Article
Theoretical Studies on Catalysis Mechanisms of Serum Paraoxonase 1 and Phosphotriesterase Diisopropyl Fluorophosphatase Suggest the Alteration of Substrate Preference from Paraoxonase to DFP.
Molecules (Basel, Switzerland) - 7 Jul 2018
Zhang Hao, Yang Ling, Ma Ying-Ying, Zhu Chaoyuan, Lin Shenghsien, Liao Rong-Zhen
Abstract excerpt
The calcium-dependent β-propeller proteins mammalian serum paraoxonase 1 (PON1) and phosphotriesterase diisopropyl fluorophosphatase (DFPase) catalyze the hydrolysis of organophosphorus compounds and enhance hydrolysis of various nerve agents. In the present work, the phosphotriesterase activity development between PON1 and DFPase was investigated by using the hybrid density functional theory method B3LYP....
Topics
- Animals
- Aryldialkylphosphatase
- Biocatalysis
- Calcium
- Catalytic Domain
- Evolution, Molecular
- Humans
- Hydrogen Bonding
- Mammals
- Mutation
- Organophosphorus Compounds