Structure-Based Modification of D-Alanine-D-Alanine Ligase from Thermotoga maritima ATCC 43589 for Depsipeptide Synthesis
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- NAKAGAWA Tomoki
- Department of Applied Chemistry, School of Advanced Science and Engineering, Faculty of Science and Engineering, Waseda University
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- SATAKE Ryoko
- Department of Applied Chemistry, School of Advanced Science and Engineering, Faculty of Science and Engineering, Waseda University
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- SATO Masaru
- Department of Applied Chemistry, School of Advanced Science and Engineering, Faculty of Science and Engineering, Waseda University
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- KINO Kuniki
- Department of Applied Chemistry, School of Advanced Science and Engineering, Faculty of Science and Engineering, Waseda University
Bibliographic Information
- Other Title
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- Structure-Based Modification of<scp>D</scp>-Alanine-<scp>D</scp>-Alanine Ligase from<i>Thermotoga maritima</i>ATCC 43589 for Depsipeptide Synthesis
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Abstract
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.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 75 (4), 700-704, 2011
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Keywords
Details 詳細情報について
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- CRID
- 1390282681453662080
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- NII Article ID
- 10028271514
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- NII Book ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 11070986
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed