89426-34-6

Basic information

• Product Name: 4-FLUORO-L-THREONINE
• Synonyms: 4-FLUORO-L-THREONINE
• CAS NO: 89426-34-6
• Molecular Formula: C₄H₈FNO₃
• Molecular Weight: 137.11
• Mol File: 89426-34-6.mol
• Article Data: 6

Chemical Properties

• Boiling Point: 388.9 °C at 760 mmHg
• Flash Point: 189 °C
• Appearance: /
• Density: 1.419 g/cm³
• CAS DataBase Reference: 4-FLUORO-L-THREONINE(CAS DataBase Reference)
• NIST Chemistry Reference: 4-FLUORO-L-THREONINE(89426-34-6)
• EPA Substance Registry System: 4-FLUORO-L-THREONINE(89426-34-6)

Safety Data

• Hazardous Substances Data: 89426-34-6(Hazardous Substances Data)

Usage

General Description

4-Fluoro-L-threonine is a synthetic fluorinated amino acid with a similar structure to the natural amino acid L-threonine. It is a non-proteinogenic amino acid, meaning it is not normally found in proteins but can be incorporated into them through genetic engineering. 4-Fluoro-L-threonine has been studied for its potential use in the development of fluorinated analogs of proteinogenic amino acids, which may have applications in drug development and in studying protein-protein interactions. It is also used as a tool in studying the structure and function of proteins, and in understanding the role of specific amino acids in biological processes. Additionally, 4-Fluoro-L-threonine has been investigated for its potential as a building block in the synthesis of peptidomimetics and other bioactive compounds.

Upstream product

• 72-19-5 L-threonine 
• 1544-46-3 2-fluoroacetaldehyde 
• 731-98-6 5’-fluoro-5’-deoxyadenosine 
• 14031-35-7 S-Adenosyl-L-methionine 
• 102608-41-3 t-butyl (4S),(5S)-5-fluoromethyl-2-oxo-4-oxazolidinecarboxylate 
• 194666-37-0 Benzoic acid (S)-1-((2R,4S)-2-tert-butyl-1-methyl-5-oxo-imidazolidin-4-yl)-2-fluoro-ethyl ester 

Downstream Products

• 1019-57-4 acetaldehyde 2,4-dinitrophenylhydrazine 
• 17610-81-0 2-Oxobutyric acid 2,4-Dinitrophenylhydrazone 
• 365-69-5 2-fluoroacetaldehyde 2,4-dinitrophenylhydrazone 

Relevant articles and documents

Defluorination of 4-fluorothreonine by threonine deaminase

4-Fluorothreonine (4-FT) is the only naturally occurring fluorinated amino acid antibiotic. Although two conserved proteins in the 4-FT pathway have been found to be involved in self-detoxification mechanisms, the 4-FT-producing strains may also require an alternative pathway to degrade the intracellular 4-FT. In this study, we examined the possible degradation role of three enzymes involved in threonine metabolite pathways toward 4-FT as a possible degradation route to avoid in vivo 4-FT accumulation. Among these three enzymes, threonine deaminase was found to catalyse a defluorination reaction to generate 4-hydroxy-α-ketobutyrate, which is supposed to be further metabolised by an aldolase that likely is a unique occurrence in the 4-FT-producing strains. Our finding may constitute a 4-FT degradation pathway as a complementary resistance mechanism.

Amalgamation of nucleosides and amino acids in antibiotic biosynthesis: Discovery of an l -threonine: Uridine-5′-aldehyde transaldolase

The lipopeptidyl nucleoside antibiotics represented by A-90289, caprazamycin, and muraymycin are structurally highlighted by a nucleoside core that contains a nonproteinogenic β-hydroxy-α-amino acid named 5′-C-glycyluridine (GlyU). Bioinformatic analysis of the biosynthetic gene clusters revealed a shared open reading frame encoding a protein with sequence similarity to serine hydroxymethyltransferases, resulting in the proposal that this shared enzyme catalyzes an aldol-type condensation with glycine and uridine-5′-aldehyde to furnish GlyU. Using LipK involved in A-90289 biosynthesis as a model, we now functionally assign and characterize the enzyme responsible for the C-C bond-forming event during GlyU biosynthesis as an l-threonine:uridine-5′-aldehyde transaldolase. Biochemical analysis revealed this transformation is dependent upon pyridoxal-5′-phosphate, the enzyme has no activity with alternative amino acids, such as glycine or serine, as aldol donors, and acetaldehyde is a coproduct. Structural characterization of the enzyme product is consistent with stereochemical assignment as the threo diastereomer (5′S,6′S)-GlyU. Thus this enzyme orchestrates C-C bond breaking and formation with concomitant installation of two stereocenters to make a new l-α-amino acid with a nucleoside side chain.

A short highly stereoselective synthesis of the fluorinated natural product (2S,3S )-4-fluorothreonine

A three step stereoselective route to the fluorinated natural product (2S,3S)-4-fluorothreonine is described; the route is amenable to the preparation of (2S,3S)-4-fluoro[3-2H]threonine and (2S,3R)-[4,4,4-2H3]threonine.