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G6893

Sigma-Aldrich

α-D-Glucose 1,6-bisphosphate potassium salt hydrate

synthetic, ≥98% (TLC)

Synonym(s):

α-D-Glucose 1,6-diphosphate potassium salt hydrate

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About This Item

Empirical Formula (Hill Notation):
C6H10K4O12P2 · xH2O
CAS Number:
Molecular Weight:
492.48 (anhydrous basis)
MDL number:
UNSPSC Code:
12352201
PubChem Substance ID:
NACRES:
NA.25

biological source

synthetic

assay

≥98% (TLC)

form

powder or crystals

color

white

solubility

water: 50 mg/mL, clear, colorless (OECD Test Guideline 105)

cation traces

K: 28.5-33.5% (ICP)

storage temp.

−20°C

SMILES string

[K+].[K+].[K+].[K+].O[C@H]1[C@H](O)[C@@H](COP([O-])([O-])=O)O[C@H](OP([O-])([O-])=O)[C@@H]1O

InChI

1S/C6H14O12P2.4K/c7-3-2(1-16-19(10,11)12)17-6(5(9)4(3)8)18-20(13,14)15;;;;/h2-9H,1H2,(H2,10,11,12)(H2,13,14,15);;;;/q;4*+1/p-4/t2-,3-,4+,5-,6-;;;;/m1..../s1

InChI key

OVRXVCAVDXBPQT-QMKHLHGBSA-J

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General description

α-D-Glucose 1,6-bisphosphate was found to be at a concentration of between 10 μm and 600 μm in various tissues including liver, brain and kidney.

Application

α-D-Glucose 1,6-bisphosphate is used in the identification, differentiation and characterization of α-phosphoglucomutase(s), β-phosphoglucomutase(s) and α- and β-hexoglucomutase(s).

Biochem/physiol Actions

Metabolite formed via the activity of Glucose-1,6-biphosphate synthase. Glucose-1,6-biphosphate (G-1,6-BP) acts as an inhibitor of hexokinase function and an activator of phosphofructokinase-1 and pyruvate kinase. G-1,6-BP also acts as a coenzyme for phosphoglucomutate and a cofactor for phosphopentomutase.

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.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

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A kinetic study of the isozymes determined by the three human phosphoglucomutase loci PGM1, PGM2, and PGM3.
C B Quick et al.
European journal of biochemistry, 42(2), 511-517 (1974-03-01)

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