Award review: Exploring the biosynthesis of natural products and their inherent suitability for the rational design of desirable compounds through genetic engineering

• 資料種別: 記事
• タイトル: Award review: Exploring the biosynthesis of natural products and their inherent suitability for the rational design of desirable compounds through genetic engineering
• 著者・編者: Kenji Watanabe
• 著者標目: Kenji Watanabe
• タイトル（掲載誌）: Bioscience, Biotechnology, and Biochemistry
• 巻号年月日等（掲載誌）: 72(10) (通号 829) 2008.10
• 掲載巻: 72
• 掲載号: 10
• 掲載通号: 829
• 掲載ページ: 2491～2506
• 掲載年月日（W3CDTF）: 2008-10
• ISSN（掲載誌）: 0916-8451
• ISSN-L（掲載誌）: 0916-8451
• 出版事項（掲載誌）: Tokyo : Japan Society for Bioscience
• 出版地（国名コード）: JP
• 本文の言語コード: eng
• 件名標目: Diels-Alder reaction; biosynthesis; polyketide synthase; nonribosomal peptide synthetase; de novo production
• NDLC: ZR7
• 対象利用者: 一般
• 所蔵機関: 国立国会図書館
• 請求記号: Z53-G223
• 連携機関・データベース: 国立国会図書館 : 国立国会図書館雑誌記事索引; https://ndlsearch.ndl.go.jp
• 書誌ID（NDLBibID）: 9696830; http://id.ndl.go.jp/bib/9696830
• 整理区分コード: 632

• 要約等: Much effort has been invested in studying how natural products are biosynthesized, and great advances have been made in understanding how these compounds acquire their structural complexity and biological activities. In recent years, significant progress has been made due to the devoted efforts of scientists in this field and to technological advancements. Numerous details, applications, and innovative findings have been elucidated by scientists using biochemical, genetic, and molecular biological approaches. Here I present a comprehensive overview of highly valued biosynthetic proteins, polyketide synthase and nonribosomal peptide synthetase. I begin with “Diels-Alderase” a captivating enzyme that has the ability to catalyze a Diels-Alder reaction valued by chemists for its usefulness in chemical synthesis. A handful of these enzymes have been characterized and chemically authenticated. The most well understood enzyme of this category is macrophomate synthase. Secondly, I focus on the polyketide and nonribosomal peptide biosynthetic pathways and the enzyme assembly for producing its metabolite. Many important natural products are produced by this biosynthetic pathway as secondary metabolites, such as erythromycin, rifamycin, and FK520, as antibiotics and an immunosuppressive, respectively. I conclude with a discussion of nonribosomal peptides and their mechanistic pathways. Special attention will be devoted to <I>de novo</I> production of echinomycin in a heterologous manner, the earliest example of totally engineered biosynthesis of the biologically active form of a nonribosomal peptide host in <I>Escherichia coli</I>.
• DOI: 10.1271/bbb.80323
• オンライン閲覧公開範囲: インターネット公開
• 連携機関・データベース: 科学技術振興機構 : J-STAGE; http://www.jstage.jst.go.jp

• 要約等: Much effort has been invested in studying how natural products are biosynthesized, and great advances have been made in understanding how these compounds acquire their structural complexity and biological activities. In recent years, significant progress has been made due to the devoted efforts of scientists in this field and to technological advancements. Numerous details, applications, and innovative findings have been elucidated by scientists using biochemical, genetic, and molecular biological approaches. Here I present a comprehensive overview of highly valued biosynthetic proteins, polyketide synthase and nonribosomal peptide synthetase. I begin with “Diels-Alderase” a captivating enzyme that has the ability to catalyze a Diels-Alder reaction valued by chemists for its usefulness in chemical synthesis. A handful of these enzymes have been characterized and chemically authenticated. The most well understood enzyme of this category is macrophomate synthase. Secondly, I focus on the polyketide and nonribosomal peptide biosynthetic pathways and the enzyme assembly for producing its metabolite. Many important natural products are produced by this biosynthetic pathway as secondary metabolites, such as erythromycin, rifamycin, and FK520, as antibiotics and an immunosuppressive, respectively. I conclude with a discussion of nonribosomal peptides and their mechanistic pathways. Special attention will be devoted to <I>de novo</I> production of echinomycin in a heterologous manner, the earliest example of totally engineered biosynthesis of the biologically active form of a nonribosomal peptide host in <I>Escherichia coli</I>.
• DOI: 10.1271/bbb.80323; https://doi.org/10.1271/bbb.80323
• 関連情報（URI）: http://id.ndl.go.jp/bib/9696830; https://ndlsearch.ndl.go.jp/books/R000000004-I9696830; http://www.tandfonline.com/doi/pdf/10.1271/bbb.80323
• 連携機関・データベース: 国立情報学研究所 : CiNii Research; https://cir.nii.ac.jp/
• 提供元機関・データベース: Japan Link Center; https://japanlinkcenter.org/top; 雑誌記事索引データベース; https://ndlsearch.ndl.go.jp; Crossref; https://www.crossref.org; CiNii Articles
• 書誌ID（NDLBibID）: 9696830; http://id.ndl.go.jp/bib/9696830
• NII論文ID: 10027532465