- Synthesis method of O-methyl-D-serine
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The invention discloses a synthesis method of O-methyl-D-serine. The synthesis method includes the following steps that 1, acrylic acid methyl ester is added into a reaction bottle, after the temperature is raised, bromine is dropwise added, after an addition reaction is conducted, decompression and distillation are conducted to remove excessive bromine, methyl alcohol is added to residues, after the temperature is lowered, sodium methylate is added, after an alcoholysis reaction, decompression and distillation are conducted to remove methyl alcohol, ammonium hydroxide is added, after an ammonium hydroxide, concentrated crystallization is conducted, and O-methyl-DL-serine is obtained; 2, acetic acid is added into the reaction bottle, the O-methyl-DL-serine, D-tartaric acid and salicylaldehyde are added in sequence, after the temperature is raised for a reaction, cooling and crystallization are conducted, separation is conducted, and O-methyl-D-serine double salt is obtained; 3, the O-methyl-D-serine double salt is dissolved in a methyl alcohol aqueous solution, ammonium hydroxide is added to regulate PH to be 7-8, crystallization and separation are conducted, and the O-methyl-D-serine is obtained. The synthesis method is mild in reaction temperature, safe to operate, low in cost and high in chirality purity, and raw materials are easy to obtain.
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Paragraph 0041
(2017/01/02)
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- An efficient chemoenzymatic method to prepare optically active O-methyl-l-serine
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O-Methyl-l-serine and its derivatives are relevant in peptide synthesis (food, pharmaceuticals, and cosmetics). Optically active O-methyl-l-serine was prepared using a chemoenzymatic method from inexpensive acrylamide. Our method is a four step reaction sequence; bromination of acrylamide; etherification of dibromopropionamide; ammonolysis of α-bromo-β-methoxy-propionamide; enzymatic racemization; and selective hydrolysis. The double-enzyme catalyst system, which consists of α-amino-*-caprolactam racemase (Locus, E01594) and peptidase B (Locus, D84499), was successfully applied to produce enantiopure O-methyl-l-serine (ee >99.9%) in high yield (>99.7%). Optically active O-methyl-l-serine was obtained with a total yield of 82.4%.
- Wang, Zhi-Yuan,Xu, Li-Sheng,Gao, Ji,Liu, Jun-Zhong,Zhang, Hong-Juan,Liu, Qian,Jiao, Qing-Cai
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p. 1653 - 1656
(2013/02/23)
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- PROCESS FOR PREPARING LACOSAMIDE
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The present invention provides a process for the preparation of lacosamide in substantially optically pure form, which in one aspect comprises the following steps: (i) resolution of O-methyl-D,L-serine to provide O-methyl-D-serine in substantially optically pure form; (ii) acetylation of O-methyl-D-serine thereby obtained to provide the N-acetyl 10 derivative thereof in substantially optically pure form; (iii) activating the carboxy group of the compound thereby obtained; and (iv) reacting the compound thereby obtained with benzylamine.
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Page/Page column 24
(2012/06/01)
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- Calyxamides A and B, cytotoxic cyclic peptides from the marine sponge Discodermia calyx
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Cyclic peptides containing 5-hydroxytryptophan and thiazole moieties were isolated from the marine sponge Discodermia calyx collected near Shikine-jima Island, Japan. The structures of calyxamides A (1) and B (2), including the absolute configurations of all amino acids, were elucidated by spectroscopic analyses and degradation experiments. The structures are similar to keramamides F and G, previously isolated from Theonella sp. The analysis of the 16S rDNA sequences obtained from the metagenomic DNA of D. calyx revealed the presence of Candidatus Entotheonella sp., an unculturable δ-proteobacterium inhabiting the Theonella genus and implicated in the biosynthesis of bioactive peptides.
- Kimura, Miki,Wakimoto, Toshiyuki,Egami, Yoko,Tan, Karen Co,Ise, Yuji,Abe, Ikuro
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experimental part
p. 290 - 294
(2012/05/05)
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- Neomastoidin A, a novel monoacylglycerol with an amino acid moiety from Macrolepiota neomastoidea
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A novel monoacylglycerol with an amino acid moiety, neomastoidin A (1), was isolated from the fruiting bodies of the poisonous mushroom Macrolepiota neomastoidea. The structure of 1 was established by extensive spectroscopic analysis and further confirmed
- Kim, Ki Hyun,Choi, Sang Un,Lee, Kang Ro
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scheme or table
p. 894 - 895
(2010/03/04)
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- Process for producing beta-1, 3-n-acetylglucosamine transferase and n-acetylglucosamine- containing composite saccharide
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The present invention can provide a process for producing a protein having β1,3-N-acetylglucosaminyltransferase activity using a transformant comprising a DNA encoding a protein having β1,3-N-acetylglucosaminyltransferase activity derived from a microorganism belonging to the genus Pasteurella and a process for producing an N-acetylglucosamine-containing complex carbohydrate using a transformant capable of producing a protein having β1,3-N-acetylglucosaminyltransferase activity derived from a microorganism.
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- METHOD OF SEARCHING SUBSTANE HAVING ANTIDIABETIC ACTIVITY
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The present invention provides a screening method of a substance which inhibits binding of a condensed purine derivative to a pancreatic β cell or a treated product of the cell, a substance which inhibits binding of a condensed purine derivative to a protein capable of the condensed purine derivative, and a substance which inhibits the expression or enzymatic activity of a protein capable of a condensed purine derivative, which comprises using the condensed purine derivative and a pancreatic β cell or a treated product of the cell or a protein capable of binding to the condensed purine derivative.
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- Process for producing alpha 2,3/ alpha 2,8-sialyltransferase and sialic acid-containing complex sugar
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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.
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- Beta1, 3-galactose transferase and dna encoding the enzyme
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The present invention provides a protein having β1,3-galactosyltransferase activity, a DNA encoding the protein, a transformant comprising the DNA, a process for producing the protein using the transformant, and a process for producing a galactose-containing complex carbohydrate using the transformant.
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- Process for producing alpha1,4-galactosyltransferase and galactose-containing complex sugar
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The present invention can provide a process for producing a protein having α1.4-galactosyltransferase activity using a transformant comprising a DNA encoding a protein having α1.4-galactosyltransferase activity derived from a microorganism belonging to the genus Pasteurella and a process for producing a galactose-containing complex carbohydrate using a transformant capable of producing a protein having α1,4-galactosyltransferase activity derived from a microorganism.
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- Human CDR-grafted antibody and antibody fragment thereof
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A human CDR-grafted antibody or the antibody fragment thereof which specifically reacts with the extracellular region of human CC chemokine receptor 4 (CCR4) but does not react with a human blood platelet; a human CDR-grafted antibody or the antibody fragment thereof which specifically reacts with the extracellular region of CCR4 and has a cytotoxic activity against a CCR4-expressing cell; and a medicament, a therapeutic agent or a diagnostic agent comprising at least one of the antibodies and the antibody fragments thereof as an active ingredient.
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- Gene recombinant antibody and antibody fragment thereof
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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.
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- Acylase I-catalyzed deacetylation of N-acetyl-L-cysteine and S-alkyl-N- acetyl-L-cysteines
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The aminoacylase that catalyzes the hydrolysis of N-acetyl-L-cysteine (NAC) was identified as acylase I after purification by column chromatography and electrophoretic analysis. Rat kidney cytosol was fractionated by ammonium sulfate precipitation, and the proteins were separated by ion-exchange column chromatography, gel-filtration column chromatography, and hydrophobic interaction column chromatography. Acylase activity with NAC and N-acetyl-L- methionine (NAM), a known substrate for acylase I, as substrates coeluted during all chromatographic steps. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the protein was purified to near homogeneity and had a subunit M(r) of 43 000, which is identical with the M(r) of acylase I from porcine kidney and bovine liver. n-Butylmalonic acid was a slow-binding inhibitor of acylase I and inhibited the deacetylation of NAC with a K(i) of 192 ± 27 μM. These results show that acylase I catalyzes the deacetylation of NAC. The acylase I-catalyzed deacetylation of a range of S-alkyl-N- acetyl-L-cysteines, their carbon and oxygen analogues, and the selenium analogue of NAM was also studied with porcine kidney acylase I. The specific activity of the acylase I-catalyzed deacetylation of these substrates was related to their calculated molar volumes and log P values. The S-alkyl-N- acetyl-L-cysteines with short (C0-C3) and unbranched S-alkyl substituents were good acylase I substrates, whereas the S-alkyl-N-acetyl-L-cysteines with long (>C3) and branched S-alkyl substituents were poor acylase I substrates. The carbon and oxygen analogues of S-methyl-N-acetyl-L-cysteine and the carbon analogue of S-ethyl-N-acetyl-L-cysteine were poor acylase I substrates, whereas the selenium analogue of NAM was a good acylase I substrate.
- Uttamsing, Vinita,Keller,Anders
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p. 800 - 809
(2007/10/03)
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- Structure-Function Relationship of Acyl Amino Acid Surfactants: Surface Activity and Antimicrobial Properties
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Amino acid surfactants (AAS), having the general structure α-amino-(N-acyl)-β-alkoxypropionate, were synthesized chemically.Surface activity and antimicrobial properties of the AAS were evaluated.Increases in acyl chain length (i.e., C10-C14) resulted in a linear reduction in surface tension (i.e., 43-36 mN*m-1), as well as dramatic decreases in critical micelle concentrations (cmc) (i.e., 17.9-0.43 mM).Strong correlations existed between the cmc of AAS and their minimal inhibitory concentrations (mic) against Escherichia coli, Pseudomonas aeruginosa, Aspergillus niger, and Saccharomyces cerevisiae.Sensitivity of the microorganisms to the various AAS followed the order Staphylococcus aureus > A. niger= S. cerevisiae> E. coli> P. aeruginosa.In comparison with methyl p-hydroxybenzoate, AAS (MN14) showed 2-8, 64, and 4-8 times the activity against Gram-negative bacteria, Gram-positive bacteria, and fungi, respectively.Surface adsorption and/or bifunctional binding to the cell membrane may account for AAS action on microorganisms.
- Xia, Jiding,Xia, Yongmei,Nnanna, Ifendu A.
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p. 867 - 871
(2007/10/02)
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- ASYMMERTIC SYNTHESIS OF Β-SUBSTITUTED α-AMINO ACIDS VIA A CHIRAL Ni(II) COMPLEX OF DEHYDROALANINE
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An efficient approach to the asymmetric synthesis of β-substituted (S)-alanines is describen.The chiral Ni(II) complex of a Schiff base derived from (S)-o-N-(N-benzylpropyl)aminobenzophenone (BBP) and glycine was treated with formaldehyde and sodium methoxide to give a corresponding (R)-serine complex which, in turn, was converted to the chiral Ni(II) dehydroalanine complex.Michael type base catalyzed addition of nucleophiles (including MeOH, Me2NH, PhCH2NH2, imidazole, PhSH, PhCH2SH,, malonic ester and benzylmagnesium chloride) produced a mixture of diastereoisomeric complexes with a 70-90percent excess of S,S (or L,L) isomers over the S,R (or L,D) ones.The cleavage of pure diastereoisomers with aqueous HCl gave, in good yields, β-substituted (S) (or L)-alanines and regenerated the chiral auxiliary (BBP).
- Belokon, , Yuri N.,Sagyan, Ashot S.,Djamgaryan, Silva M.,Bakhmutov, Vladimir I.,Belikov, Vasili M.
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p. 5507 - 5514
(2007/10/02)
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- Mechanism of Asymmetric Production of L-Aromatic Amino Acids from the Corresponding Hydantoins by Flavobacterium sp.
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The mechanism of asymmetric production of L-aromatic amino acids from the corresponding hydantoins by Flavobacterium sp.AJ-3912 was examined by investigating the properties of the enzymes involved in the hydrolysis of 5-substituted hydantoins corresponding to aromatic amino acids (AAH).The enzymatic hydrolysis of AAH by Flavobacterium sp.AJ-3912 consisted of the following two successive reactions; a hydrolytic ring opening reaction of DL-AAH to L- and D-form N-carbamyl aromatic amino acids (NCA), involving an enzyme (hydantoin hydrolase) followed by a hydrolytic cleaving reaction of the L-form NCA to L-aromatic amino acids involving another enzyme (N-carbamyl-L-aromatic amino acid hydrolase, abbreviated as L-NCA hydrolase).The ring opening reaction involving hydantoin hydrolase was not stereospecific, but the NCA cleaving reaction involving L-NCA hydrolase was completely L-specific.The pathway for the conversion of the by-produced D-form NCA to L-aromatic amino acids was as follows; conversion of D-form NCA to D-AAH through the reverse reaction of hydantoin hydrolase, and then conversion of the D-AAH to L-AAH through spontaneous racemization, followed by the successive hydrolysis of the L-AAH to L-aromatic amino acids by hydantoin hydrolase and L-NCA hydrolase.
- Yokozeki, Kenzo,Hirose, Yoshiteru,Kubota, Koji
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p. 737 - 746
(2007/10/02)
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- Mechanism of formation of serine β-lactones by Mitsunobu cyclization: synthesis and use of L-serine stereospecifically labelled with deuterium at C-3
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The ring closure of N-benzyloxycarbonyl-L-serine (1) under Mitsunobu conditions (Ph3P, dimethyl azodicarboxylate, -78 deg C) to give the corresponding β-lactone (2) is shown by deuterium and oxygen-18 labelling studies to proceed by hydroxy group activation, in contrast to analogous cyclizations of more hindered β-hydroxy acids, which usually occur by carboxy group activation.Samples of 1 stereospecifically labelled with deuterium at C-3 were prepared by hydrogenation of (Z)-2-acetamido-3-methoxyacrylic acid (9) with deuterium, followed by selective Acylase I deacetylation of the 2S isomer, removal of the protecting groups, and N-acylation of the resulting L-serine with benzyl chloroformate.Mitsunobu cyclizations of this 3R deuterated N-acyl serine, of the analog lg, and of the derivative 1f show that lactonization occurs with inversion of configuration at C-3, loss of the hydroxy oxygen, and retention of the carboxy oxygens.Similar labelling experiments demonstrate that aqueous sodium hydroxide opens the β-lactone ring by exclusive attack at the carbonyl to regenerate 1, whereas acidic hydrolysis proceeds primarily by attack of water at the C-3 methylene group of 2.This information allows interconversion of L-serines that are stereospecifically labelled at C-3 with hydrogen isotopes and affords access to other labelled β-substituted alanines.
- Ramer, Shawn E.,Moore, Richard N.,Vederas, John C.
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p. 706 - 713
(2007/10/02)
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