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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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About This Item

Empirical Formula (Hill Notation):
C5H12O11P2 · xNa+ · yH2O
CAS Number:
1897433-92-9
Molecular Weight:
310.09 (anhydrous free acid basis)
UNSPSC Code:
12352201
NACRES:
NA.25

Assay

≥99.0% (TLC)

form

powder

color

white

solubility

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

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

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

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)

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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
T Kawaguchi et al.
The Journal of biological chemistry, 276(30), 28554-28561 (2001-05-25)
Macrophages can adapt to the absence of oxygen by switching to anaerobic glycolysis. In this study, we investigated (a) the roles of fructose 2,6-bisphosphate (Fru-2,6-P2) and ribose 1,5-bisphosphate (Rib-1,5-P2), potent activators of phosphofructokinase, (b) the enzymes responsible for the synthesis
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
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
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