Improvement of the activity and thermostability of l-threonine aldolase from Pseudomonas putida via tailoring of the active sites lining the binding pocket
Author:
Funder
National Natural Science Foundation of China
Publisher
Springer Science and Business Media LLC
Subject
Microbiology,Applied Microbiology and Biotechnology,Biochemistry, Genetics and Molecular Biology (miscellaneous),Food Science
Link
https://link.springer.com/content/pdf/10.1007/s43393-023-00171-6.pdf
Reference27 articles.
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3. Rocha JF, Pina AF, Sousa SF. PLP-dependent enzymes as important biocatalysts for the pharmaceutical, chemical and food industries: a structural and mechanistic perspective. Catal Sci Technol. 2019;9(18):4864–76.
4. Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H. Diversity of microbial threonine aldolases and their application. J Mol Catal B Enzym. 2000;10(1–3):107–15.
5. Zhao GH, Li H, Liu W, Zhang WG, Zhang F, Liu Q. Preparation of optically active beta-hydroxy-alpha-amino acid by immobilized Escherichia coli cells with serine hydroxymethyl transferase activity. Amino Acids. 2011;40(1):215–20.
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