284665-18-5Relevant articles and documents
Method for efficiently preparing deuterated iodomethane and application of deuterated iodomethane
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Paragraph 0020-0033, (2021/08/07)
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.
Rationally engineered variants of S-adenosylmethionine (SAM) synthase: Reduced product inhibition and synthesis of artificial cofactor homologues
Dippe,Brandt,Rost,Porzel,Schmidt,Wessjohann
supporting information, p. 3637 - 3640 (2015/03/30)
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
Biosynthesis of the modified peptide antibiotic nosiheptide in Streptomyces actuosus
Mocek,Knaggs,Tsuchiya,Nguyen,Beale,Floss
, p. 7557 - 7568 (2007/10/02)
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