Characterization of three amidinotransferases involved in the biosynthesis of ketomemicins.
We recently reported a novel class of amide bond forming enzymes (peptide ligases) involved in the biosynthesis of pheganomycins, resorcinomycins and ketomemicins. This class of enzymes exclusively utilizes Nα-amidino amino acids as the N-terminal substrate. In this Letter, we characterized three new amidinotransferases involved in the biosynthesis of ketomemicins and showed that l-arginine was the amidino-acceptor of amidinotransferases in both the Micromonospora sp. and Streptomyces mobaraensis clusters, while the Salinispora tropica enzyme recognized l-valine. Unexpectedly, the S. tropica enzyme accepted several different amino acids as amidino acceptors in addition to l-valine. Accordingly, we re-investigated the specific metabolites governed by the gene cluster of S. tropica and identified several minor congeners of ketomemicin C with different N-terminal amidino-amino acids. These results indicate that the amidinotransferase of S. tropica is promiscuous and could be useful to generate new ketomemicin-type natural products.
Graduate School of Engineering, Hokkaido University, N 13 W 8, Kita-ku, Sapporo, Hokkaido 060-8628, Japan. Electronic address: yogasawa@eng.hokudai.ac.jp.
Yasushi
Y
Ogasawara
Graduate School of Engineering, Hokkaido University, N 13 W 8, Kita-ku, Sapporo, Hokkaido 060-8628, Japan.
Michiko
M
Fujimori
Graduate School of Engineering, Hokkaido University, N 13 W 8, Kita-ku, Sapporo, Hokkaido 060-8628, Japan.
Junpei
J
Kawata
Graduate School of Engineering, Hokkaido University, N 13 W 8, Kita-ku, Sapporo, Hokkaido 060-8628, Japan. Electronic address: dairi@eng.hokudai.ac.jp.
Tohru
T
Dairi
D000579:Amidinotransferases / Q000737:chemistry / Q000378:metabolism*; D001688:Biological Products / Q000737:chemistry / Q000378:metabolism*; D015394:Molecular Structure; D009842:Oligopeptides / Q000096:biosynthesis* / Q000737:chemistry
D001688:Biological Products; D009842:Oligopeptides; D000579:Amidinotransferases
Amidinotransferase; Biosynthesis; Ketomemicins; Pseudopeptide