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Merck
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79470

Sigma-Aldrich

D(+)-2-Phosphoglyceric acid sodium salt hydrate

≥75% (calc. on dry substance, enzymatic)

Sinónimos:

D-Glycerate 2-phosphate sodium salt, Sodium D-2-phosphoglycerate hydrate

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About This Item

Fórmula empírica (notación de Hill):
C3H7O7P · xNa+ · yH2O
Número de CAS:
83418-48-8
Peso molecular:
186.06 (anhydrous free acid basis)
UNSPSC Code:
12352204
PubChem Substance ID:
329768458
NACRES:
NA.26

assay

≥75% (calc. on dry substance, enzymatic)

form

powder

impurities

≤1% Pi
≤35% water

storage temp.

−20°C

SMILES string

O=C(O)[C@@H](CO)OP(O)(O)=O.C.C

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Categorías relacionadas

Biochem/physiol Actions

The enzyme enolase is responsible for reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP). Phosphoglycerate mutase causes reversible isomerization of 3-phosphoglycerate and 2-phosphoglycerate in glycolysis and gluconeogenesis.
Enantiomerically pure metabolite of glycolysis/gluconeogenesis and also substrate for a number of important enzymes in central metabolism like enolase and phosphoglycerate mutase.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

ppe

Eyeshields, Gloves, type N95 (US)

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T M Larsen et al.
Biochemistry, 35(14), 4349-4358 (1996-04-09)
The equilibrium mixture of yeast enolase with substrate, 2-phospho-D-glycerate (2-PGA), and product, phosphoenolpyruvate (P-enolpyruvate), has been crystallized from solutions of poly(ethylene glycol) (PEG) at pH 8.0. Crystals belong to the space group C2 and have unit cell dimensions a =
Molecular characterization of phosphoglycerate mutase in archaea.
van der Oost J, et al.
FEMS Microbiology Letters, 212, 111-120 (2002)
Jin-Ha Lee et al.
FEMS microbiology letters, 259(2), 240-248 (2006-06-01)
Enolase on the surface of streptococci putatively facilitates pathogenic invasion of the host organisms. The related Leuconostoc mesenteroides 512FMCM is nonpathogenic, but it too has an extracellular enolase. Purified isolates of extracellular dextransucrase from cultures of L. mesenteroides contain minute
Grégory Boël et al.
Journal of molecular biology, 337(2), 485-496 (2004-03-09)
We observed that in vivo and in vitro a small fraction of the glycolytic enzyme enolase became covalently modified by its substrate 2-phosphoglycerate (2-PG). In modified Escherichia coli enolase, 2-PG was bound to Lys341, which is located in the active
E Zhang et al.
Biochemistry, 36(41), 12526-12534 (1997-11-05)
Enolase, a glycolytic enzyme that catalyzes the dehydration of 2-phospho-d-glycerate (PGA) to form phosphoenolpyruvate (PEP), is a homodimer in all eukaryotes and many prokaryotes. Here, we report the crystal structure of a complex between yeast enolase and an equilibrium mixture
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