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About This Item
Linear Formula:
HOCH2COCOOLi · aq
CAS Number:
Molecular Weight:
109.99 (anhydrous basis)
UNSPSC Code:
12352100
NACRES:
NA.22
PubChem Substance ID:
MDL number:
Beilstein/REAXYS Number:
5774840
Assay:
≥97.0% (calc. based on dry substance, NT)
InChI
1S/C3H4O4.Li.H2O/c4-1-2(5)3(6)7;;/h4H,1H2,(H,6,7);;1H2/q;+1;/p-1
SMILES string
[Li+].O.OCC(=O)C([O-])=O
InChI key
YHTVWBANKNBEKJ-UHFFFAOYSA-M
assay
≥97.0% (calc. based on dry substance, NT)
impurities
~1 mol water
functional group
ketone
Quality Level
Related Categories
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; Preparation of optically pure L-2-hydroxy aldehydes
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Gloves
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F. Effenberger et al.
Tetrahedron Letters, 33, 5157-5157 (1992)
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
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
Renwick C J Dobson et al.
Protein science : a publication of the Protein Society, 17(12), 2080-2090 (2008-09-13)
In recent years, dihydrodipicolinate synthase (DHDPS, E.C. 4.2.1.52) has received considerable attention from a mechanistic and structural viewpoint. DHDPS catalyzes the reaction of (S)-aspartate-beta-semialdehyde with pyruvate, which is bound via a Schiff base to a conserved active-site lysine (Lys161 in
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