Backbone and side chain chemical shift assignment of diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris, an organophosphorus-degrading enzyme

IF 0.8 4区生物学 Q4 BIOPHYSICS

Biomolecular NMR Assignments Pub Date : 2023-02-10 DOI:10.1007/s12104-023-10120-y

Julian C.-H. Chen, Marco Tonelli, Penelope Anderson, Ryszard Michalczyk, Marc-Michael Blum, Robert F. Williams

引用次数: 0

Abstract

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.

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有机磷降解酶Loligo vulgaris二异丙基氟磷酸酶(DFPase)的主链和侧链化学移位配位

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，报道了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。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Biomolecular NMR Assignments 生物-光谱学

CiteScore

1.70

自引率

11.10%

发文量

审稿时长

6-12 weeks

期刊介绍： Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.