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Merck

54913

Sigma-Aldrich

Lithium β-hydroxypyruvate hydrate

≥97.0% (calc. based on dry substance, NT)

Synonym(s):

β-Hydroxypyruvic acid lithium salt hydrate, 3-Hydroxy-2-oxopropanoic acid lithium salt, 3-Hydroxy-2-oxopropionic acid lithium salt

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About This Item

Linear Formula:
HOCH2COCOOLi · aq
CAS Number:
Molecular Weight:
109.99 (anhydrous basis)
Beilstein:
5774840
MDL number:
UNSPSC Code:
12352100
PubChem Substance ID:
NACRES:
NA.22

Assay

≥97.0% (calc. based on dry substance, NT)

impurities

~1 mol water

functional group

ketone

SMILES string

[Li+].O.OCC(=O)C([O-])=O

InChI

1S/C3H4O4.Li.H2O/c4-1-2(5)3(6)7;;/h4H,1H2,(H,6,7);;1H2/q;+1;/p-1

InChI key

YHTVWBANKNBEKJ-UHFFFAOYSA-M

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Application

  • Chiral polyol synthesis catalyzed by a thermostable Transketolase immobilized on Layered Double Hydroxides in Ionic liquids: Examines the catalytic applications of lithium β-hydroxypyruvate in chiral synthesis processes (Ali et al., 2015).

Other Notes

Substrate for transketolase[1]; Preparation of optically pure L-2-hydroxy aldehydes[2]

Pictograms

Exclamation mark

Signal Word

Warning

Hazard Statements

Hazard Classifications

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

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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F. Effenberger et al.
Tetrahedron Letters, 33, 5157-5157 (1992)
Seong Pil Chung et al.
Journal of biochemistry, 148(6), 743-753 (2010-09-30)
D-amino acid oxidase (DAO) is a flavoenzyme that exists in the kidney, liver and brain of mammals. This enzyme catalyzes the oxidation of D-amino acids to the corresponding α-keto acid, hydrogen peroxide and ammonia. Recently D-serine, one of the substrates
Ronald G Duggleby
Journal of enzyme inhibition and medicinal chemistry, 20(1), 1-4 (2005-05-18)
Acetohydroxyacid synthase (Ec 2.2.1.6) catalyses the thiamine diphosphate-dependent reaction between two molecules of pyruvate yielding 2-acetolactacte and CO2. The enzyme will also utilise hydroxypyruvate with a k(cat) value that is 12% of that observed with pyruvate. When hydroxypyruvate is the
Juhan Kim et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(42), E2856-E2864 (2012-09-18)
Evolution or engineering of novel metabolic pathways can endow microbes with new abilities to degrade anthropogenic pollutants or synthesize valuable chemicals. Most studies of the evolution of new pathways have focused on the origins and quality of function of the
Chen Yang et al.
Journal of bacteriology, 190(5), 1773-1782 (2007-12-25)
Members of a novel glycerate-2-kinase (GK-II) family were tentatively identified in a broad range of species, including eukaryotes and archaea and many bacteria that lack a canonical enzyme of the GarK (GK-I) family. The recently reported three-dimensional structure of GK-II

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