嗜 Alteromonas 菌 JD6.5 中有机磷酸酸酐酶对 p-硝基苯基磷酸三酯的底物及立体化学特异性
Substrate and stereochemical specificity of the organophosphorus acid anhydrolase from Alteromonas sp. JD6.5 toward p-nitrophenyl phosphotriesters.
作者信息
Hill C M, Wu F, Cheng T C, DeFrank J J, Raushel F M
机构信息
Department of Chemistry, Texas A&M University, College Station 77843, USA.
出版信息
Bioorg Med Chem Lett. 2000 Jun 5;10(11):1285-8. doi: 10.1016/s0960-894x(00)00213-4.
Abstract
The enzyme OPAA hydrolyzes p-nitrophenyl phosphotriesters bearing substituents at the phosphorus center ranging in size from methyl to phenyl. The enzyme exhibits stereoselectivity toward the hydrolysis of chiral substrates with a preference for the Sp enantiomer.
摘要
OPAA酶可水解磷中心带有从甲基到苯基不同大小取代基的对硝基苯基磷酸三酯。该酶对手性底物的水解表现出立体选择性，优先选择Sp对映体。
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