Enzymatic aminopropylation of certain secondary amines

Article abstract of DOI:10.1248/bpb.18.355

Two unusual aminopropyl acceptors found in a survey of putrescine binding sites of mammalian spermidine synthase, N-methylputrescine (I) and 4-aminomethylpiperidine (II), were examined for their aminopropyl derivatives. Studies under In vitro incubation conditions suggested that the aminopropyl derivatives of the secondary amine of I and II, N⁴-methylspermidine (Is) and 1-N-(3-aminopropyl)-4-aminomethylpiperidine (IIs), and of the primary amine of I and II, N⁸-methy]spermidine (Ip) and 4-[N-(3-aminopropyl)aminomethyl]piperidine (IIp), respectively, were biosynthesized by rat spermidine synthase. Studies on the cell culture system of cultured rat hepatoma (HTC) cells treated with α-difluoromethylornithine, an ornithine decarboxylase inhibitor, clearly showed the presence of Is and Ip when I was administered, and IIs and IIp when II was administered, with no detection of putrescine or spermidine. These results suggested that mammalian spermidine synthase can transfer the anunop}opyl moiety of decarboxylated S-adenosylmethionine to certain secondary amines in living cells.

Full text of DOI:10.1248/bpb.18.355

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NII-Electronic Library Service

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