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83895

Sigma-Aldrich

D-Ribulose 1,5-bisphosphate sodium salt hydrate

≥99.0% (TLC)

Synonym(s):

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

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$234.00
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$877.00

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Estimated to ship onMarch 29, 2025


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10 MG
$234.00
50 MG
$877.00

About This Item

Empirical Formula (Hill Notation):
C5H12O11P2 · xNa+ · yH2O
CAS Number:
Molecular Weight:
310.09 (anhydrous free acid basis)
MDL number:
UNSPSC Code:
12352201
NACRES:
NA.25

$234.00


Estimated to ship onMarch 29, 2025


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Quality Level

assay

≥99.0% (TLC)

form

powder

color

white

solubility

H2O: 50 mg/mL, clear, colorless to light yellow

storage temp.

−20°C

SMILES string

[P](=O)(OC[C@@H](O)[C@@H](O)C(=O)CO[P](=O)(O)O)(O)O

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

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 characterize 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.
Active site studies with ribulose-1,5-biphosphate carboxylase[1]

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


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S N Mogel et al.
Biochemistry, 28(13), 5428-5431 (1989-06-27)
Irradiation of ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach in the presence of vanadate at 4 degrees C resulted in rapid loss of carboxylase activity. The inactivation was light and vanadate dependent. When the enzyme was irradiated in the presence of the substrate
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
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
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
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

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