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生物源
synthetic (inorganic)
化驗
≥90% (TLC)
形狀
powder
雜質
≤16% water (Karl Fischer)
顏色
white
溶解度
water: ~50 g/L
正離子痕跡
Na: 17.1-24.6% (dry basis)
儲存溫度
−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 密鑰
YAHZABJORDUQGO-NQXXGFSBSA-N
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應用
- 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).
生化/生理作用
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)。
儲存類別代碼
11 - Combustible Solids
水污染物質分類(WGK)
WGK 3
閃點(°F)
Not applicable
閃點(°C)
Not applicable
個人防護裝備
Eyeshields, Faceshields, Gloves, type P2 (EN 143) respirator cartridges
其他客户在看
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
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
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
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
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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