83895
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:
Molecular Weight:
310.09 (anhydrous free acid basis)
UNSPSC Code:
12352201
NACRES:
NA.25
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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
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
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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
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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