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Enhancing the thermal stability of L-threonine dehydrogenase through computational-driven combinatorial mutagenesis.

International journal of biological macromolecules - 1 Feb 2026

Zhang Xichuan, Bai Xueyang, Fu Muran, Shi Hongling, Dong Zixing, Gao Wenchao, Li Dandan, Yao Lunguang, Jia Dianyong, Tang Cunduo

Abstract excerpt

L-Threonine dehydrogenases (L-TDHs) are crucial industrial enzymes that catalyze the dehydrogenation of L-threonine to produce L-2-aminoethyl acetate, demonstrating significant application value in the food additive and pharmaceutical industries. Although L-threonine dehydrogenase derived from Escherichia coli (EcTDH) exhibits high catalytic efficiency, its poor thermal stability limits its widespread industrial...

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Alcohol Oxidoreductases
Amino Acid Oxidoreductases
Enzyme Stability
Escherichia coli
Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Engineering

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PMID: 41547509
DOI: 10.1016/j.ijbiomac.2026.150276

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

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