Enzymatic synthesis of S-adenosyl-l-homocysteine and its nucleoside analogs from racemic homocysteine thiolactone.

ABSTRACT: S-Adenosyl methionine (SAM)-dependent methyltransferases hold significant potential as tools for the biocatalytic synthesis of complex molecules due to their ability to methylate or alkylate substrates with high regio-, chemo-, and stereoselectivity. Recent advancements in enzyme-catalyzed S-methylation and S-alkylation of S-adenosyl homocysteine (SAH) using synthetic alkylation agents have expanded the scope of methyltransferases in preparative biocatalysis. This development has transformed SAH from an unwanted byproduct into a crucial - and currently expensive - reagent. In this report, we present a simple and scalable one-pot synthesis of SAH, starting from racemic homocysteine thiolactone and adenosine. This process is catalyzed by recombinant α-amino-ε-capr

SUBMITTER: Wen X 

PROVIDER: S-EPMC11391342 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature