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Computer-assisted semi-rational design enhanced the enzymatic activity and protein stability of Proteinase K in calcium-free conditions.

Biochemical and biophysical research communications - 20 Aug 2024

Duan Rongdi, Wang Shen, Li Zhetao, Zhang Wenjun, Wu Junteng, Jiang Yifei, Lin Qinting, Yuan Peixiong, Yue Xiaoyan, Yao Yunxiao, Xiao Xiaoyue, Xiao Yunjie, Wang Zefang

Abstract excerpt

Wild-type Proteinase K binds to two Ca2+ ions, which play an important role in regulating enzymaticactivity and maintaining protein stability. Therefore, a predetermined concentration of Ca2+ must be added during the use of Proteinase K, which increases its commercial cost. Herein, we addressed this challenge using a computational strategy to engineer a Proteinase K mutant that does not require Ca2+ and exhibits...

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PMID: 38762932
DOI: 10.1016/j.bbrc.2024.150109

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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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