactors to synthesize glucose precursors from CO₂. The approach demonstrates an energy conversion efficiency significantly higher than that of rice, highlighting its potential for efficient carbon fixation and bioengineering applications (Zhu et al., 2024).

  • Designing Stacked Assembly of Type III Rubisco for CO₂ Fixation with Higher Efficiency.: The research utilizes D-Ribulose 1,5-bisphosphate sodium salt hydrate to enhance the efficiency of CO₂ fixation through the stacked assembly of Type III Rubisco. This innovative approach offers improvements in metabolic engineering for carbon capture and utilization (Zeng et al., 2022).

  • Continuous artificial synthesis of glucose precursor using enzyme-immobilized microfluidic reactors.: This study explores the continuous synthesis of glucose precursors using microfluidic reactors with immobilized enzymes, including D-Ribulose 1,5-bisphosphate sodium salt hydrate. The technique demonstrates potential for scalable biochemical production processes (Zhu et al., 2019).

Biochem/physiol Actions

Ribulose-1,5-bisphosphate (RuBP) is a component of the Calvin cycle that is metabolized into glycerate 3-phosphate (G3P) by the enzyme ribulose bisphosphate carboxylase/oxygenase (RuBisCO). RuBP is used to identify, differentiate and characterized ribulose bisphosphate carboxylase(s)/oxygenase(s) (RuBisCO).

Other Notes

To gain a comprehensive understanding of our extensive range of Monosaccharides for your research, we encourage you to visit our Carbohydrates Category page.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Faceshields, Gloves, type P2 (EN 143) respirator cartridges


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Robert E Sharwood et al.
Journal of experimental botany, 67(10), 3137-3148 (2016-04-29)
Plants operating C3 and C4 photosynthetic pathways exhibit differences in leaf anatomy and photosynthetic carbon fixation biochemistry. Fully understanding this underpinning biochemical variation is requisite to identifying solutions for improving photosynthetic efficiency and growth. Here we refine assay methods for
M Sawada et al.
The international journal of biochemistry & cell biology, 32(4), 447-454 (2000-04-13)
6-Phosphofructo-1-kinase and fructose-1,6-bisphosphatase are rate-limiting enzymes for glycolysis and gluconeogenesis respectively, in the fructose 6-phosphate/fructose 1,6-bisphosphate cycle in the liver. The effect of ribose 1,5-bisphosphate on the enzymes was investigated. Ribose 1,5-bisphosphate synergistically relieved the ATP inhibition and increased the
I Ozaki et al.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 125(1), 97-102 (2000-06-07)
Fructose-1,6-bisphosphatase is one of the regulatory enzymes of gluconeogenesis in kidney cortex. The effect of ribose 1,5-bisphosphate on fructose-1,6-bisphosphatase purified from rat kidney cortex was studied. Rat kidney cortex, fructose-1,6-bisphosphatase exhibited hyperbolic kinetics with regard to its substrate, but the
S Ogushi et al.
The Journal of biological chemistry, 265(19), 10943-10949 (1990-07-05)
The tissue contents of previously known allosteric effectors of brain phosphofructokinase (EC 2.7.1.11) (PFK) and the kinetic behavior of isolated PFK were investigated during the initiation of rapid glycolytic flux in freeze-blown rat brain. Comparing 0- with 5-s brains revealed
M Willemoës et al.
Biochemistry, 36(16), 5078-5083 (1997-04-22)
The mechanism of binding of the substrates Mg x ATP and ribose 5-phosphate as well as Mg2+ to the enzyme 5-phospho-D-ribosyl (alpha-1-diphosphate synthetase from Escherichia coli has been analyzed. By use of the competive inhibitors of ATP and ribose 5-phosphate

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