Backbone and side chain chemical shift assignment of diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris, an organophosphorus-degrading enzyme.
Backbone and side chain chemical shift assignment of diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris, an organophosphorus-degrading enzyme.
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来自 Loligo vulgaris（一种有机磷降解酶）的二异丙基氟磷酸酶 (DFPase) 的主链和侧链化学位移分配。
DOI：
10.1007/s12104-023-10120-y
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发表时间：
2023
影响因子：
0.9
通讯作者：
Williams,RobertF
中科院分区：
文献类型：
--
作者：
Chen,JulianC-H;Tonelli,Marco;Anderson,Penelope;Michalczyk,Ryszard;Blum,Marc-Michael;Williams,RobertF
二异丙基氟磷酸酶（DFPase）是一种钙依赖性磷酸三酯酶，能够水解多种有毒有机磷化合物中的磷-氟键，据报道，DFPase的主链（15N,1H）和部分侧链（13Cα和β，侧链1H）原子的核磁共振化学位移分配。对DFPase活性位点的残基进行分析，发现一些残基的化学位移可以作为有机磷化合物结合的诊断和检测。
NMR chemical shift assignments are reported for backbone (15N,1H) and partial side chain (13Cα and β, side chain1H) 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.