284665-20-9

Usage

Uses

Methionine-methyl-d3 is the labeled Methionine-methyl, a useful building block.

Upstream product

• 626-72-2 L-homocystine 
• 20710-47-8 [13C₂H₃] methyl iodide 
• 331665-05-5 C₅H₄⁽²⁾H₇NO₂S 
• 93709-61-6 DL-[3,3,4,4-⁽²⁾H₄]methionine 
• 331665-06-6 C₇H₆⁽²⁾H₇NO₃S 
• 865-50-9 iodomethane-d3 
• 78496-74-9 (4R)-L-<4-2H>homocysteine 
• 18265-50-4 DL-homocysteine thiolactone hydrochloride 

Downstream Products

• 521-03-9 22-dihydrochondrillasterol 
• 6785-58-6 22-dihydro-25-dehydrochondrillasterol 

Relevant academic research and scientific papers

Method for efficiently preparing deuterated iodomethane and application of deuterated iodomethane

The invention discloses a method for efficiently preparing deuterated iodomethane and an application of the deuterated iodomethane; according to the method, deuterated methanol and iodine elementary substance are used as reaction raw materials, in a hydrogen atmosphere, a transition metal catalyst and a ligand are added, and the deuterated iodomethane is generated in situ at the temperature of 0 DEG C-120 DEG C. The application is the application of deuterated iodomethane as a methylation reagent in preparation of S-(methyl-D3)homocysteine, and mainly comprises the steps: carrying out methylation reaction on a compound a, namely (t-butyloxycarboryl)-L-homocysteine methyl ester and deuterated iodomethane in an organic solvent under the action of a base catalyst to obtain a product b; and performing deprotection on the product b to obtain a target product c, namely S-(methyl-D3)homocysteine. Anhydrous hydrogen iodide is prepared through catalysis of a transition metal catalyst, the anhydrous hydrogen iodide and deuterated methanol directly react through a one-pot method to obtain deuterated iodomethane with the high yield (88%), and the deuterated iodomethane serves as a deuterated methyl reagent to prepare S-(methyl-D3)homocysteine with the high deuterium doping rate and the yield (75%). The method is simple and easy to operate, and reaction conditions are mild.

Synthetic method of stable isotope deuterium-labeled alpha-amino acid

The invention relates to a synthetic method of stable isotope deuterium-labeled alpha-amino acid. According to the method, one or more deuterium-labeled halides are taken as labeled precursors and subjected to a reaction with phthalimide dimethyl malonate sodium salt, one or more deuterium-substituted phthalimide dimethyl malonate is obtained, and after hydrolysis, stable isotope deuterium-labeledalpha-amino acid is obtained. Compared with the prior art, the synthetic method is simple, safe and reliable, chemical purity of a product after simple separation and purification reaches 99% or higher, isotope abundance is 99% or higher, and the method can be applied to fields of protein metabolism tracing, food safety testing and the like.

Rationally engineered variants of S-adenosylmethionine (SAM) synthase: Reduced product inhibition and synthesis of artificial cofactor homologues

S-Adenosylmethionine (SAM) synthase was engineered for biocatalytic production of SAM and long-chain analogues by rational re-design. Substitution of two conserved isoleucine residues extended the substrate spectrum of the enzyme to artificial S-alkylhomocysteines. The variants proved to be beneficial in preparative synthesis of SAM (and analogues) due to a much reduced product inhibition. This journal is

Synthesis of L-[3,3,4,4,S-methyl-2H7]methionine for use as a substrate for the methionine loading test

Optically pure L-[3,3,4,4,S-methyl-2H7]methionine (L-[2H7]methionine) for use as a substrate for the methionine loading test has been prepared. The racemic [2H7]methionine was prepared from DL-[3,3,4,4-2H4]methionine (DL-[2H4]methionine) by conversion of the S-CH3 group to a C2H3 group. The racemate was resolved by stereospecific hydrolysis of the N-acetylated derivative with acylase. After an intravenous administration of L-[2H7]methionine in a rat, the concentration of L-[2H7]methionine and the metabolites in plasma were determined by GC-MS-SIM. L-[2H4]Homocysteine and L-[2H4]methionine were detected in plasma at 30 min after dosing. These results show that L-[2H7]methionine was converted by de-methylation and subsequent remethylation to form L-[2H4] methionine.

Biosynthetic Studies of Marine Lipids. 4. Mechanism of Side Chain Alkylation in (E)-24-Propylidenecholesterol by a Chrysophyte Alga

A photosynthetic marine Chrysophyte (unicellular alga) was cultured in a medium containing labeled methionine (methyl-13C, methyl-d3).The 2H and 13C distribution in the alkyl substituents of the sterols was determined by 2H and 13C NMR.Although two novel cyclopropyl sterols - (24R,28R)- and (24S,28R)-24,28-methylene-5-stigmasten-3β-ol - and their ring opening products were found as trace sterols in the alga, the results of 2H NMR indicate that the substituent in the side chain of the main sterol ((E)-24-propylidenecholesterol) is not formed by ring opening of these cyclopropyl sterols.Instead, the main sterol is most likely formed by further alkylation of a 24-vinyl sterol which has so far not been been encountered in nature.Other novel sterols encountered in the Chrysophyte belong to the rare classes of Δ23, 14α-methyl, and Δ8(14),15-diene sterols.

Stereochemical Analysis of γ-Replacement and γ-Elimination Processes Catalyzed by a Pyridoxal Phosphate Dependent Enzyme

(Z)- and (E)-Vinylglycine samples have been synthesized and used to determine the stereochemical outcome of a pyridoxal phosphate dependent bacterial enzyme cyctathionine γ-synthase.For the first time both the γ-replacement mode, vinylglycine or O-succinylhomoserine to cystathionine, and the γ-elimination mode, vinylglycine or O-succinylhomoserine to α-ketobutyrate, have been solved stereochemically.The diastereomeric cyctathionines produces enzymically in the γ-replacement mode were degraded to homoserines, the absolute chiralities were determined, and then the compounds were succinilated.The O-succinylhomoserines were then processed enzymically to cystathionines enzymically, and the stereochemical course of the first half-reaction was thereby determined.