title: D-cysteine occurrence in thiostrepton may not necessitate an epimerase.
abstract: The natural product thiopeptide antibiotic thiostrepton is shown to undergo facile epimerization at its thiazoline residue in favor of the naturally observed D-configuration, suggesting that a classical epimerase enzyme may not be involved in its biosynthesis.
authors.affiliation: Technische Universität Dortmund, Fakultät Chemie, Otto-Hahn-Str. 6, D-44227 Dortmund, Germany.
authors.forename: Sebastian
authors.initials: S
authors.lastname: Schoof
authors.forename: Hans-Dieter
authors.initials: HD
authors.lastname: Arndt
mesh_terms: D000900:Anti-Bacterial Agents / Q000096:biosynthesis; D003545:Cysteine; D019998:Racemases and Epimerases / Q000378:metabolism*; D013883:Thiostrepton / Q000096:biosynthesis* / Q000737:chemistry
chemical_list: D000900:Anti-Bacterial Agents; D019998:Racemases and Epimerases; D013883:Thiostrepton; D003545:Cysteine