R0878
D-核糖1,5-双磷酸酯 钠盐 水合物
≥90% (TLC)
别名:
D-赤型-2-戊糖，1,5-双（磷酸二氢）, D-核糖1,5-二磷酸酯, RuDP
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关于此项目
经验公式（希尔记法）:
C5H12O11P2 · xNa+ · yH2O
化学文摘社编号:
分子量:
310.09 (anhydrous free acid basis)
UNSPSC Code:
12352201
NACRES:
NA.28
产品名称
D-核糖1,5-双磷酸酯 钠盐 水合物, ≥90% (TLC)
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
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
Quality Level
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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.：该研究用D-核酮糖-1,5-二磷酸钠盐水合物与CO₂通过生物启发式微反应器合成葡萄糖前体。这种方法的能量转换效率远高于大米，具有高效固碳和生物工程应用潜力(Zhu et al., 2024)。
- Designing Stacked Assembly of Type III Rubisco for CO₂ Fixation with Higher Efficiency.：该研究通过堆积装配III型Rubisco（核酮糖二磷酸羧化酶）提高CO₂固定效率，其中用到D-核酮糖-1,5-二磷酸钠盐水合物。这种创新方法改进了碳捕获和利用方面的代谢工程(Zeng et al., 2022)。
- Continuous artificial synthesis of glucose precursor using enzyme-immobilized microfluidic reactors.：该研究用微流控反应器固定酶连续合成葡萄糖前体，反应用到D-核酮糖-1,5-二磷酸钠盐水合物。说明本品在可放大生物生产过程中的应用前景(Zhu et al., 2019)。
Biochem/physiol Actions
1,5-双磷酸核糖（RuBP）是加尔文循环的一个组成部分，被核糖双磷酸羧化酶/加氧酶（RuBisCO）代谢为 3-磷酸甘油酯（G3P）。RuBP 用于鉴定、鉴别和表征核糖双磷酸羧化酶/加氧酶（RuBisCO）。
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Faceshields, Gloves, type P2 (EN 143) respirator cartridges
法规信息
涉药品监管产品
此项目有
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
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
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
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
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