F4004
β-Fluoropyruvic acid sodium salt monohydrate
≥98%
Sinónimos:
sodium 3-fluoro-2-oxopropanoate hydrate
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About This Item
Fórmula lineal:
FCH2COCO2Na · H2O
Número de CAS:
Peso molecular:
146.05
MDL number:
UNSPSC Code:
12352106
PubChem Substance ID:
NACRES:
NA.25
Productos recomendados
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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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
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
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
A P Yates et al.
The Biochemical journal, 265(1), 283-287 (1990-01-01)
Addition of pyruvate to rat islets perifused in the presence of 5 mM-glucose elicited an immediate pronounced biphasic stimulation of insulin secretion. At lower concentrations of glucose (2.5 mM), only the initial, transient, phase of secretion was observed. Pyruvate inhibited
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