2646-35-7

Basic information

• Product Name: Sedoheptulose-7-phosphate
• Synonyms: Sedoheptulose-7-phosphate;(2,3,4,5,7-pentahydroxy-6-oxo-heptoxy)phosphonic acid;D-Sedoheptulose-7-phosphate barium salt;D-altro-Heptulose 7-phosphate lithium salt;D-Sedoheptulose 7-phosphate lithium salt
• CAS NO: 2646-35-7
• Molecular Formula: C₇H₁₅O₁₀P
• Molecular Weight: 425.474
• Mol File: 2646-35-7.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 751.4°Cat760mmHg
• Flash Point: 408.3°C
• Appearance: /
• Density: 1.862g/cm³
• Vapor Pressure: 4.61E-26mmHg at 25°C
• Refractive Index: 1.605
• Storage Temp.: ?20°C
• PKA: 1.83±0.10(Predicted)
• CAS DataBase Reference: Sedoheptulose-7-phosphate(CAS DataBase Reference)
• NIST Chemistry Reference: Sedoheptulose-7-phosphate(2646-35-7)
• EPA Substance Registry System: Sedoheptulose-7-phosphate(2646-35-7)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 2646-35-7(Hazardous Substances Data)

Usage

Definition

ChEBI: A ketoheptose phosphate consisting of sedoheptulose having a phosphate group at the 7-position. It is an intermediate metabolite in the pentose phosphate pathway.

InChI:InChI=1/C7H15O10P/c8-1-3(9)5(11)7(13)6(12)4(10)2-17-18(14,15)16/h4-8,10-13H,1-2H2,(H2,14,15,16)/t4-,5-,6-,7+/m1/s1

Upstream product

• 533-50-6 L-erythrulose 
• 3615-55-2 D-ribose 5-phosphate 

Downstream Products

• 80186-87-4 ADP-D-glycero-β-D-manno-heptose 
• 244195-43-5 2-epi-5-epi-valiolone 
• 1384518-63-1 2-epi-valiolone 

Relevant articles and documents

Chiral Polyol Synthesis Catalyzed by a Thermostable Transketolase Immobilized on Layered Double Hydroxides in Ionic liquids

In this work we set out to study the activity of a thermostable Transketolase (TK) from Geobacillus stearothermophilus (TKgst) in an ionic liquid as cosolvent, which has never been investigated before with this enzyme. 1-Butyl-3-methylimidazolium chloride ([BMIm][Cl]) in the range 30-50% in water maintained the total activity of TKgst and increased the reaction rate in the presence of pentoses as acceptor substrates, particularly d-ribose. To improve the synthetic process, TKgst was immobilized on an inorganic support, layered double hydroxides (LDHs), with excellent immobilization yield and catalytic activity using a simple, eco-compatible, efficient coprecipitation procedure. The biohybrid MgAl@TKgst was tested in 30% [BMIm][Cl] for the synthesis of a rare, very costly commercially available sugar, d-sedoheptulose, which was obtained in one step from d-ribose with an isolated yield of 82%. This biohybrid was reusable over four cycles with no loss of enzymatic activity. The particular activity of free and immobilized TKgst in [BMIm][Cl] holds promise to extend the applications of TKgst in other ionic liquids and unusual media in biocatalysis.

Efficient immobilization of yeast transketolase on layered double hydroxides and application for ketose synthesis

Transketolase (TK) from S. cerevisiae was successfully immobilized on layered double hydroxides (LDH) using simple, affordable and efficient adsorption and coprecipitation based immobilization procedures. Optimization of the preparation was performed using zinc aluminium nitrate (Zn 2Al-NO3) and magnesium aluminium nitrate (Mg 2Al-NO3) LDH as immobilization supports, and the protein-to-LDH weight ratio (Q) was varied. The highest immobilization yields (98-99%) and highest relative specific activities (4.2-4.4 U·mg -1 for the immobilized enzyme compared to 4.5 U·mg -1 for the free enzyme) were both achieved when using a protein-to-LDH weight ratio (Q) of 0.38. Efficient lyophilization of the LDH-TK bionanocomposites thus synthesized was proven to allow easy use and storage of the supported TK with no significant loss of activity over a three-month period. The kinetic parameters of the LDH-TK enzyme were comparable to those of the free TK. The LDH-TK enzyme was finally tested for the synthesis of L-erythrulose starting from hydroxypyruvate lithium salt (Li-HPA) and glycolaldehyde (GA) as substrates. L-erythrulose was characterized and obtained with an isolated yield of 56% similar to that obtained with free TK. The reusability of the LDH-TK biohybrid material was then investigated, and we found no loss of enzymatic activity over six cycles. Copyright