Novel characteristics of selenomonas ruminantium lysine decarboxylase capable of decarboxylating both L-Lysine and L-Ornithine

Yumiko Takatsuka, Motoko Onoda, Takeyoshi Sugiyama, Koji Muramoto, Toshio Tomita, Yoshiyuki Kamio

    Research output: Contribution to journalArticle

    36 Citations (Scopus)

    Abstract

    Lysine decarboxylase (LDC; EC 4.1.1.18) of Selenomonas ruminantium is a constitutive enzyme and is involved in the synthesis of cadaverine, which is an essential constituent of the peptidoglycan for normal cell growth. We purified the S. ruminantium LDC by an improved method including hydrophobic chromatography and studied the fine characteristics of the enzyme. Kinetic study of LDC showed that S. ruminanitum LDC decarboxylated both L-lysine and L-ornithine with similar Km and the decarboxylase activities towards both substrates were competitively and irreversibly inhibited by DL-α-difluoromethylornithine, which is a specific inhibitor of ornithine decarboxylase (EC 4.1.1.17). We also showed a drastic descent of LDC activity owing to the degradation of LDC at entry into the stationary phase of cell growth.

    Original languageEnglish
    Pages (from-to)1063-1069
    Number of pages7
    JournalBioscience, Biotechnology and Biochemistry
    Volume63
    Issue number6
    DOIs
    Publication statusPublished - 1999 Jan 1

    Keywords

    • DL-α-difluoromethyllysine
    • DL-α-difluoromethylornithine
    • Lysine decarboxylase
    • Ornithine decarboxylase
    • Selenomonas ruminantium

    ASJC Scopus subject areas

    • Biotechnology
    • Analytical Chemistry
    • Biochemistry
    • Applied Microbiology and Biotechnology
    • Molecular Biology
    • Organic Chemistry

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