P450-mediated dehydrotyrosine formation during WS9326 biosynthesis proceeds via dehydrogenation of a specific acylated dipeptide substrate

• Main Authors: Songya Zhang (Author), Lin Zhang (Author), Anja Greule (Author), Julien Tailhades (Author), Edward Marschall (Author), Panward Prasongpholchai (Author), Daniel J. Leng (Author), Jingfan Zhang (Author), Jing Zhu (Author), Joe A. Kaczmarski (Author), Ralf B. Schittenhelm (Author), Oliver Einsle (Author), Colin J. Jackson (Author), Fabrizio Alberti (Author), Andreas Bechthold (Author), Youming Zhang (Author), Manuela Tosin (Author), Tong Si (Author), Max J. Cryle (Author)
• Format: Book
• Published: Elsevier, 2023-08-01T00:00:00Z.
• Subjects: article
• Online Access: Connect to this object online.

WS9326A is a peptide antibiotic containing a highly unusual N-methyl-E-2-3-dehydrotyrosine (NMet-Dht) residue that is incorporated during peptide assembly on a non-ribosomal peptide synthetase (NRPS). The cytochrome P450 encoded by sas16 (P450Sas) has been shown to be essential for the formation of...