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A4394

Sigma-Aldrich

N-Acetyl-D-glucosamine 6-phosphate sodium salt

≥98% (TLC)

Sinónimos:

GlcNAc-6-P Sodium Salt

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About This Item

Fórmula empírica (notación de Hill):
C8H16NO9P · xNa+
Peso molecular:
301.19 (free acid basis)
MDL number:
MFCD00057520
UNSPSC Code:
12352201
PubChem Substance ID:
24890856
NACRES:
NA.25

biological source

natural (inorganic)

Quality Level

200

assay

≥98% (TLC)

form

powder

technique(s)

thin layer chromatography (TLC): suitable

impurities

<10% water (Karl Fischer)

color

white to light yellow

solubility

water: 50 mg/mL, clear, colorless

storage temp.

−20°C

SMILES string

[Na].CC(=O)NC1C(O)OC(COP(O)(O)=O)C(O)C1O

InChI

1S/C8H16NO9P.Na.H/c1-3(10)9-5-7(12)6(11)4(18-8(5)13)2-17-19(14,15)16;;/h4-8,11-13H,2H2,1H3,(H,9,10)(H2,14,15,16);;

InChI key

AILBPHCGSZBCSM-UHFFFAOYSA-N

Categorías relacionadas

Application

N-Acetyl-D-glucosamine 6-phosphate (GlcNAc-6P), an intracellular form of GlcNAc, is a substrate used to identify, differentiate and characterize N-acetyl-D-glucosamine-phosphate deacetylase(s).

Other Notes

To gain a comprehensive understanding of our extensive range of Monosaccharides for your research, we encourage you to visit our Carbohydrates Category page.

pictograms

Exclamation mark
GHS07

signalword

Warning

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

ppe

dust mask type N95 (US), Eyeshields, Gloves

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Tim Miyashiro et al.
Molecular microbiology, 82(4), 894-903 (2011-10-14)
To successfully colonize and persist within a host niche, bacteria must properly regulate their gene expression profiles. The marine bacterium Vibrio fischeri establishes a mutualistic symbiosis within the light organ of the Hawaiian squid, Euprymna scolopes. Here, we show that
Richard S Hall et al.
Biochemistry, 46(27), 7942-7952 (2007-06-15)
NagA is a member of the amidohydrolase superfamily and catalyzes the deacetylation of N-acetyl-d-glucosamine-6-phosphate. The catalytic mechanism of this enzyme was addressed by the characterization of the catalytic properties of metal-substituted derivatives of NagA from Escherichia coli with a variety
Juan Wang et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 62(Pt 11), 1097-1099 (2006-11-02)
Glucosamine-6-phosphate N-acetyltransferase from human liver, which catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to the primary amine of D-glucosamine 6-phosphate to form N-acetyl-D-glucosamine 6-phosphate, was expressed in a soluble form from Escherichia coli strain BL21
Richard S Hall et al.
Biochemistry, 46(27), 7953-7962 (2007-06-15)
NagA catalyzes the hydrolysis of N-acetyl-d-glucosamine-6-phosphate to d-glucosamine-6-phosphate and acetate. X-ray crystal structures of NagA from Escherichia coli were determined to establish the number and ligation scheme for the binding of zinc to the active site and to elucidate the

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