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• W2767482390 endingPage "6097" @default.
• W2767482390 startingPage "6087" @default.
• W2767482390 abstract "Dimethylation of amino acids consists of an interesting and puzzling series of events that could be achieved, during nonribosomal peptide biosynthesis, either by a single adenylation (A) domain interrupted by a methyltransferase (M) domain or by the sequential action of two of such independent enzymes. Herein, to establish the method by which Nature N,S-dimethylates l-Cys, we studied its formation during thiochondrilline A biosynthesis by evaluating TioS(A3aM3SA3bT3) and TioN(AaMNAb). This study not only led to identification of the exact pathway followed in Nature by these two enzymes for N,S-dimethylation of l-Cys, but also revealed that a single interrupted A domain can N,N-dimethylate amino acids, a novel phenomenon in the nonribosomal peptide field. These findings offer important and useful insights for the development and engineering of novel interrupted A domain enzymes to serve, in the future, as tools for combinatorial biosynthesis." @default.
• W2767482390 created "2017-11-17" @default.
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• W2767482390 date "2017-11-07" @default.
• W2767482390 modified "2023-10-12" @default.
• W2767482390 title "Deciphering Nature’s Intricate Way of <i>N</i>,<i>S</i>-Dimethylating <scp>l</scp>-Cysteine: Sequential Action of Two Bifunctional Adenylation Domains" @default.
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• W2767482390 doi "https://doi.org/10.1021/acs.biochem.7b00980" @default.
• W2767482390 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29112395" @default.
• W2767482390 hasPublicationYear "2017" @default.
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