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Article

Thermostability and activity improvement in l-threonine aldolase through targeted mutations in V-shaped subunit.

International journal of biological macromolecules - 1 Oct 2024

Fang Sai, Wang Zhe, Xiao Lanxin, Meng Yan, Lei Yixuan, Liang Tianxin, Chen Yuhuan, Zhou Xiaoshu, Xu Gang, Yang Lirong, Zheng Wenlong, Wu Jianping

Abstract excerpt

l-threonine aldolase (LTA) catalyzes the synthesis of β-hydroxy-α-amino acids, which are important chiral intermediates widely used in the fields of pharmaceuticals and pesticides. However, the limited thermostability of LTA hinders its industrial application. Furthermore, the trade-off between thermostability and activity presents a challenge in the thermostability engineering of this enzyme. This study proposes...

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PMID: 39181367
DOI: 10.1016/j.ijbiomac.2024.134994

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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