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Crystal structure of the adenylation domain from an ε-poly-l-lysine synthetase provides molecular mechanism for substrate specificity.
Okamoto, Takaki; Yamanaka, Kazuya; Hamano, Yoshimitsu; Nagano, Shingo; Hino, Tomoya.
Affiliation
  • Okamoto T; Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori, 680-8552, Japan.
  • Yamanaka K; Department of Life Science & Technology, Kansai University, Osaka, 564-8680, Japan; Graduate School of Science and Engineering, Kansai University, Osaka, 564-8680, Japan.
  • Hamano Y; Department of Bioscience, Fukui Prefectural University, Fukui, 910-1195, Japan.
  • Nagano S; Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori, 680-8552, Japan; Centre for Research on Green Sustainable Chemistry, Tottori University, Tottori, 680-8552, Japan.
  • Hino T; Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori, 680-8552, Japan; Centre for Research on Green Sustainable Chemistry, Tottori University, Tottori, 680-8552, Japan. Electronic address: t_hino@tottori-u.ac.jp.
Biochem Biophys Res Commun ; 596: 43-48, 2022 03 12.
Article in En | MEDLINE | ID: mdl-35108653
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Full text: 1 Database: MEDLINE Main subject: Peptide Synthases / Polylysine / Streptomyces / Bacterial Proteins / Adenosine Monophosphate Type of study: Prognostic_studies Language: En Year: 2022 Type: Article
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Full text: 1 Database: MEDLINE Main subject: Peptide Synthases / Polylysine / Streptomyces / Bacterial Proteins / Adenosine Monophosphate Type of study: Prognostic_studies Language: En Year: 2022 Type: Article