119736-88-8

Basic information

• Product Name: L-Homoserine
• Synonyms: L-Homoserine;(2S)-2-Amino-4-hydroxybutyric acid;(S)-2-Amino-4-hydroxybutanoic acid
• CAS NO: 119736-88-8
• Molecular Formula: C4H9NO3
• Molecular Weight: 119.12
• Mol File: 119736-88-8.mol
• Article Data: 62

Chemical Properties

• Boiling Point: 368.7 °C at 760 mmHg
• Flash Point: 176.8 °C
• Appearance: /
• Density: 1.312 g/cm³
• CAS DataBase Reference: L-Homoserine(CAS DataBase Reference)
• NIST Chemistry Reference: L-Homoserine(119736-88-8)
• EPA Substance Registry System: L-Homoserine(119736-88-8)

Safety Data

• Hazardous Substances Data: 119736-88-8(Hazardous Substances Data)

Usage

General Description

L-Homoserine is a non-proteinogenic amino acid and a precursor in the biosynthesis of several essential compounds in the body. It is an intermediate in the metabolic pathway that leads to the production of threonine and methionine, two amino acids critical for protein synthesis and other biochemical processes. L-Homoserine is also a key molecule in the biosynthesis of the antibiotic penicillin, as well as in the formation of various secondary metabolites in microorganisms. In addition to its role in protein and antibiotic production, L-Homoserine has been studied for its potential therapeutic applications in treating neurodegenerative diseases and cancer, as well as in developing new strategies for drug delivery and targeting specific cells and tissues.

Upstream product

• 3157-50-4 2-amino-4-chlorobutyric acid 
• 90918-62-0 4-hydroxy-2-phenylhydrazono-butyric acid 
• 2185-02-6 L-homoserine lactone 
• 104347-13-9 (R)-(+)-α-amino-γ-butyrolactone hydrochloride 
• 51744-82-2 D-homoserine lactone 
• 6305-38-0 α-amino-γ-butyrolactone hydrobromide 
• 3493-11-6 (3S)-(3-amino-3-carboxypropyl)dimethylsulfonium iodide 
• 76224-57-2 avenic acid A 
• 29625-73-8 2-acetamido-4-O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-1-N-(4-L-aspartoyl)-2-deoxy-β-D-glucopyranosylamine 
• 76338-90-4 α-amino-γ-bromobutyric acid hydrobromide 
• 50992-08-0 2-(N,N-dibenzylamino)-4-hydroxybutyric acid lactone 
• 52161-80-5 2-amino-4-phenoxybutanoic acid 
• 50-00-0 formaldehyd 
• 56-41-7 L-alanin 

Downstream Products

• 15159-65-6 (2S)-2-amino-4-bromobutanoic acid hydrobromide 
• 745011-75-0 (R)-2-((tert-butoxycarbonyl)amino)-4-hydroxybutanoic acid 
• 672-15-1 L-homoserine 
• 6893-26-1 D-Glutamic acid 
• 6027-21-0 D-homoserine 
• 56-86-0 L-glutamic acid 
• 109-78-4 3-Hydroxypropionitrile 
• 15920-74-8 N-Formyl-homoserin-cyclohexylamid 
• 58611-62-4 benzyl DL-N-(benzyloxycarbonyl)homoserinate 
• 5746-78-1 N-Carbamoyl-homoserin 
• 38308-92-8 2-(tert-butoxycarbonylamino)-4-hydroxy-butanoic acid 
• 38308-93-9 2-tert-butoxycarbonylamino-4-hydroxy-butyric acid benzyl ester 
• 4096-48-4 O-oxalylhomoserine 
• 41088-87-3 N-benzoyl-L-homoserine 

Relevant articles and documents

Ds-ERYTHRO-2-AMINO-4-ETHOXY-3-HYDROXYBUTANOIC ACID FROM THE FRUITING BODIES OF THE EDIBLE MUSHROOM, LYOPHYLLUM ULMARIUM

A new β-hydroxy amino acid isolated from the fruiting bodies of Lyophyllum ulmarium was identified as Ds-erythro-2-amino-4-ethoxy-3-hydroxybutanoic acid by chemical degradation and spectroscopic analyses. Key Word Index - Lyophyllum ulmarium; Tricholomataceae; mushroom; amino acid; Ds-erythro-2-amino-4-ethoxy-3-hydroxybutanoic acid.

Large-scale, protection-free synthesis of Se-adenosyl-l-selenomethionine analogues and their application as cofactor surrogates of methyltransferases

S-Adenosyl-l-methionine (SAM) analogues have previously demonstrated their utility as chemical reporters of methyltransferases. Here we describe the facile, large-scale synthesis of Se-alkyl Se-adenosyl-l-selenomethionine (SeAM) analogues and their precursor, Se-adenosyl-l-selenohomocysteine (SeAH). Comparison of SeAM analogues with their equivalent SAM analogues suggests that sulfonium-to-selenonium substitution can enhance their compatibility with certain protein methyltransferases, favoring otherwise less reactive SAM analogues. Ready access to SeAH therefore enables further application of SeAM analogues as chemical reporters of diverse methyltransferases.

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Radiation chemical studies of methionine in aqueous solution: Understanding the role of molecular oxygen

The oxidation of methionine is an important reaction in the biological milieu. Despite a few decades of intense studies, several fundamental aspects remain to be defined. We have investigated in detail the γ-radiolysis of free methionine in the absence and presence of molecular oxygen followed by product characterization and quantification. The primary site of attack by HO? radicals and H? atoms is the sulfur atom of methionine. We have disclosed that HO? radicals do not oxidize methionine to the corresponding sulfoxide in either the presence or the absence of oxygen; the oxidizing species is H2O2 derived either from the radiolysis of water or from the disproportionation of the byproduct O2?-. 3-Methylthiopropionaldehyde is the major product of HO? radical attack in the presence of molecular oxygen. Together with the direct oxidation at sulfur as the major product, the potential of H? atoms is also proven to be highly specific for sulfur atom attack under anoxic and aerobic conditions. The major products derived from the H? atoms attack are found to be α-aminobutyric acid or homoserine, in the absence or presence of oxygen, respectively. All together, these results help clarify the fate of methionine related to a biological environment and offer a molecular basis for envisaging other possible pathways of in vivo degradation as well as other markers.

Synthesis of L-(+)-selenomethionine

A novel three-pot synthesis of L-(+)-selenomethionine suitable for small and large scale preparations is presented. The method gives high optical purity and avoids evil smelling selenium species.

Structure of the O-antigen of Acinetobacter lwoffii EK30A; Identification of d-homoserine, a novel non-sugar component of bacterial polysaccharides

We established a peculiar structure of the O-specific polysaccharide (O-antigen) of a psychrotrophic strain of Acinetobacter lwoffii, EK30A, isolated from a 1.6-1.8 million-year-old Siberian permafrost subsoil sediment sample. The polysaccharide was released by mild acid degradation of the lipopolysaccharide and studied using chemical analyses, Smith degradation, 1H and 13C NMR spectroscopy and mass spectrometry. It was found to contain d-homoserine, which is N-linked to 4-amino-4,6-dideoxy-d- glucose (Qui4N) and is N-acylated itself with acetyl in about half of the repeating units or (S)-3-hydroxybutanoyl group in the other half. The following is the structure of the tetrasaccharide repeating unit of the polysaccharide: →3)-β-d-Quip4NAcyl-(1→6)-α-d-Galp-(1→4) -α-d-GalpNAc-(1→3)-α-d-FucpNAc-(1→ where Acyl stands for either N-acetyl- or N-[(S)-3-hydroxybutanoyl]-d-homoseryl. The Royal Society of Chemistry 2010.

Deracemization of amino acids by coupling transaminases of opposite stereoselectivity

Biocatalytic deracemization of amino acids without relying on oxidase-based deamination of an unwanted enantiomer was demonstrated by coupling a-and w-transaminases displaying opposite stereoselectivity. This strategy employs isopropylamine and a keto acid as cosubstrates and is free of generation of hydrogen peroxide which is troublesome in the conventional oxidase-based methods.

Combining Aldolases and Transaminases for the Synthesis of 2-Amino-4-hydroxybutanoic Acid

Amino acids are of paramount importance as chiral building blocks of life, for drug development in modern medicinal chemistry, and for the manufacture of industrial products. In this work, the stereoselective synthesis of (S)- and (R)-2-amino-4-hydroxybutanoic acid was accomplished using a systems biocatalysis approach comprising a biocatalytic one-pot cyclic cascade by coupling of an aldol reaction with an ensuing stereoselective transamination. A class II pyruvate aldolase from E. coli, expressed as a soluble fusion protein, in tandem with either an S- or R-selective, pyridoxal phosphate dependent transaminase was used as a catalyst to realize the conversion, with formaldehyde and alanine being the sole starting materials. Interestingly, the class II pyruvate aldolase was found to tolerate formaldehyde concentrations of up to 1.4 M. The cascade system was found to reach product concentrations for (S)- or (R)-2-amino-4-hydroxybutanoic acid of at least 0.4 M, rendering yields between 86% and >95%, respectively, productivities of >80 g L-1 d-1, and ee values of >99%.

Synthesis of fluorinated analogues of sphingosine-1-phosphate antagonists as potential radiotracers for molecular imaging using positron emission tomography

Sphingosine-1-phosphate (S1P) receptors play major roles in cardiovascular, immunological and neurological diseases. The recent approval of the sphingolipid drug Fingolimod (Gilenya), a sphingosine-1-phosphate agonist for relapsing multiple sclerosis, in 2010 exemplifies the potential for targeting sphingolipids for the treatment of human disorders. Moreover, non-invasive in vivo imaging of S1P receptors that are not available till now would contribute to the understanding of their role in specific pathologies and is therefore of preclinical interest. Based on fluorinated analogues of the S1P1receptor antagonist W146 showing practically equal in vitro potency as the lead structure, the first S1P receptor antagonist [18F]-radiotracer has been synthesized and tested for in vivo imaging of the S1P1receptor using positron emission tomography (PET). Though the tracer is serum stable, initial in vivo images show fast metabolism and subsequent accumulation of free [18F]fluoride in the bones.

Synthesis and delivery of a stable phosphorylated ubiquitin probe to study ubiquitin conjugation in mitophagy

Protein post-translational modifications are involved in essentially all aspects of cellular signaling. Their dynamic nature and the difficulties in installing them using enzymatic approaches limits their direct study in human cells. Reported herein is the first synthesis, delivery and cellular study of a stable phosphoubiquitin probe. Our results compare Parkin's substrate preference during mitophagyviadirect visualization of a phosphorylated ubiquitin probe in the cellular environment.

Design, synthesis, and evaluation of compounds capable of reducing Pseudomonas aeruginosa virulence

Anti-virulence approaches in the treatment of Pseudomonas aeruginosa (PA)-induced infections have shown clinical potential in multiple in vitro and in vivo studies. However, development of these compounds is limited by several factors, including the lack of molecules capable of penetrating the membrane of gram-negative organisms. Here, we report the identification of novel structurally diverse compounds that inhibit PqsR and LasR-based signaling and diminish virulence factor production and biofilm growth in two clinically relevant strains of P. aeruginosa. It is the first report where potential anti-virulent agents were evaluated for inhibition of several virulence factors of PA. Finally, co-treatment with these inhibitors significantly reduced the production of virulence factors induced by the presence of sub-inhibitory levels of ciprofloxacin. Further, we have analyzed the drug-likeness profile of designed compounds using quantitative estimates of drug-likeness (QED) and confirmed their potential as hit molecules for further development.

Identification of 2, 3-dihydrodipicolinate as the product of the dihydrodipicolinate synthase reaction from Escherichia coli

Dihydrodipicolinate synthase (DHDPS) catalyzes the first step in the pathway for the biosynthesis of L-lysine in most bacteria and plants. The substrates for the enzyme are pyruvate and L-aspartate-β-semialdehyde (ASA). The product of the reaction was originally proposed to be 2,3-dihydrodipicolinate (DHDP), but has now generally been assumed to be (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate (HTPA). ASA is unstable at high pH and it is proposed that ASA reacts with itself. At high pH ASA also reacts with Tris buffer and both reactions are largely reversible at low pH. It is proposed that the basic un-protonated form of the amine of Tris or the α-amine of ASA reacts with the aldehyde functional group of ASA to generate an imine product. Proton NMR spectra of ASA done at different pH values shows new NMR peaks at high pH, but not at low pH, confirming the presence of reaction products for ASA at high pH. The enzymatic product of the DHDPS reaction was examined at low pH by proton NMR starting with either 3 h-pyruvate or 3 d-pyruvate and identical NMR spectra were obtained with four new NMR peaks observed at 1.5, 2.3, 3.9 and 4.1 ppm in both cases. The NMR results were most consistent with DHDP as the reaction product. The UV-spectral studies of the DHDPS reaction shows the formation of an initial product with a broad spectral peak at 254 nM. The DHDPS reaction product was further examined by reduction of the enzymatic reaction components with borohydride followed by GC-MS analysis of the mixture. Three peaks were found at 88, 119 and 169 m/z, consistent with pyruvate, homoserine (reduction product of ASA), and the reduction product of DHDP (1,2,3,6-tetrahydropyridine-2,6-dicarboxylate). There was no indication for a peak associated with the reduced form of HTPA.