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
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Les clients ont également consulté
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 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
Bjarne Hove-Jensen et al.
Journal of bacteriology, 185(9), 2793-2801 (2003-04-18)
An enzymatic pathway for synthesis of 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP) without the participation of PRPP synthase was analyzed in Escherichia coli. This pathway was revealed by selection for suppression of the NAD requirement of strains with a deletion of the prs
Akira Nakamura et al.
The Journal of biological chemistry, 287(25), 20784-20796 (2012-04-19)
Ribose-1,5-bisphosphate isomerase (R15Pi) is a novel enzyme recently identified as a member of an AMP metabolic pathway in archaea. The enzyme converts d-ribose 1,5-bisphosphate into ribulose 1,5-bisphosphate, providing the substrate for archaeal ribulose-1,5-bisphosphate carboxylase/oxygenases. We here report the crystal structures
T Ozeki et al.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 124(3), 327-332 (2000-01-13)
Phosphofructokinase (EC 2.7.1.11) is a major enzyme of the glycolytic pathway, catalyzing the conversion of fructose 6-phosphate to fructose 1,6-bisphosphate. In this study, we demonstrated the effect of ribose 1,5-bisphosphate on phosphofructokinase purified from rat kidney cortex. Ribose 1,5-bisphosphate relieved
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