Development of a recombinant ε-poly-L-lysine synthetase expression system to perform mutational analysis(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

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概要

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• ε-Poly-L-lysine (ε-PL) synthetase (Pls), which is a membrane protein with adenylation and thiolation domains characteristic of the nonribosomal peptide synthetases, catalyzes polymerization of L-lysine molecules (25-mer to 35-mer). Here, we report on the development of a recombinant Pls expression system that allowed us to perform a site-directed mutational analysis.

• 公益社団法人日本生物工学会の論文

著者

• Hamano Yoshimitsu

  Department Of Bioscience Fukui Prefectural University

• Hamano Yoshimitsu

  Department Of Biological Sciences The Nishi Tokyo University

• Kito Naoko

  Department Of Bioscience Fukui Prefectural University

• Maruyama Chitose

  Department Of Bioscience Fukui Prefectural University

• Yamanaka Kazuya

  Yokohama Research Center Chisso Corporation

• Kita Akihiro

  Department of Bioscience, Fukui Prefectural University

• Imokawa Yuuki

  Department of Bioscience, Fukui Prefectural University

• Utagawa Takashi

  Department of Bioscience, Fukui Prefectural University

• Imokawa Yuuki

  Department Of Bioscience Fukui Prefectural University

• Utagawa Takashi

  Department Of Bioscience Fukui Prefectural University

• Kita Akihiro

  Department Of Bioscience Fukui Prefectural University

関連論文

• MOLECULAR CLONING OF THE PROMOTER REGION OF CHERRY SALMON INSULIN-LIKE GROWTH FACTOR I(IGF-I)GENE
• Development of Gene Delivery Systems for the ε-Poly-L-Lysine Producer, Streptomyces albulus(Genetics, Molecular Biology, and Gene Engineering)
• Overexpression and Characterization of an Aminoglycoside 6'-N-Acetyltransferase with Broad Specificity from an ε-Poly-L-lysine Producer, Streptomyces albulus IFO14147
• Construction of a Knockout Mutant of the Streptothricin-Resistance Gene in Streptomyces albulus by Electroporation
• Development of a recombinant ε-poly-L-lysine synthetase expression system to perform mutational analysis(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
• The Biological Function of the Bacterial Isochorismatase-Like Hydrolase SttH
• Occurrence, Biosynthesis, Biodegradation, and Industrial and Medical Applications of a Naturally Occurring ε-Poly-L-lysine
• Mutational analysis of the three tandem domains of ε-poly-L-lysine synthetase catalyzing the L-lysine polymerization reaction(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

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