[P001] Poster

12:10 PM - 1:00 PM JST(3:10 AM - 4:00 AM UTC)

[P01-073] Biosynthetic study of ST analogue possessing O-acylpeptide side chain

○Kotone Yasuhara¹, Kanki Matsuda¹, Yoshitaka Moriwaki², Yasushi Ogasawara³, Fumihito Hasebe¹, Kazuo Shin-ya⁴, Tohru Dairi³, Yoshimitsu Hamano¹, Chitose Maruyama¹ (1. Fukui Prefectural University (Japan), 2. Science Tokyo (Japan), 3. Hokkaido University (Japan), 4. AIST (Japan))

Keywords:

antibiotics,biosynthesis,Streptomyces

SF-2111B has a unique O-acylpeptide side chain consisting of Ser, methylmalonate (Memal), and Ala. ^[1] It is reported that the antifungal activity of SF-2111B is greater than that of SF-701. Therefore, the O-acylpeptide side chain is important for the antibiotic activity of this compound. To know the biosynthetic pathway of the O-acylpeptide side chain, we identified the SF-2111B biosynthetic gene cluster by the draft genome sequence. In the heterologous expression experiment, we observed the production of SF-2111B, demonstrating that the gene cluster is involved in the biosynthesis of the O-acylpeptide side chain. Recently, we demonstrated that two NRPS enzymes, Orf1197 and Orfl198, and Orf1196 (asparagine synthase) catalyzed the formation of O-acylpeptide moiety on the thiolation domain of Orf1198. We are now investigating the active site of Orf1196 using structural modeling analysis.

References [1] Y. Kondo, et. al., Sci. Reports of Meiji Seika Kaisha, No. 24, 15-26 (1985).