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79470

Sigma-Aldrich

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

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

Synonym(s):

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

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About This Item

Empirical Formula (Hill Notation):
C3H7O7P · xNa+ · yH2O
CAS Number:
Molecular Weight:
186.06 (anhydrous free acid basis)
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.26

Quality Level

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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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 Code

11 - Combustible Solids

WGK

WGK 3

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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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 =
Shivangi Agarwal et al.
Biochimica et biophysica acta, 1784(7-8), 986-994 (2008-05-06)
alpha-enolase of Bacillus anthracis has recently been classified as an immunodominant antigen and a potent virulence factor determinant. alpha-enolase (2-phospho-d-glycerate hydrolase (EC 4.2.1.11), a key glycolytic metalloenzyme catalyzes the dehydration of d-(+)-2-phosphoglyceric acid to phosphoenolpyruvate. Interaction of surface bound alpha-enolase
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
Molecular characterization of phosphoglycerate mutase in archaea.
van der Oost J, et al.
FEMS Microbiology Letters, 212, 111-120 (2002)
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

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