59-56-3

Usage

Uses

Used in Pharmaceutical Industry:
Glucose 1-(dihydrogen phosphate) is used as an intermediate in the synthesis of various pharmaceutical compounds for [application reason]. Its unique structure allows it to be a key component in the development of drugs targeting specific biological pathways.
Used in Biochemical Research:
In the field of biochemical research, glucose 1-(dihydrogen phosphate) is used as a substrate or a starting material for the study of enzymatic reactions and metabolic pathways. Its role in understanding the fundamental processes of cellular metabolism is significant.
Used in Food Industry:
Glucose 1-(dihydrogen phosphate) is utilized as an additive in the food industry for [application reason]. Its properties can enhance the texture, flavor, or shelf life of certain products, making it a valuable component in the development of various food items.
Used in Agricultural Industry:
In agriculture, glucose 1-(dihydrogen phosphate) is used as a component in the formulation of fertilizers and plant growth regulators for [application reason]. Its ability to support plant growth and development makes it a beneficial addition to agricultural products.
Used in Energy Production:
Glucose 1-(dihydrogen phosphate) is also used in the production of bioenergy, such as biofuels, due to its role in cellular respiration and energy metabolism. Its involvement in the conversion of glucose to energy makes it a potential candidate for enhancing energy production in biological systems.

Purification Methods

Two litres of a 5% aqueous solution of the phosphate are purified by adjusting the pH to 3.5 with glacial acetic acid (+ 3g of charcoal) and filtering. An equal volume of EtOH is added, the pH is adjusted to 8.0 (glass electrode) and the solution is stored at 3o overnight. The precipitate is filtered off, dissolved in 1.2L of distilled water, filtered and an equal volume of EtOH is added. After standing at 0o overnight, the crystals are collected at the centrifuge and washed with 95% EtOH, then absolute EtOH, ethanol/diethyl ether (1:1), and diethyl ether. [Sutherland & Wosilait, J Biol Chem 218 459 1956.] Its barium salt can be crystallised from water and EtOH. Heavy metal impurities are removed by passage of an aqueous solution (ca 1%) through an Amberlite IR-120 column (in the appropriate H+, Na+ or K+ forms). Di-K salt crystallises as a dihydrate from EtOH. [see McGready Biochemical Preparations 4 63 1955.] [Beilstein 17/8 V 247.]

InChI:InChI=1/C6H13O9P/c7-1-2-3(8)4(9)5(6(10)14-2)15-16(11,12)13/h2-10H,1H2,(H2,11,12,13)/t2-,3-,4+,5-,6+/m1/s1

Upstream product

• 25546-57-0 dibenzyl (2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl) phosphate 
• 572-09-8 2,3,4,6-tetra-O-acetyl-α-D-glucopyranosyl bromide 
• 38768-84-2 Dibenzyl(2,3,4,6-tetra-O-benzyl-β-D-glucopyranosyl)phosphat 
• 82300-63-8 Dibenzyl(β-D-glucopyranosyl)phosphat 
• 58526-05-9 2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl phosphate 
• 64-17-5 ethanol 
• 74808-10-9 O-(2,3,4,6-Tetra-O-acetyl-α-D-glucopyranosyl)trichloroacetimidate 
• 492-62-6 alpha-D-glucopyranose 
• 2520-52-7 α-D-galactopyranosyl phosphate 
• 69-79-4 D-maltose 
• 299-31-0 glucose-6-phosphate 
• 82300-58-1 dibezylphosphoryl 2,3,4,6-tetra-O-benzyl-α-D-glucopyranoside 
• 2280-44-6 D-Glucose 
• 71-43-2 benzene 

Downstream Products

• 14034-70-9 β-D-glucopyranosyl 
• 69557-93-3 O-α-D-Glucopyranosyl-(1-3)-α,β-L-rhamnopyranose 
• 492-62-6 alpha-D-glucopyranose 
• 2520-52-7 α-D-galactopyranosyl phosphate 
• 492-61-5 β-D-glucose 
• 5077-26-9 O³-α-D-Glucopyranosyl-L-arabinose 
• 1668-09-3 Maltopentaose 
• 64161-84-8 α-D-glucopyranosyl 1,2-cyclic phosphate monocyclohexylammonium salt 
• 133-89-1 UDP-glucose 
• 452322-67-7 TDP-L-mycarose 
• 2140-58-1 adenosine-5'-(α-D-glucopyranosyl)diphosphate 
• 244226-72-0 thymidine 5'-diphospho-4-amino-4,6-dideoxy-α-D-glucopyranose 
• 50-99-7 D-glucose 
• 22160-26-5 2-O-(α-D-glucopyranosyl)-glycerol 

Relevant academic research and scientific papers

Kinetic and NMR spectroscopic study of the chemical stability and reaction pathways of sugar nucleotides

The alkaline cleavage of two types of sugar nucleotides has been studied by 1H and 31P NMR in order to obtain information on the stability and decomposition pathways in aqueous solutions under alkaline conditions. The reaction of glucose 1-UDP is straightforward, and products are easy to identify. The results obtained with ribose 5-UDP and ribose 5-phosphate reveal, in contrast, a more complex reaction system than expected, and the identification of individual intermediate species was not possible. Even though definite proof for the mechanisms previously proposed could not be obtained, all the spectroscopic evidence is consistent with them. Results also emphasise the significant effect of conditions, pH, ionic strength, and temperature, on the reactivity under chemical conditions.

Toward Automated Enzymatic Glycan Synthesis in a Compartmented Flow Microreactor System

Immobilized microfluidic enzyme reactors (IMER) are of particular interest for automation of enzyme cascade reactions. Within an IMER, substrates are converted by paralleled immobilized enzyme modules and intermediate products are transported for further conversion by subsequent enzyme modules. By optimizing substrate conversion in the spatially separated enzyme modules purification of intermediate products is not necessary, thus shortening process time and increasing space-time yields. The IMER enables the development of efficient enzyme cascades by combining compatible enzymatic reactions in different arrangements under optimal conditions and the possibility of a cost-benefit analysis prior to scale-up. These features are of special interest for automation of enzymatic glycan synthesis. We here demonstrate a compartmented flow microreactor system using six magnetic enzyme beads (MEBs) for the synthesis of the non-sulfated human natural killer cell-1 (HNK-1) glycan epitope. MEBs are assembled to build compartmented enzyme modules, consisting of enzyme cascades for the synthesis of uridine 5′- diphospho-α- d-galactose (UDP-Gal) and uridine 5′-diphospho-α-d-glucuronic acid (UDP-GlcA), the donor substrates for the Leloir glycosyltransferases β4-galactosyltransferase and β3-glucuronosyltransferase, respectively. Glycan synthesis was realized in an automated microreactor system by a cascade of individual enzyme module compartments each performing under optimal conditions. The products were analyzed inline by an MS-system connected to the microreactor. The high synthesis yield of 96% for the non-sulfated HNK-1 glycan epitope indicates the excellent performance of the automated enzyme module cascade. Furthermore, combinations of other MEBs for nucleotide sugars synthesis with MEBs of glycosyltransferases have the potential for a fully automated and programmed glycan synthesis in a compartmented flow microreactor system. (Figure presented.).

β-Glucose-1,6-Bisphosphate stabilizes pathological phophomannomutase2 mutants in vitro and represents a lead compound to develop pharmacological chaperones for the most common disorder of glycosylation, PMM2-CDG

A large number of mutations causing PMM2-CDG, which is the most frequent disorder of glycosylation, destabilize phosphomannomutase2. We looked for a pharmacological chaperone to cure PMM2-CDG, starting from the structure of a natural ligand of phosphomannomutase2, α-glucose-1,6-bisphosphate. The compound, β-glucose-1,6-bisphosphate, was synthesized and characterized via 31P-NMR. β-glucose-1,6-bisphosphate binds its target enzyme in silico. The binding induces a large conformational change that was predicted by the program PELE and validated in vitro by limited proteolysis. The ability of the compound to stabilize wild type phosphomannomutase2, as well as frequently encountered pathogenic mutants, was measured using thermal shift assay. β-glucose-1,6-bisphosphate is relatively resistant to the enzyme that specifically hydrolyses natural esose-bisphosphates.

A mutant of phosphomannomutase1 retains full enzymatic activity, but is not activated by IMP: Possible implications for the disease PMM2-CDG

The most frequent disorder of glycosylation, PMM2-CDG, is caused by a deficiency of phosphomannomutase activity. In humans two paralogous enzymes exist, both of them require mannose 1,6-bis-phosphate or glucose 1,6-bis-phosphate as activators, but only phospho-mannomutase1 hydrolyzes bis-phosphate hexoses. Mutations in the gene encoding phos-phomannomutase2 are responsible for PMM2-CDG. Although not directly causative of the disease, the role of the paralogous enzyme in the disease should be clarified. Phosphoman-nomutase1 could have a beneficial effect, contributing to mannose 6-phosphate isomerization, or a detrimental effect, hydrolyzing the bis-phosphate hexose activator. A pivotal role in regulating mannose-1phosphate production and ultimately protein glycosylation might be played by inosine monophosphate that enhances the phosphatase activity of phosphoman-nomutase1. In this paper we analyzed human phosphomannomutases by conventional enzymatic assays as well as by novel techniques such as 31P-NMR and thermal shift assay. We characterized a triple mutant of phospomannomutase1 that retains mutase and phosphatase activity, but is unable to bind inosine monophosphate.

Facile enzymatic synthesis of sugar 1-phosphates as substrates for phosphorylases using anomeric kinases

Three sugar 1-phosphates that are donor substrates for phosphorylases were produced at the gram scale from phosphoenolpyruvic acid and the corresponding sugars by the combined action of pyruvate kinase and the corresponding anomeric kinases in good yields. These sugar 1-phosphates were purified through two electrodialysis steps. α-d-Galactose 1-phosphate was finally isolated as crystals of dipotassium salts. α-d-Mannose 1-phosphate and 2-acetamido-2-deoxy-α-d-glucose 1-phosphate were isolated as crystals of bis(cyclohexylammonium) salts.

Efficient chemoenzymatic synthesis of novel galacto-N-biose derivatives and their sialylated forms

Galacto-N-biose (GNB) derivatives were efficiently synthesized from galactose derivatives via a one-pot two-enzyme system containing two promiscuous enzymes from Bifidobacterium infantis: a galactokinase (BiGalK) and a d-galactosyl-β1-3-N-acetyl-d-hexosamine phosphorylase (BiGalHexNAcP). Mono-sialyl and di-sialyl galacto-N-biose derivatives were then prepared using a one-pot two-enzyme system containing a CMP-sialic acid synthetase and an α2-3-sialyltransferase or an α2-6-sialyltransferase.

Engineering the specificity of trehalose phosphorylase as a general strategy for the production of glycosyl phosphates

A two-step process is reported for the anomeric phosphorylation of galactose, using trehalose phosphorylase as biocatalyst. The monosaccharide enters this process as acceptor but can subsequently be released from the donor side, thanks to the non-reducing nature of the disaccharide intermediate. A key development was the creation of an optimized enzyme variant that displays a strict specificity (99%) for β-galactose 1-phosphate as product. This journal is the Partner Organisations 2014.

Purification and characterization of 1,3-β-D-glucan phosphorylase from Ochromonas danica

1,3-β-D-Glucan phosphorylase (BGP) is an enzyme that catalyzes the reversible phosphorolysis of 1,3-β- glucosidic linkages to form α-D-glucose 1-phosphate (G1P). Here we report on the purification and characterization of BGP from Ochromonas danica (OdBGP). The purified enzyme preparation showed three bands (113, 118, and 124 kDa) on SDS-polyacrylamide gel electrophoresis. The optimum pH and temperature were 5.5 and 25°C-30°C. OdBGP phosphorolysed laminaritriose, larger laminarioligosaccharides, and laminarin, but not laminaribiose. In the synthesis reaction, laminarin and laminarioligosaccharides served as good acceptors, but OdBGP did not act on glucose. Kinetic analysis indicated that the phosphorolysis reaction of OdBGP follows a sequential Bi Bi mechanism. The equilibrium of the enzymatic reaction indicated that OdBGP favors the reaction in the synthetic direction. Overnight incubation of OdBGP with laminaribiose and G1P resulted in the formation of precipitates, which were probably 1,3-β-glucans.

A highly efficient galactokinase from Bifidobacterium infantis with broad substrate specificity

Galactokinase (GalK), particularly GalK from Escherichia coli, has been widely employed for the synthesis of sugar-1-phosphates. In this study, a GalK from Bifidobacterium infantis ATCC 15697 (BiGalK) was cloned and over-expressed with a yield of over 80 mg/L cell cultures. The kcat/Km value of recombinant BiGalK toward galactose (164 s-1 mM -1) is 296 times higher than that of GalK from E. coli, indicating that BiGalK is much more efficient in the phosphorylation of galactose. The enzyme also exhibits activity toward galacturonic acid, which has never been observed on other wild type GalKs. Further activity assays showed that BiGalK has broad substrate specificity toward both sugars and phosphate donors. These features make BiGalK an attractive candidate for the large scale preparation of galactose-1-phosphate and derivatives.