Structure-Based Modification of<scp>D</scp>-Alanine-<scp>D</scp>-Alanine Ligase from<i>Thermotoga maritima</i>ATCC 43589 for Depsipeptide Synthesis

• NAKAGAWA Tomoki

  Department of Applied Chemistry, School of Advanced Science and Engineering, Faculty of Science and Engineering, Waseda University

• SATAKE Ryoko

  Department of Applied Chemistry, School of Advanced Science and Engineering, Faculty of Science and Engineering, Waseda University

• SATO Masaru

  Department of Applied Chemistry, School of Advanced Science and Engineering, Faculty of Science and Engineering, Waseda University

• KINO Kuniki

  Department of Applied Chemistry, School of Advanced Science and Engineering, Faculty of Science and Engineering, Waseda University

書誌事項

タイトル別名

• Structure-Based Modification of D-Alanine-D-Alanine Ligase from Thermotoga maritima ATCC 43589 for Depsipeptide Synthesis

抄録

Depsipeptides are peptide-like polymers consisting of amino acids and hydroxy acids, and are expected to be new functional materials for drug-delivery systems and polymer science. In our previous study, D-alanyl-D-lactate, a type of depsipeptide, was enzymatically synthesized using D-alanine-D-alanine ligase from Thermotoga maritima ATCC 43589 (TmDdl) by Y207F substitution. Thereafter, in this study, further mutagenesis was introduced, based on structural comparison between TmDdl and a well-characterized D-alanine-D-alanine ligase from Escherichia coli. The S137A/Y207F mutant showed higher D-alanyl-D-lactate and lower D-alanyl-D-alanine synthesizing activity than the Y207F mutant. This suggests that substitution at the S137 residue contributes to product selectivity. Saturated mutagenesis on S137 revealed that the S137G/Y207F mutant showed the highest D-alanyl-D-lactate synthesizing activity. Moreover, the mutant showed broad substrate specificity toward D-amino acid and recognized D-lactate and D,L-isoserine as substrates. On the basis of these characteristics, various depsipeptides can be produced using S137G/Y207F-replaced TmDdl.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 75 (4), 700-704, 2011

  公益社団法人 日本農芸化学会

キーワード

• depsipeptide
• dipeptide
• <small>D</small>-alanine-<small>D</small>-alanine ligase
• <I>Thermotoga maritima</I>
• enzymatic peptide synthesis

詳細情報

• CRID: 1390282681453662080
• NII論文ID: 10028271514
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.100832
• ISSN: 13476947
• ISSN: 09168451
• NDL書誌ID: 11070986
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I11070986
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.100832
• 本文言語コード: en
• データソース種別:
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  • NDL
  • Crossref
  • CiNii Articles
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