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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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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D S Flournoy et al.
Biochemistry, 25(20), 6036-6043 (1986-10-07)
The pyruvate dehydrogenase component (E1) of the pyruvate dehydrogenase complex catalyzes the decomposition of 3-fluoropyruvate to CO2, fluoride anion, and acetate. Acetylthiamin pyrophosphate (acetyl-TPP) is an intermediate in this reaction. Incubation of the pyruvate dehydrogenase complex with 3-fluoro[1,2-14C]pyruvate, TPP, coenzyme
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
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
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
E B Borthwick et al.
The Biochemical journal, 305 ( Pt 2), 521-524 (1995-01-15)
Simplified procedures for assaying and purifying dihydrodipicolinate synthase (EC 4.2.1.52), the first enzyme of the lysine biosynthetic pathway, have been developed and electrospray ionization m.s. has been used to observe the imine intermediate with pyruvate and to investigate the reaction
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