Phosphotriesterase: An Enzyme in Search of Its Natural Substrate
作者： Frank M. Raushel , Hazel M. Holden
DOI: 10.1002/9780470123201.CH2
关键词: Stereochemistry 、 Bond cleavage 、 Paraoxon 、 Conformational change 、 Hydroxide 、 Substrate (chemistry) 、 Hydrolysis 、 Enzyme 、 Chemistry 、 Active site
摘要: The bacterial PTE is able to catalyze the hydrolysis of a wide range organophosphate nerve agents. active site has been shown consist unique binuclear metal center that evolved deliver hydroxide bond cleavage. reaction rate for activated substrates such as paraoxon limited by product release or an associated protein conformational change.
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