Dippe, M. et al. published their research in Chemical Communications (Cambridge, United Kingdom) in 2015 |CAS: 6038-19-3

The Article related to adenosylmethionine synthase bacillus protein engineering sam analog methylation, Enzymes: Substrates-Cofactors-Inhibitors-Activators-Coenzymes-Products and other aspects.Name: 3-Aminodihydrothiophen-2(3H)-one hydrochloride

Dippe, M.; Brandt, W.; Rost, H.; Porzel, A.; Schmidt, J.; Wessjohann, L. A. published an article in 2015, the title of the article was Rationally engineered variants of S-adenosylmethionine (SAM) synthase: reduced product inhibition and synthesis of artificial cofactor homologues.Name: 3-Aminodihydrothiophen-2(3H)-one hydrochloride And the article contains the following content:

S-Adenosylmethionine (SAM) synthase was engineered for biocatalytic production of SAM and long-chain analogs 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 analogs) due to a much reduced product inhibition. The experimental process involved the reaction of 3-Aminodihydrothiophen-2(3H)-one hydrochloride(cas: 6038-19-3).Name: 3-Aminodihydrothiophen-2(3H)-one hydrochloride

The Article related to adenosylmethionine synthase bacillus protein engineering sam analog methylation, Enzymes: Substrates-Cofactors-Inhibitors-Activators-Coenzymes-Products and other aspects.Name: 3-Aminodihydrothiophen-2(3H)-one hydrochloride

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Ester – an overview | ScienceDirect Topics