F4004
β-Fluoropyruvic acid sodium salt monohydrate
≥98%
Synonym(s):
sodium 3-fluoro-2-oxopropanoate hydrate
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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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Recommended Products
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
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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D S Flournoy et al.
Biochemistry, 28(25), 9594-9602 (1989-12-12)
The pyruvate dehydrogenase complex (PDH complex) of Escherichia coli and its pyruvate dehydrogenase component (E1) are rapidly inactivated by low concentrations of fluoropyruvate in a thiamin pyrophosphate (TPP) dependent process. The inactivation rates for the PDH complex and for its
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
N Nemeria et al.
Biochemistry, 37(3), 911-922 (1998-02-10)
Variants of the Escherichia coli 1-lip pyruvate dehydrogenase multienzyme complex (1-lip PDHc) with the C259N and C259S substitutions in the putative thiamin diphosphate-(ThDP-) binding motif of the pyruvate dehydrogenase component (E1, EC 1.2.4.1) were characterized. Single substitutions were made at
H Hoving et al.
Biochemistry, 24(22), 6163-6169 (1985-10-22)
The stereochemistry of the transcarboxylase-catalyzed carboxylation of 3-fluoropyruvate has been studied by using fluorine NMR of unpurified reaction mixtures. When the product 3-fluorooxaloacetate was trapped by using malate dehydrogenase, only the 2R,3R diastereomer of 3-fluoromalate was formed. The fluoromethyl group
H Saumweber et al.
European journal of biochemistry, 114(2), 407-411 (1981-02-01)
Free pyruvate dehydrogenase component of the Escherichia coli K12 pyruvate dehydrogenase complex was isolated from a mutant lacking the dihydrolipoamide transacetylase component. The procedure, employing three chromatographic steps, yields a product that is electrophoretically pure. The purified enzyme reassociates with
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