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F4004

Sigma-Aldrich

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

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


Certificates of Analysis (COA)

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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
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
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
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

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