D-cysteine occurrence in thiostrepton may not necessitate an epimerase.
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.
Schoof
Sebastian
S
Technische Universität Dortmund, Fakultät Chemie, Otto-Hahn-Str. 6, D-44227 Dortmund, Germany.
Arndt
Hans-Dieter
HD
D000900:Anti-Bacterial Agents / Q000096:biosynthesis; D003545:Cysteine; D019998:Racemases and Epimerases / Q000378:metabolism*; D013883:Thiostrepton / Q000096:biosynthesis* / Q000737:chemistry
D000900:Anti-Bacterial Agents; D019998:Racemases and Epimerases; D013883:Thiostrepton; D003545:Cysteine