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R0878

Sigma-Aldrich

D-Ribulose 1,5-bisphosphate sodium salt hydrate

≥90% (TLC)

Synonym(s):

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

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About This Item

Empirical Formula (Hill Notation):
C5H12O11P2 · xNa+ · yH2O
CAS Number:
Molecular Weight:
310.09 (anhydrous free acid basis)
UNSPSC Code:
12352201
NACRES:
NA.28

biological source

synthetic (inorganic)

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘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 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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