F4004
β-Fluoropyruvic acid sodium salt monohydrate
≥98%
Synonym(s):
sodium 3-fluoro-2-oxopropanoate hydrate
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All Photos(3)
About This Item
Linear Formula:
FCH2COCO2Na · H2O
CAS Number:
Molecular Weight:
146.05
MDL number:
UNSPSC Code:
12352106
PubChem Substance ID:
NACRES:
NA.25
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Quality Level
Assay
≥98%
storage temp.
−20°C
SMILES string
FCC(C([O-])=O)=O.O.[Na+]
InChI
1S/C3H3FO3.Na.H2O/c4-1-2(5)3(6)7;;/h1H2,(H,6,7);;1H2/q;+1;/p-1
InChI key
HDSZBLZMLDQKRW-UHFFFAOYSA-M
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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A Balme et al.
Protein science : a publication of the Protein Society, 3(1), 109-117 (1994-01-01)
The family of FMN-dependent, alpha-hydroxy acid-oxidizing enzymes catalyzes substrate dehydrogenation by a mechanism the first step of which is abstraction of the substrate alpha-proton (so-called carbanion mechanism). For flavocytochrome b2 and lactate oxidase, it was shown that once on the
R R Taylor et al.
FEMS microbiology letters, 115(2-3), 163-167 (1994-01-15)
In contrast to previously studied non-fermentative arginine-hydrolysing (F-/A+) Mycoplasma species, M. gallinarum cells suspended in a salts solution oxidised ethanol and L-lactic, pyruvic and 2-oxobutyric acids. The organic acids were additionally shown effectively to replace arginine as energy sources in
Lisa M Eubanks et al.
Biochemistry, 42(4), 1140-1149 (2003-01-29)
1-Deoxy-d-xylulose 5-phosphate synthase (DXP synthase) catalyzes the thiamine diphosphate (TPP)-dependent condensation of pyruvate and d-glyceraldehyde 3-phosphate (GAP) to yield DXP in the first step of the methylerythritol phosphate pathway for isoprenoid biosynthesis. Steady-state kinetic constants for DXP synthase calculated from
L G Korotchkina et al.
Archives of biochemistry and biophysics, 369(2), 277-287 (1999-09-16)
Pyruvate dehydrogenase (E1), a heterotetramer (alpha(2)beta(2)), is the first catalytic component of the mammalian pyruvate dehydrogenase complex (PDC). To investigate the roles of cysteine-62 of E1alpha (alphaC62) and tryptophan-135 of E1beta (betaW135) (identified previously as active site residues using chemical
S Cheema-Dhadli et al.
Biochemistry and cell biology = Biochimie et biologie cellulaire, 65(5), 458-466 (1987-05-01)
The purpose of these experiments was to examine the factors which regulate ethanol metabolism in vivo. Since the major pathway for ethanol removal requires flux through hepatic alcohol dehydrogenase, the activity of this enzyme was measured and found to be
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