1927-25-9

Basic information

• Product Name: DL-Homoserine
• Synonyms: DL-HoMoser;(RS)-2-Amino-4-hydroxybutyric acid;DL-Homoserine≥98% (HPLC);DL-HomoSer-OH;(+/-)-2-AMINO-4-HYDROXYBUTYRIC ACID;2-AMINO-4-HYDROXYBUTYRIC ACID;DL-HOMOSERINE;DL-2-AMINO-4-HYDROXYBUTYRIC ACID
• CAS NO: 1927-25-9
• Molecular Formula: C₄H₉NO₃
• Molecular Weight: 119.12
• EINECS: 217-661-8
• Product Categories: NULL;Serine [Ser, S];Amino Acids 13C, 2H, 15N;Amino Acids & Derivatives
• Mol File: 1927-25-9.mol

Chemical Properties

• Melting Point: 188-189 °C
• Boiling Point: 222.38°C (rough estimate)
• Flash Point: 176.8 °C
• Appearance: White/Fine Crystalline Powder or Needles
• Density: 1.3126 (rough estimate)
• Vapor Pressure: 6.16E-07mmHg at 25°C
• Refractive Index: 1.4183 (estimate)
• Storage Temp.: Store at RT.
• Solubility: Water (Sparingly)
• PKA: 2.21±0.10(Predicted)
• Water Solubility: soluble
• Merck: 14,4739
• CAS DataBase Reference: DL-Homoserine(CAS DataBase Reference)
• NIST Chemistry Reference: DL-Homoserine(1927-25-9)
• EPA Substance Registry System: DL-Homoserine(1927-25-9)

Safety Data

• Safety Statements: 24/25
• Hazardous Substances Data: 1927-25-9(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
DL-Homoserine is used as an intermediate in the synthesis of various pharmaceuticals, including antibiotics, antifungal agents, and antiviral drugs. Its ability to act as a building block for the development of new drugs makes it a valuable compound in the pharmaceutical industry.
Used in Agrochemical Industry:
In the agrochemical industry, DL-Homoserine is utilized as a precursor for the synthesis of various agrochemicals, such as herbicides, insecticides, and fungicides. Its role in the production of these chemicals helps to improve crop yields and protect plants from pests and diseases.
Used in Organic Synthesis:
DL-Homoserine is used as a versatile building block in organic synthesis for the preparation of a wide range of organic compounds. Its unique structure allows for various chemical reactions, making it a valuable component in the synthesis of complex organic molecules.
Used in Research and Development:
In the field of research and development, DL-Homoserine is employed as a key compound for studying the synthesis and properties of various organic compounds. Its use in research helps to advance the understanding of chemical reactions and the development of new synthetic methods.

InChI:InChI=1/C4H9NO3/c5-3(1-2-6)4(7)8/h3,6H,1-2,5H2,(H,7,8)/t3-/m1/s1

Upstream product

• 52161-80-5 2-amino-4-phenoxybutanoic acid 
• 50992-08-0 2-(N,N-dibenzylamino)-4-hydroxybutyric acid lactone 
• 3157-50-4 2-amino-4-chlorobutyric acid 
• 90918-62-0 4-hydroxy-2-phenylhydrazono-butyric acid 
• 76338-90-4 α-amino-γ-bromobutyric acid hydrobromide 
• 29625-73-8 2-acetamido-4-O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-1-N-(4-L-aspartoyl)-2-deoxy-β-D-glucopyranosylamine 
• 76224-57-2 avenic acid A 
• 7647-01-0 hydrogenchloride 
• 24186-16-1 2-phenylhydrazono-γ-butyrolactone 
• 543-38-4 l-canavanine 
• 7732-18-5 water 
• 3493-11-6 (3S)-(3-amino-3-carboxypropyl)dimethylsulfonium iodide 
• 6305-38-0 α-amino-γ-butyrolactone hydrobromide 
• 59-51-8 DL-methionine 

Downstream Products

• 7471-52-5 5-(β-bromoethyl)hydantoin 
• 600-18-0 2-Oxobutyric acid 
• 38308-93-9 2-tert-butoxycarbonylamino-4-hydroxy-butyric acid benzyl ester 
• 38308-92-8 2-(tert-butoxycarbonylamino)-4-hydroxy-butanoic acid 
• 5746-78-1 N-Carbamoyl-homoserin 
• 58611-62-4 benzyl DL-N-(benzyloxycarbonyl)homoserinate 
• 15920-74-8 N-Formyl-homoserin-cyclohexylamid 
• 73739-19-2 3-benzoyl-[1,3]oxazinane-4-carboxylic acid 
• 320-77-4 1-hydroxy-propane-1,2,3-tricarboxylic acid 
• 77-92-9 citric acid 
• 118516-11-3 N-benzoylhomoserine lactone 
• 138252-17-2 2-(3-diphenylmethoxy-4-pyridon-1-yl)-4-hydroxybutyric acid, sodium salt 
• 42417-39-0 (RS)-α-amino-γ-butyrolactone hydrochloride 
• 2185-03-7 L-homoserine lactone hydrochloride 

Relevant articles and documents

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.

Microorganisms and methods for the biosynthesis of butadiene

The invention provides non-naturally occurring microbial organisms having a butadiene pathway. The invention additionally provides methods of using such organisms to produce butadiene.

FUNCTIONALIZED FLUORINE CONTAINING PHTHALOCYANINE MOLECULES

Functionalized fluorine containing phthalocyanine molecules, methods of making, and methods of use in diagnostic applications and disease treatment are disclosed herein. In some embodiments, the fluorine containing phthalocyanine molecules are functionalized with a reactive functional group or at least one cancer-targeting ligand (CTL). The CTL can facilitate more efficient binding and/or internalization to a cancer cell than to a healthy cell. The CTL can inhibit expression of oncoprotein in some embodiments. The pthalocyanine moiety can be used in diagnostic applications, such as fluorescence labeling of a cancer cell, and/or treatment applications, such as catalyzing formation of a reactive oxygen species (ROS) which can contribute to cell death of a cancer cell.

MICROORGANISMS AND METHODS FOR THE BIOSYNTHESIS OF BUTADIENE

The invention provides non-naturally occurring microbial organisms having a butadiene pathway. The invention additionally provides methods of using such organisms to produce butadiene.

METHOD FOR PREPARING AN AMINO ACID FROM 2 AMINOBUTYROLACTONE

The invention relates to a method for preparing an amino acid, or its salts, from 2-aminobutyrolactone (2ABL), said amino acid fitting the formula I, XCH2CH2CHNH2COOH, wherein X is such that X? represents a nucleophilic ion, according to which N-carboxylation of 2-aminobutyrolactone (2ABL) is achieved with carbon dioxide, and the thereby obtained 2ABL carbamate is reactive with an XH reagent or its salts.

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.

Structure-activity study of new inhibitors of human betaine-homocysteine S-methyltransferase

Betaine-homocysteine S-methyltransferase (BHMT) catalyzes the transfer of a methyl group from betaine to L-homocysteine, yielding dimethylglycine and L-methionine. In this study, we prepared a new series of BHMT inhibitors. The inhibitors were designed to mimic the hypothetical transition state of BHMT substrates and consisted of analogues with NH, N(CH3), or N(CH 3)2 groups separated from the homocysteine sulfur atom by a methylene, ethylene, or a propylene spacer. Only the inhibitor with the N(CH3) moiety and ethylene spacer gave moderate inhibition. This result led us to prepare two inhibitors lacking a nitrogen atom in the S-linked alkyl chain: (RS,RS)-5-(3-amino-3-carboxypropylthio)-3-methylpentanoic acid and (RS)-5-(3-amino-3-carboxypropylthio)-3,3-dimethylpentanoic acid. Both of these compounds were highly potent inhibitors of BHMT. The finding that BHMT does not tolerate a true betaine mimic within these inhibitors, especially the nitrogen atom, is surprising and evokes questions about putative conformational changes of BHMT upon the binding of the substrates/products and inhibitors.

Positional scanning for peptide secondary structure by systematic solid-phase synthesis of amino lactam peptides

Incorporation of amino lactams into biologically active peptides has been commonly used to restrict conformational mobility, enhance selectivity, and increase potency. A solid-phase method using a Fmoc-protection strategy has been developed for the systematic synthesis of peptides containing configurationally defined α- and β-amino γ-lactams. N-Alkylation of N-silyl peptides with five- and six-member cyclic sulfamidates 9 and 8 minimized bis-alkylation and provided N-alkyl peptides,which underwent lactam annulation under microwave heating. Employing th is solid-phase protocol on the growth hormone secretagogue GHRP-6, as well as on the allosteric modulator of the IL-1 receptor 101.10, has furnished 16 lactam derivatives and validated the effectiveness of this approach on peptides bearing aliphatic, aromatic, branched, charged, and heteroatomic side chains. The binding affinity IC 50 values of the GHRP-6 lactam analogues on both the GHS-R1a and CD36 receptors are reported as well as inhibition of thymocyte proliferation measurements for the 101.10 lactam analogues. In these cases, lactam analogues were prepared exhibiting similar or improved properties compared with the parent peptide. Considering the potential for amino lactams to induce peptide turn conformations, the effective method described herein for their supported construction on growing peptides, and for the systematical amino lactam scan of peptides, has proven useful for the rapid identification of the secondary structure necessary for peptide biological activity.

Process for producing alpha 2,3/ alpha 2,8-sialyltransferase and sialic acid-containing complex sugar

The present invention can provide a process for producing a protein having α2,3/α2,8-sialyltransferase activity using a transformant comprising a DNA encoding a protein having α2,3/α2,8-sialyltransferase activity derived from a microorganism belonging to the genus Pasteurella and a process for producing a sialic acid-containing complex carbohydrate using a transformant capable of producing a protein having α2,3/α2,8-sialyltransferase activity derived from a microorganism.

Gene recombinant antibody and antibody fragment thereof

A recombinant antibody or the antibody fragment thereof which specifically reacts with an extracellular domain of human CCR4; a DNA which encodes the recombinant antibody or the antibody fragment thereof; a method for producing the recombinant antibody or the antibody fragment thereof; a method for immunologically detecting CCR4, a method for immunologically detecting a cell which expressed CCR4 on the cell surface, a method for depleting a cell which expresses CCR4 on the cell surface, and a method for inhibiting production of Th2 cytokine, which comprise using the recombinant antibody according or antibody fragment thereof; a therapeutic or diagnostic agent for Th2-mediated immune diseases; and a therapeutic or diagnostic agent for a blood cancer.