R0878
D-Ribulose 1,5-bisphosphate sodium salt hydrate
≥90% (TLC)
Synonyme(s) :
D-érythro-2-Pentulose, 1,5-bis(dihydrogénophosphate), D-Ribulose 1,5-diphosphate, RuDP
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About This Item
Formule empirique (notation de Hill):
C5H12O11P2 · xNa+ · yH2O
Numéro CAS:
Poids moléculaire :
310.09 (anhydrous free acid basis)
Code UNSPSC :
12352201
Nomenclature NACRES :
NA.28
Produits recommandés
Source biologique
synthetic (inorganic)
Pureté
≥90% (TLC)
Forme
powder
Impuretés
≤16% water (Karl Fischer)
Couleur
white
Solubilité
water: ~50 g/L
Traces de cations
Na: 17.1-24.6% (dry basis)
Température de stockage
−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
Clé InChI
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).
Actions biochimiques/physiologiques
Le ribulose-1,5-bisphosphate (RuBP) est un composant du cycle de Calvin qui est métabolisé en glycérate 3-phosphate (G3P) par l′enzyme dénommée ribulose bisphosphate carboxylase/oxygénase (RuBisCO). Le RuBP sert à identifier, différencier et caractériser la (les) ribulose bisphosphate carboxylase(s)/oxygénase(s) (RuBisCO).
Autres remarques
Pour bien comprendre notre vaste gamme de monosaccharides et tout ce qu'elle peut apporter à vos recherches, nous vous encourageons à visiter notre page dédiée aux glucides.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Faceshields, Gloves, type P2 (EN 143) respirator cartridges
Certificats d'analyse (COA)
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Journal of experimental botany, 67(10), 3137-3148 (2016-04-29)
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S Ogushi et al.
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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
Takaaki Sato et al.
Science (New York, N.Y.), 315(5814), 1003-1006 (2007-02-17)
The type III ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCO) present in the archaeon Thermococcus kodakaraensis was found to participate in adenosine 5'-monophosphate (AMP) metabolism, a role that is distinct from that of classical RuBisCOs of the Calvin-Benson-Bassham cycle. Genes annotated as thymidine phosphorylase
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
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