title: Thioether crosslinkages created by a radical SAM enzyme.
abstract: Unusually versatile: While the β-carbon thioether linkage in lantibiotics has long been appreciated and is relatively well characterized, a recent publication shows that the unusual sulfur-to-α-carbon thioether crosslinks in subtilosin A are produced by a radical SAM enzyme, AlbA, that contains two [4 Fe-4 S] clusters, thus highlighting the versatility of post-translational modifications in natural product biosynthesis.
authors.affiliation: Key Laboratory of Combinatory Biosynthesis and Drug Discovery (Ministry of Education) and School of Pharmaceutical Sciences, Wuhan University, 185 East Lake Road, Wuhan 430071, PR China. qizhang@sioc.ac.cn
authors.forename: Qi
authors.initials: Q
authors.lastname: Zhang
authors.forename: Yi
authors.initials: Y
authors.lastname: Yu
mesh_terms: D000595:Amino Acid Sequence; D001430:Bacteriocins / Q000096:biosynthesis; D001688:Biological Products / Q000378:metabolism; D004798:Enzymes / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000378:metabolism; D008969:Molecular Sequence Data; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D012436:S-Adenosylmethionine / Q000378:metabolism*; D013440:Sulfides / Q000378:metabolism*
chemical_list: D001430:Bacteriocins; D001688:Biological Products; D004798:Enzymes; D007506:Iron-Sulfur Proteins; D013440:Sulfides; D012436:S-Adenosylmethionine