Studies on the reaction specificity of the flavoprotein lysine monooxygenase with modified substrates

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Abstract

Various modified substrates of lysine monooxygenase were examined to determine whether they were oxygenated or oxidized. Among various methyllysines tested, Nϵ- and δ-methyllysine underwent predominantly an oxygenative decarboxylation, producing the corresponding acid amides, while γ-methyllysine underwent predominantly an oxidative deamination with an α-keto acid as the reaction product. β-Methyllysine was inactive as substrate. All four methyllysines decreased the cooperativity of the enzyme with the normal substrate, lysine. Furthermore, lysine oxygenation was competitively inhibited by all of them except for β-methyllysine, which was much less inhibitory than the other methyllysines. Other analogs with a chloro or hydroxyl group at either the δ or the γ position were both oxygenated and oxidized. Analogs with a modified carboxyl or α-amino group were inactive as substrates.

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Cited by (4)

  • Flavoprotein monooxygenases: Versatile biocatalysts

    2021, Biotechnology Advances
    Citation Excerpt :

    They have been proposed to use enzyme-bound hydrogen peroxide for the monooxygenation of the intermediate product, generated during the reductive half-reaction (Fig. 10) (Lockridge et al., 1972; Ralph et al., 2006). Group G enzymes catalyze oxygenative decarboxylation reactions of several amino acids such as arginine (AMO; EC 1.13.12.1 (van Thoai and Olomucki, 1962a, 1962b)), lysine (LMO; EC 1.13.12.2; Fig. 10a) (Ohnishi et al., 1976)), tryptophan (TMO; EC 1.13.12.3 (Gaweska et al., 2013)) and phenylalanine (PAO; EC 1.13.12.9; Fig. 10b) (Ida et al., 2008)) to give the corresponding amides. Depending on the amino acid used, group G enzymes can also function as oxidases, thereby converting the intermediate imino acids through oxidative deamination to α-keto acids (Fig. 10a and 10b).

This work has been supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture, Japan, and by a grant from the Tanabe Amino Acid Research Foundation. This is paper IX in a series entitled “Studies on Monooxygenases.” The preceding paper is Ref. (21).

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Present address: Mitsui Petroleum Chemistry Company, Otake, Hiroshima, Japan.

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