LodB is required for the recombinant synthesis of the quinoprotein l-lysine-ε-oxidase from Marinomonas mediterranea
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- 作者：María Dolores Chacón-Verdú (1)
Daniel Gómez (1)
Francisco Solano (2)
Patricia Lucas-Elío (1)
Antonio Sánchez-Amat (1) - 关键词：l ; Lysine ; ε ; oxidase ; Quinoprotein ; Marinomonas mediterranea ; Recombinant protein ; Escherichia coli
- 刊名：Applied Microbiology and Biotechnology
- 出版年：2014
- 出版时间：April 2014
- 年：2014
- 卷：98
- 期：7
- 页码：2981-2989
- 全文大小：677 KB
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Daniel Gómez (1)
Francisco Solano (2)
Patricia Lucas-Elío (1)
Antonio Sánchez-Amat (1)
1. Department of Genetics and Microbiology, University of Murcia, Murcia, 30100, Spain
2. Department of Biochemistry and Molecular Biology B and Immunology, University of Murcia, Murcia, 30100, Spain - ISSN：1432-0614
文摘
Marinomonas mediterranea is a marine gamma-proteobacterium that synthesizes LodA, a novel l-lysine-ε-oxidase (E.C. 1.4.3.20). This enzyme oxidizes L-lysine generating 2-aminoadipate 6-semialdehyde, ammonium, and hydrogen peroxide. Unlike other l-amino acid oxidases, LodA is not a flavoprotein but contains a quinone cofactor. LodA is encoded by an operon with two genes, lodA and lodB. In the native system, LodB is required for the synthesis of a functional LodA. In this study, we report the recombinant expression of LodA in Escherichia coli using vectors that allow its expression and accumulation in the cytoplasm. To reveal the l-lysine-ε-oxidase activity using the Amplex Red method for hydrogen peroxide detection, it is necessary to first remove the E. coli cytoplasmic catalases. The flavoprotein LodB is the only M. mediterranea protein required in the recombinant system for the generation of the cofactor of LodA. In the absence of LodB, LodA does not contain the quinone cofactor and remains in an inactive form. The results presented indicate that LodB participates in the posttranslational modification of LodA that generates the quinone cofactor.