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We developed mixed MtaABC\/MtgABC enzyme platforms capable of catalyzing methylation of non\u2010native thiol and aniline substrates using unactivated methyl donors like methanol and glycine betaine. This approach allows highly enantioselective and site\u2010selective methylation of aliphatic thiols with high turnover number (up to 6000), providing the first demonstration of enantioselective non\u2010native catalysis by cobamide\u2010dependent enzymes. The MtaAC+MtgB system was subsequently engineered through site\u2010directed mutagenesis, resulting in large enhancements in activity for the desymmetrization of non\u2010native ester\u2010containing prochiral thiols. These findings establish MTase complexes as a promising platform for non\u2010native biocatalysis.<\/jats:p>","DOI":"10.1002\/anie.1537547","type":"journal-article","created":{"date-parts":[[2026,9,17]],"date-time":"2026-09-17T04:03:53Z","timestamp":1789617833000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Nonnative Thiol and Aniline Methylation, Including Enantioselective Dithiol Desymmetrization, by Multicomponent Cobamide\u2010Dependent Methyltransferases Using Unactivated Methyl Donors"],"prefix":"10.1002","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5725-9262","authenticated-orcid":false,"given":"Amardeep","family":"Kumar","sequence":"first","affiliation":[{"name":"Department of Chemistry Indiana University  Bloomington Indiana USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Osman Ishag","family":"Adam","sequence":"additional","affiliation":[{"name":"Department of Chemistry 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