10456-01-6

Basic information

• Product Name: glucose 1-phosphate
• CAS NO: 10456-01-6
• Molecular Weight: 260.138
• Mol File: 10456-01-6.mol
• Article Data: 25

Chemical Properties

• CAS DataBase Reference: glucose 1-phosphate(CAS DataBase Reference)
• NIST Chemistry Reference: glucose 1-phosphate(10456-01-6)
• EPA Substance Registry System: glucose 1-phosphate(10456-01-6)

Safety Data

• Hazardous Substances Data: 10456-01-6(Hazardous Substances Data)

Upstream product

• 82300-63-8 Dibenzyl(β-D-glucopyranosyl)phosphat 
• 64-17-5 ethanol 
• 25546-57-0 dibenzyl (2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl) phosphate 
• 3068-32-4 1-bromo-1-deoxy-2,3,4,6-tetra-O-acetyl-a-D-galactopyranoside 
• 71-43-2 benzene 
• 3646-73-9 α-D-galactopyranose 
• 572-10-1 2,3,4,6-tetra-O-acetyl-α-D-mannopyranosyl chloride 
• 1144104-32-4 (2,3-di-O-benzyl-4,6-O-benzylidene-α-D-mannopyranosyl) dibenzyl phosphate 
• 81347-80-0 adenosin 5'-(2,3,4,6-tetra-O-acetyl-α-D-glucopyranosyl diphosphate) 
• 10139-18-1 glucosee 1,6-diphosphate 
• 2280-44-6 D-Glucose 
• 952585-00-1 uridine-5'-diphosphoglucose 
• 99-20-7 TREHALOSE 
• 4163-65-9 per-O-acetyl-α-D-mannopyranose 

Downstream Products

• 492-62-6 alpha-D-glucopyranose 
• 2520-52-7 α-D-galactopyranosyl phosphate 
• 50787-09-2 β-Galp-(1->3)-GlcNAc 
• 154235-70-8 guanosine 5’-diphospho-β-L-fucose 
• 991-43-5 guanosine 5'-diphospho-D-mannose 
• 133-89-1 UDP-glucose 
• 18404-72-3 benzyl 4-O-β-D-galactopyranosyl-β-D-glucopyranoside 
• 73448-32-5 4-methylumbelliferyl β-D-galactopyranosyl-(1->4)-2-acetamido-2-deoxy-β-D-glucopyranoside 
• 14034-70-9 α-D-mannopyranosyl (bis(cyclohexylammonium)phosphate) 
• 133-89-1 Uridine diphosphate mannose 
• 19046-60-7 α-D-galactopyranosyl phosphate dipotassium salt 
• 50692-66-5 benzyl-2-acetamido-2-deoxy-3-O-(β-D-galactopyranosyl)-α-D-glucopyranoside 
• 14034-70-9 β-D-glucopyranosyl 
• 50-99-7 D-glucose 

Relevant articles and documents

The role of the active site residues in human galactokinase: Implications for the mechanisms of GHMP kinases

Galactokinase catalyses the phosphorylation of galactose at the expense of ATP. Like other members of the GHMP family of kinases it is postulated to function through an active site base mechanism in which Asp-186 abstracts a proton from galactose. This asparate residue was altered to alanine and to asparagine by site-directed mutagenesis of the corresponding gene. This resulted in variant enzyme with no detectable galactokinase activity. Alteration of Arg-37, which lies adjacent to Asp-186 and is postulated to assist the catalytic base, to lysine resulted in an active enzyme. However, alteration of this residue to glutamate abolished activity. All the variant enzymes, except the arginine to lysine substitution, were structurally unstable (as judged by native gel electrophoresis in the presence of urea) compared to the wild type. This suggests that the lack of activity results from this structural instability, in addition to any direct effects on the catalytic mechanism. Computational estimations of the pKa values of the arginine and aspartate residues, suggest that Arg-37 remains protonated throughout the catalytic cycle whereas Asp-186 has an abnormally high pKa value (7.18). Quantum mechanics/molecular mechanics (QM/MM) calculations suggest that Asp-186 moves closer to the galactose molecule during catalysis. The experimental and theoretical studies presented here argue for a mechanism in which the C 1-OH bond in the sugar is weakened by the presence of Asp-186 thus facilitating nucleophilic attack by the oxygen atom on the γ-phosphorus of ATP.

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.

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.

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Crystallographic studies on two bioisosteric analogues, N-acetyl-β-D-glucopyranosylamine and N-trifluoroacetyl-β-D- glucopyranosylamine, potent inhibitors of muscle glycogen phosphorylase

Structure-based inhibitor design has led to the discovery of a number of potent inhibitors of glycogen phosphorylase b (GPb), N-acyl derivatives of β-d-glucopyranosylamine, that bind at the catalytic site of the enzyme. The first good inhibitor in this class of compounds, N-acetyl-β-d- glucopyranosylamine (NAG) (Ki = 32 μM), has been previously characterized by biochemical, biological and crystallographic experiments at 2.3 A resolution. Bioisosteric replacement of the acetyl group by trifluoroacetyl group resulted in an inhibitor, N-trifluoroacetyl-β-d- glucopyranosylamine (NFAG), with a Ki = 75 μM. To elucidate the structural basis of its reduced potency, we determined the ligand structure in complex with GPb at 1.8 A resolution. To compare the binding mode of N-trifluoroacetyl derivative with that of the lead molecule, we also determined the structure of GPb-NAG complex at a higher resolution (1.9 A). NFAG can be accommodated in the catalytic site of T-state GPb at approximately the same position as that of NAG and stabilize the T-state conformation of the 280s loop by making several favourable contacts to Asn284 of this loop. The difference observed in the Ki values of the two analogues can be interpreted in terms of subtle conformational changes of protein residues and shifts of water molecules in the vicinity of the catalytic site, variations in van der Waals interaction, and desolvation effects.

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.).

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.