- STORAGE-STABLE FORM OF 3-METHYLTHIOPROPIONALDEHYDE
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A chemical compound of formula (I), and specific compositions including 3-methylthiopropionaldehyde, 3-methylthiopropane-1,1-diol, a compound of formula I and water, and processes for producing same and also the use of same may be used for the production of 2-hydroxy-4-(methylthio)butyronitrile, methionine hydantoin, methionine. Protected forms may be used for the storage and/or transport of 3-methylthiopropionaldehyde.
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Paragraph 0058-0059
(2021/11/13)
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- METHOD FOR PRODUCING METHIONINE
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The present invention pertains to a method for producing methionine or salts or derivatives thereof from hydrogen cyanide (HCN), the method comprising a step of producing 2-hydroxy-4-(methylthio)butyronitrile (MMP-CN), or a crude product mixture comprising MMP-CN, by contacting a hydrogen cyanide (HCN) process gas mixture prepared according to the Andrussow process from methane, ammonia and oxygen, with 3-methylmercaptopropionaldehyde (MMP), wherein the HCN process gas mixture is obtained from the crude HCN process gas mixture by adjusting the amount of ammonia to between 20 % (v/v) and 60% (v/v) of the amount of the ammonia in the crude HCN process gas mixture.
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Page/Page column 18-19
(2020/07/07)
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- Effect of high hydrostatic pressure on prebiotic peptide synthesis
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Prebiotic peptide synthesis is a central issue concerning life's origins. Many studies considered that life might come from Hadean deep-sea environment, that is, under high hydrostatic pressure conditions. However, the properties of prebiotic peptide formation under high hydrostatic pressure conditions have seldom been mentioned. Here we report that the yields of dipeptides increase with raised pressures. Significantly, effect of pressure on the formation of dipeptide was obvious at relatively low temperature. Considering that the deep sea is of high hydrostatic pressure, the pressure may serve as one of the key factors in prebiotic peptide synthesis in the Hadean deep-sea environment. The high hydrostatic pressure should be considered as one of the significant factors in studying the origin of life.
- Ying, Jianxi,Chen, Peng,Wu, Yile,Yang, Xu,Yan, Kaili,Xu, Pengxiang,Zhao, Yufen
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supporting information
p. 367 - 370
(2018/06/18)
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- METHOD FOR PREPARING METHIONINE
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The present invention relates to a method for preparing methionine or methionine salts. In particular, the invention describes the step of preparing 2-hydroxy-4-(methylthio)butyronitrile (MMP-CN) from 3-methylthiopropanal (MMP) and hydrogen cyanide (HCN) in the presence of ammonia by bringing a gaseous mixture comprising HCN and ammonia into contact with MMP.
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Page/Page column 17; 18
(2018/07/29)
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- Preparation and use of methionylmethionine as feed additive for fish and crustaceans
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An animal feed mixture containing DL-methionyl-DL-methionine and salts thereof for animals kept in aquacultures is provided. Methods for preparing DL-methionyl-DL-methionine of formula (I) and methods to fractionate the diasteriomeric forms obtained are also provided.
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- Peptide bond formation by aminolysin-A catalysis: A simple approach to enzymatic synthesis of diverse short oligopeptides and biologically active puromycins
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A new S9 family aminopeptidase derived from the actinobacterial thermophile Acidothermus cellulolyticus was cloned and engineered into a transaminopeptidase by site-directed mutagenesis of catalytic Ser491 into Cys. The engineered biocatalyst, designated aminolysin-A, can catalyze the formation of peptide bonds to give linear homo-oligopeptides, hetero-dipeptides, and cyclic dipeptides using cost-effective substrates in a one-pot reaction. Aminolysin-A can recognize several C-terminal-modified amino acids, including the l- and d-forms, as acyl donors as well as free amines, including amino acids and puromycin aminonucleoside, as acyl acceptors. The absence of amino acid esters prevents the formation of peptides; therefore, the reaction mechanism involves aminolysis and not a reverse reaction of hydrolysis. The aminolysin system will be a beneficial tool for the preparation of structurally diverse peptide mimetics by a simple approach.
- Usuki, Hirokazu,Yamamoto, Yukihiro,Arima, Jiro,Iwabuchi, Masaki,Miyoshi, Shozo,Nitoda, Teruhiko,Hatanaka, Tadashi
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supporting information; experimental part
p. 2327 - 2335
(2011/05/02)
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- A novel L-amino acid ligase from bacillus subtilis NBRC3134 catalyzed oligopeptide synthesis
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L-Amino acid ligase catalyzes dipeptide synthesis from unprotected L-amino acids in an ATP-dependent manner. We have purified a new L-amino acid ligase, RizA, which synthesizes dipeptides whose N-terminus is Arg, from Bacillus subtilis NBRC3134, a microorganism that produces a rhizocticin peptide antibiotic. It was suggested that RizA is probably involved in rhizocticin biosynthesis. In this study, we performed sequence analysis of unknown regions around rizA, and newly identified a gene that encodes a protein that possesses an ATP-grasp motif upstream of rizA. This gene was designated rizB, and its recombinant protein was prepared. Recombinant RizB synthesized homo-oligo-mers of branched-chain L-amino acids and L-methionine consisting of two to five amino acids in an ATP-dependent manner. RizB also synthesized various heteropeptides. Further examination showed that RizB might elongate a peptide chain at the N-terminus. This is the first report on an L-amino acid ligase catalyzing oligopeptide synthesis.
- Kino, Kuniki,Arai, Toshinobu,Tateiwa, Daisuke
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experimental part
p. 129 - 134
(2010/04/24)
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- Investigation on interaction of L-methionine dipeptide with ct-DNA by ultraviolet spectroscopy
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In this article, L-methionine peptides were synthesized with the assistance of phosphorus oxychloride. L-methionine dipeptide was purified by HPLC and characterized by the means of 1H-NMR, 13C-NMR and ESI-MS. The interaction of L-Methionine dipeptide with ct-DNA was studied by ultraviolet spectra. The results showed that L-Methionine dipeptide could interact with phosphorous groups of ct-DNA. The influences of interaction time, ionic strength, and phosphate anion on the interaction between L-methionine dipeptide and ct-DNA were also investigated. Copyright Taylor & Francis Group, LLC.
- Lu, Kui,Li, Rui,Ma, Li
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body text
p. 596 - 602
(2009/04/06)
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- PROCESS FOR PREPARING AMINO ACIDS USING THE AMIDOCARBONYLATION REACTION (1)
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The present invention relates to a sequence for the preparation of amino acids, for example alpha amino acids, in particular methionine, by making use of an amidocarbonylation reaction and reuse of the catalyst.
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Page/Page column 12-13
(2008/06/13)
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- Photooxidation of Methionine Derivatives by the 4-Carboxybenzophenone Triplet State in Aqueous Solution. Intracomplex Proton Transfer Involving the Amino Group
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Oxidation of the triplet state of 4-carboxybenzophenone (CB) by a series of five substituted methionines and three methionine-containing dipeptides was monitored under laser flash photolysis conditions in aqueous solution. Spectral resolution techniques were employed to follow the concentration profiles of the intermediates formed from the quenching events. From these concentration profiles, quantum yields for the intermediates were determined. Branching ratios were evaluated for the decay of the charge-transfer complex by the competing processes of back electron transfer, proton transfer and escape of radical ions. The relative prominence of these processes was discussed in terms of the proton-transfer tendencies of the nominal sulfur-radical-cationic species. A systematic decrease was observed in the quantum yields for the escape of radical ions along with a correlated increase in the proton-transfer yields. The enhanced propensity of the sulfur radical cations to deprotonate is due to deprotonation at the carbons adjacent to the sulfur-cationic site and at the unsubstituted amino groups when present. This scheme was supported by an observed decrease in the yields of dimeric sulfur radical cations with an increase in the electron-withdrawing abilities of the substituents, making the radical-cationic species stronger acids. The involvement of protons on the amino groups was implicated by the correlation of the quantum yields of ketyl radical formation in the photo-chemistry experiments with the rate constants for the reaction of the CB radical anion with the sulfur-containing substrates in pulse radiolysis experiments.
- Hug, Gordon L.,Bobrowski, Krzysztof,Kozubek, Halina,Marciniak, Bronislaw
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p. 785 - 796
(2007/10/03)
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- A process for enzymatic production of dipeptides
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Dipeptides having the general formula, H-A-B-Y, wherein A represents an optionally side-chain protected L- or D-α-amino acid or ω-amino acid and B represents an optionally side-chain protected L- or D-α-amino-carboxylic acid which may be the same as or different from A, an L- or D-aminophosphonic acid or L- or D--aminosulfonic acid or the corresponding ω-amino acids or salts and hydrates thereof, and Y is OH or a C-terminal blocking group, are prepared by reacting a substrate component, which is an amino acid derivative having the formula wherein A is as defined above, R1 represents hydrogen, alkyl, aryl or aralkyl optionally substituted with inert substituents or an α-des-amino fragment of an amino acid, and R2 and R3 are the same or different and each represents hydrogen, alkyl, aryl or aralkyl optionally substituted with inert substituents,with a nucleophile component which when A = B may be formed in situ and is selected from (a) L-amino acids having the formula, H-B-OH (b) L-amino acid amides having the formula wherein B is an L-amino acid, and R2 and R3 have the above meaning, except that when R2 represents hydrogen, R3 may also represent hydroxy or amino (c) L-amino acid esters having the formula, H-B-OR4, wherein B is an L-amino acid, and R4 represents alkyl, aryl or aralkyl, and (d) optionally acid group protected straight chain or branched amino phosphonic acids or amino sulfonic acids having the formula, NH2CxHzPO3H2 or NH2CxHzSO3H, wherein x is 1-6 and z is 2-12 in the presence of a serine or thiol carboxypeptidase from yeast or of animal, vegetable or other microbial origin, preferably CPD-Y from yeast in an aqueous solution or suspension having a pH value between 5 and 10.5 optionally containing an organic solvent and/or a salt, and then, if desired, cleaving a present side--chain protecting group or protective group Y and/or, if desired, converting the resulting dipeptide derivative to a salt or hydrate. The process allows for production of L,L-, LD-, DL- and DD-dipeptides without risk of racemization in a simple and economic manner.
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- FORMATION CONSTANTS OF SILVER(I) COMPLEXES OF SOME SULPHUR-CONTAINING DIPEPTIDES AND VALYLVALINE
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Formation constants at 25 deg C and l = 0.10 mol dm-3 (KNO3) have been determined for the complexes of AgI with a range of nine dipeptides which incorporate side-chains containing one (glycylmethionine and methionylglycine) or two sulphur donor atoms.In the latter case dipeptides formed from amino acids of the same and of different chiralities were studied (e.g.L-methionyl-L-methionine and L-methionyl-D-methionine).The results are compared with those for valylvaline.Values for the formation constants are interpreted in terms of the preferred conformations of the dipeptides, and the tendency for AgI to bond to S-donor atoms or to adopt linear co-ordination through the formation of dimeric complexes.
- Lyons, Anthony Q.,Pettit, Leslie D.
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p. 2305 - 2308
(2007/10/02)
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