7349-78-2

Basic information

• Product Name: H-MET-MET-OH
• Synonyms: MET-MET;L-MET-MET;L-METHIONYL-L-METHIONINE;H-MET-MET-OH;Dimethionine;L-Met-L-Met-OH;Met-Met-OH;Methionine, N-L-methionyl-, L-
• CAS NO: 7349-78-2
• Molecular Formula: C₁₀H₂₀N₂O₃S₂
• Molecular Weight: 280.41
• Mol File: 7349-78-2.mol

Chemical Properties

• Melting Point: 224.0-226.5 °C
• Boiling Point: 555.1°Cat760mmHg
• Flash Point: 289.5°C
• Appearance: /
• Density: 1.237g/cm³
• Storage Temp.: -15°C
• PKA: 3.02±0.10(Predicted)
• CAS DataBase Reference: H-MET-MET-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-MET-MET-OH(7349-78-2)
• EPA Substance Registry System: H-MET-MET-OH(7349-78-2)

Safety Data

• Hazardous Substances Data: 7349-78-2(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
H-MET-MET-OH is used as a pharmaceutical compound for its potential therapeutic applications. Its antioxidant properties and involvement in the methylation process make it a candidate for the development of drugs targeting various health conditions.
Used in Nutritional Supplements:
H-MET-MET-OH is used as a dietary supplement to provide the essential amino acid methionine, which is crucial for protein synthesis and overall health. It can be included in products designed to support muscle growth, immune function, and antioxidant defense.
Used in Cosmetics Industry:
H-MET-MET-OH is used as an ingredient in cosmetic products for its antioxidant properties. It can be incorporated into skincare formulations to protect the skin from oxidative stress and promote a healthy complexion.
Used in Food Industry:
H-MET-MET-OH is used as a food additive to enhance the nutritional value of products. It can be added to protein-rich foods or supplements to provide the essential amino acid methionine, contributing to overall health and well-being.

Upstream product

• 63-68-3 L-methionine 
• 61413-48-7 (S)-2-[(S)-2-benzyloxycarbonylamino-4-methylsulfanylbutyrylamino]-3-methylsulfanylbutanoic acid 
• 45012-54-2 methionine isopropyl ester 
• 101833-60-7 N-(N-phenylmethanesulfonyl-L-methionyl)-L-methionine 
• 51529-24-9 N-t-butoxycarbonyl-L-methionine-L-methionine 
• 2488-15-5 N-tert-butoxycarbonyl-L-methionine 
• 3845-64-5 tertbutoxycarbonyl-L-methionine N-hydroxysuccinimide ester 
• 27169-27-3 Z-Met-Met-OMe 
• 2899-36-7 L-methionine ethyl ester monohydrochloride 
• 72-18-4 L-valine 
• 10332-17-9 Met-OMe 
• 17773-41-0 2-hydroxy-4-(methylthio)butyronitrile 
• 1115-47-5 N-acetyl-DL-methionine 
• 59-51-8 DL-methionine 

Downstream Products

• 59-51-8 DL-methionine 

Relevant articles and documents

STORAGE-STABLE FORM OF 3-METHYLTHIOPROPIONALDEHYDE

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.

METHOD FOR PRODUCING METHIONINE

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.

Effect of high hydrostatic pressure on prebiotic peptide synthesis

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.

METHOD FOR PREPARING METHIONINE

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.

Preparation and use of methionylmethionine as feed additive for fish and crustaceans

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.

Peptide bond formation by aminolysin-A catalysis: A simple approach to enzymatic synthesis of diverse short oligopeptides and biologically active puromycins

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.

A novel L-amino acid ligase from bacillus subtilis NBRC3134 catalyzed oligopeptide synthesis

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.

Investigation on interaction of L-methionine dipeptide with ct-DNA by ultraviolet spectroscopy

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.

PROCESS FOR PREPARING AMINO ACIDS USING THE AMIDOCARBONYLATION REACTION (1)

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.

Photooxidation of Methionine Derivatives by the 4-Carboxybenzophenone Triplet State in Aqueous Solution. Intracomplex Proton Transfer Involving the Amino Group

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.