433-48-7

Usage

Uses

Used in Chemical Synthesis:
3-Fluoropyruvate is used as a building block for the synthesis of various organic compounds. Its unique fluoro substituent allows for the creation of a wide range of molecules with different properties and applications.
Used in Pharmaceutical Industry:
3-Fluoropyruvate is used as a mechanistic agent for the inactivation of mandelate racemase, an enzyme involved in the bacterial degradation of aromatic compounds. This property makes it a potential candidate for the development of new antibiotics or other therapeutic agents targeting bacterial infections.
Used in Biochemical Research:
3-Fluoropyruvate is used as a research tool to study the effects of fluorination on the structure and function of pyruvic acid and its derivatives. This can provide valuable insights into the role of fluorine in biological systems and help in the design of new drugs and bioactive molecules.

InChI:InChI=1/C3H3FO3/c4-1-2(5)3(6)7/h1H2,(H,6,7)/p-1

Upstream product

• 392-58-5 Diethyl fluoroxaloacetate 
• 16652-37-2 3-fluoroalanine 

Downstream Products

• 399-87-1 fluoro-pyruvic acid methyl ester 
• 401-48-9 Fluoropyruvic acid Semicarbazone 
• 51033-95-5 3-ethylthio-2-oxopropanoic acid 
• 16652-37-2 3-fluoroalanine 
• 35455-20-0 (S)-3-fluoroalanine 
• 35523-45-6 α-2H-β-19F-D-alanine 
• 127-17-3 2-oxo-propionic acid 
• 35455-21-1 (R)-3-fluoroalanine 

Relevant academic research and scientific papers

Kinetic resolution of 3-fluoroalanine using a fusion protein of D-amino acid oxidase with Vitroscilla hemoglobin

In this study, a fusion protein (VHb-DAAO) of D-amino acid oxidase (DAAO) with Vitreoscilla hemoglobin (VHb) was functionally expressed in Escherichia coli and purified. The kcat value VHb-DAAO (47.1 s-1) towards rac-3-flouroalanine was about 2-fold higher than that of DAAO (21.9 s -1). rac-3-Flouroalanine (500 mm) was kinetically resolved into (R)-3-fluoroalanine with high enatiomeric excess (>99%) by VHb-DAAO with about 52% conversion.

Thermodynamics and kinetic aspects involved in the enzymatic resolution of (R,S)-3-fluoroalanine in a coupled system of redox reactions catalyzed by dehydrogenases

Two systems of redox enzymatic reactions were tested, looking forward to the preparation of (S)-3-fluoroalanine, a potent antibiotic, by kinetic resolution of rac-3-fluoroalanine. This starting material was the main substrate for the deaminative oxidation reaction catalyzed by L-alanine dehydrogenase (L-AlaDH) in the presence of NAD+. One system was formed by coupling this reaction (main reaction) to the reduction of 3-fluoropyruvate (a cascade system) produced in the main reaction catalyzed by L-lactate dehydrogenase (L-LDH) in the presence of NADH, also formed in the main reaction. This system, that was able to achieve 92% of conversion, allows the accumulation of NH 4+, one of the secondary products of the main reaction. The other coupled redox system involved the coupling to the L-AlaDH reaction to the aminative reduction reaction of α-ketoglutarate in the presence of NADH and NH4+ (both side products of the main reaction) catalyzed by L-glutamate dehydrogenase (L-GluDH), that allows accumulation of 3-fluoropyruvate. With this system, the extent of the reaction in the coupled system was only 22%. This big difference in the efficiency of both systems was identified as being the result of a different potency of the products that accumulates in both systems, acting as inhibitors of L-AlaDH. It was demonstrated that 3-fluoropyruvate is a much stronger inhibitor of L-AlaDH than NH4+. This fact, and not thermodynamic considerations, explains the results obtained with both systems.