[P001] Poster

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

[P01-081] Study on the biosynthetic mechanism of resormycin

○Kazuma Sasaki¹, Yasushi Ogasawara², Kazuya Yamanaka³, Masayuki Igarashi⁴, Fumihito Hasebe¹, Tohru Dairi², Yoshimitsu Hamano¹, Chitose Maruyama¹ (1. Fukui Prefectural University (Japan), 2. Hokkaido University (Japan), 3. Kansai University (Japan), 4. BIKAKEN (Japan))

Keywords:

antibiotics,biosynthesis,Streptomyces

In our biosynthetic study of β-homolysine (β-hLys) in the antibiotic resormycin (RM), we have previously reported that β-hLys is synthesized from L-Arg via 2-amino-7-guanidino heptanoic acid (AGH). Then we searched for the genes involved in the carbon skeleton rearrangement from L-Arg to AGH and found that Res11 is homologous to 2-isopropylmalate synthase, which catalyzes the condensation reaction between 2-oxo-isovalerate and acetyl-CoA. Given that Res11 would be involved in this carbon chain elongation, we suggested that L-Arg be converted to 2-oxo-Arg and accepted by Res11 as a substrate. Therefore, we focused on the PLP-dependent aminotransferase, Res4, as the only candidate related to the amino group transfer and performed the in vitro reaction using the Res4 recombinant enzyme.
References [1] M. Igarashi et al., J. Antibiot. Tokyo, 50(12): 1020-1025 (1997).