2152-75-2

Basic information

• Product Name: ALPHA-D-GLUCOSAMINE 1-PHOSPHATE
• Synonyms: ALPHA-D-GLUCOSAMINE 1-PHOSPHATE;A-D-glucosamine 1-phosphate free acid;α-d-glucosamine 1-phosphate;glucosamine 1-phosphate;alpha-D-glucosamine phosphate;[(2R,3R,4R,5S,6R)-3-amino-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl] dihydrogen phosphate;[(2R,3R,4R,5S,6R)-3-amino-4,5-dihydroxy-6-methylol-tetrahydropyran-2-yl] dihydrogen phosphate;[(2R,3R,4R,5S,6R)-3-azanyl-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl] dihydrogen phosphate
• CAS NO: 2152-75-2
• Molecular Formula: C6H14NO8P
• Molecular Weight: 259.15
• Product Categories: Carbohydrates;Carbohydrates A to;Carbohydrates GBiochemicals and Reagents;Monosaccharide;Carbohydrates & Derivatives;Intermediates & Fine Chemicals;Pharmaceuticals;Phosphorylating and Phosphitylating Agents
• Mol File: 2152-75-2.mol
• Article Data: 9

Chemical Properties

• Boiling Point: 596°Cat760mmHg
• Flash Point: 314.3°C
• Appearance: /
• Density: 1.81g/cm³
• Vapor Pressure: 1.09E-16mmHg at 25°C
• Refractive Index: 1.605
• Storage Temp.: −20°C
• Solubility: Water (Sparingly),
• PKA: 1.73±0.10(Predicted)
• Stability: Hygroscopic
• CAS DataBase Reference: ALPHA-D-GLUCOSAMINE 1-PHOSPHATE(CAS DataBase Reference)
• NIST Chemistry Reference: ALPHA-D-GLUCOSAMINE 1-PHOSPHATE(2152-75-2)
• EPA Substance Registry System: ALPHA-D-GLUCOSAMINE 1-PHOSPHATE(2152-75-2)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 2152-75-2(Hazardous Substances Data)

Usage

Uses

Different sources of media describe the Uses of 2152-75-2 differently. You can refer to the following data:
1. ALPHA-D-GLUCOSAMINE 1-PHOSPHATE is a phosphorylated glucosamine used in the enzymatic α-glucosaminylation of maltooligosaccharides catalyzed by phosphorylase.
2. A phosphorylated glucosamine used in the enzymatic α-glucosaminylation of maltooligosaccharides catalyzed by phosphorylase.

InChI:InChI=1/C6H14NO8P/c7-3-5(10)4(9)2(1-8)14-6(3)15-16(11,12)13/h2-6,8-10H,1,7H2,(H2,11,12,13)/t2-,3-,4-,5-,6-/m1/s1

Upstream product

• 79781-69-4 2-azido-3,4,6-tri-O-benzyl-2-deoxy-D-galactopyranose 
• 90-76-6 D-galactosamine 
• 1334525-86-8 2-azido-2-deoxy-D-glucopyranose-1-(dihydrogen phosphate) 
• 1355005-35-4 2-azido-2-deoxy-D-glucopyranose-3,4,6-triacetate-1-(dihydrogen phosphate) 
• 171032-74-9 1,3,4,6-tetra-O-acetyl-2-azido-2-deoxy-D-glucopyranose 
• 1078691-95-8 (+)-D-glucosamine hydrochloride 
• 66-84-2 D-(+)-glucosamine hydrochloride 
• 884856-12-6 (2-azido-3,4,6-tri-O-benzyl-2-deoxy-α-D-glucpyranosyl) dibenzyl phosphate 
• 79184-08-0 3,4,6-tri-O-acetyl-2-acetamido-1-O-[bis(benzyloxy)phophoryl]-2-deoxy-α-D-glucopyranose 
• 35946-68-0 O³,O⁴,O⁶-triacetyl-2-amino-O¹-diphenoxyphosphoryl-2-deoxy-α-D-glucopyranose; hydrochloride 
• 6665-06-1 D-glucosamine-6-phosphate 

Downstream Products

• 16503-17-6 [13C]-N-acetylglucosamine-1-phosphate 
• 92283-18-6 3,4,6-tri-O-acetyl-2-acetamido-2-deoxy-α-D-galactopyranosyl dihydrogen phosphate 
• 17479-06-0 uridine 5'-(2-amino-2-deoxy-α-D-galactopyranosyl diphosphate) 
• 1109-79-1 uridine 5'-(2-amino-2-deoxy-α-D-glucopyranosyl)-diphosphate 
• 528-04-1 uridine-5'-diphospho-N-acetyl-D-galactosamine 
• 28446-21-1 N-acetylglucosamine-1-phosphate 
• 528-04-1 uridine 5'-diphospho-N-acetylglucosamine 

Relevant articles and documents

Allosteric Modulation of the Faecalibacterium prausnitzii Hepatitis Delta Virus-like Ribozyme by Glucosamine 6-Phosphate: The Substrate of the Adjacent Gene Product

Self-cleaving ribozymes were discovered 30 years ago and have been found throughout nature, from bacteria to animals, but little is known about their biological functions and regulation, particularly how cofactors and metabolites alter their activity. A hepatitis delta virus-like self-cleaving ribozyme maps upstream of a phosphoglucosamine mutase (glmM) open reading frame in the genome of the human gut bacterium Faecalibacterium prausnitzii. The presence of a ribozyme in the untranslated region of glmM suggests a regulation mechanism of gene expression. In the bacterial hexosamine biosynthesis pathway, the enzyme glmM catalyzes the isomerization of glucosamine 6-phosphate into glucosamine 1-phosphate. In this study, we investigated the effect of these metabolites on the co-transcriptional self-cleavage rate of the ribozyme. Our results suggest that glucosamine 6-phosphate, but not glucosamine 1-phosphate, is an allosteric ligand that increases the self-cleavage rate of drz-Fpra-1, providing the first known example of allosteric modulation of a self-cleaving ribozyme by the substrate of the adjacent gene product. Given that the ribozyme is activated by the glmM substrate, but not the product, this allosteric modulation may represent a potential feed-forward mechanism of gene expression regulation in bacteria.

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.

Artificial N-functionalized UDP-glucosamine analogues as modified substrates for N-acetylglucosaminyl transferases

Analogues of UDP-GlcNAc modified at the 2-acetamido group of the GlcNAc moiety were prepared in order to study their role in the mechanism of N-acetylglucosaminyl transferase mediated glycosylation reactions. The structural analogues with N-formyl-, N-pro