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Article

Multiscale Simulations Reveal Distal Allosteric Reprogramming of Pocket Dynamics and Dual Hydrolytic Pathways in Engineered Methyl Parathion Hydrolase.

The journal of physical chemistry. B - 7 May 2026

Liu Xiaoyuan, Fu Yuzhuang, Yu Jun, Lv Nan, Zhang Zhiyang, Zhao Yuan, Si Yubing, Cao Zexing

Abstract excerpt

Methyl parathion hydrolase (MPH) is an important organophosphorus (OP) detoxifying enzyme, yet achieving a balance between catalytic activity and thermostability remains a major challenge. Notably, two engineered MPH variants, MPHase-m5a and MPHase-m5b, achieve this balance through predominantly distal substitutions, yet the underlying mechanisms remain unclear. Understanding how such remote mutations...

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Identifiers

PMID: 42045117
DOI: 10.1021/acs.jpcb.6c01732

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