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Backbone and side chain chemical shift assignment of diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris, an organophosphorus-degrading enzyme
Biomolecular NMR Assignments ( IF 0.9 ) Pub Date : 2023-02-10 , DOI: 10.1007/s12104-023-10120-y
Julian C-H Chen 1 , Marco Tonelli 2 , Penelope Anderson 1 , Ryszard Michalczyk 1 , Marc-Michael Blum 1, 3 , Robert F Williams 1
Affiliation  

NMR chemical shift assignments are reported for backbone (15N, 1H) and partial side chain (13Cα and β, side chain 1H) atoms of diisopropyl fluorophosphatase (DFPase), a calcium-dependent phosphotriesterase capable of hydrolyzing phosphorus – fluorine bonds in a variety of toxic organophosphorus compounds. Analysis of residues lining the active site of DFPase highlight a number of residues whose chemical shifts can be used as a diagnostic of binding and detection of organophosphorus compounds.



中文翻译:

来自 Loligo vulgaris 的二异丙基氟磷酸酶 (DFPase) 的主链和侧链化学位移分配,一种有机磷降解酶

报告了二异丙基氟磷酸酶 (DFPase) 的主链 ( 15 N, 1 H) 和部分侧链 ( 13 Cα 和 β, 侧链1 H) 原子的 NMR 化学位移分配,DFPase 是一种能够水解磷-氟键的钙依赖性磷酸三酯酶在多种有毒的有机磷化合物中。对排列在 DFPase 活性位点的残基的分析突出了一些残基,这些残基的化学位移可用作有机磷化合物结合和检测的诊断。

更新日期:2023-02-10
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