Monitoring of phosphatase and kinase activity using P NMR spectroscopy

Traditionally, enzymatic assays require the addition of labels or exogenous supplementation sources. Phosphorus-31 nuclear magnetic resonance ( 31 P NMR) spectroscopy has proven to be a powerful and reliable tool, but it is scarcely employed to evaluate enzymatic activity. Herein, we provide a versa...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:New journal of chemistry 2023-09, Vol.47 (35), p.16631-16635
Hauptverfasser: Guo, Xiaofan, Han, Bowen, Qiu, Wenhan, Deng, Peiran, Fu, Songsen, Ying, Jianxi, Zhao, Yufen
Format: Artikel
Sprache:eng
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 16635
container_issue 35
container_start_page 16631
container_title New journal of chemistry
container_volume 47
creator Guo, Xiaofan
Han, Bowen
Qiu, Wenhan
Deng, Peiran
Fu, Songsen
Ying, Jianxi
Zhao, Yufen
description Traditionally, enzymatic assays require the addition of labels or exogenous supplementation sources. Phosphorus-31 nuclear magnetic resonance ( 31 P NMR) spectroscopy has proven to be a powerful and reliable tool, but it is scarcely employed to evaluate enzymatic activity. Herein, we provide a versatile method to directly characterize phosphatase and kinase activities by exploiting the apparently differential 31 P NMR shifts between substrates and products, without requiring tags or additional reagents. The utility of this method for inhibitor identification is also presented. We provide a new method for the direct identification of enzyme activity based on signal changes of phosphorus-containing small molecules in 31 P NMR spectroscopy.
doi_str_mv 10.1039/d3nj00642e
format Article
fullrecord <record><control><sourceid>rsc</sourceid><recordid>TN_cdi_rsc_primary_d3nj00642e</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>d3nj00642e</sourcerecordid><originalsourceid>FETCH-LOGICAL-r92t-30887db0637a008ad0a533c9da617e02b2dd056983dd748de92302097e5165f43</originalsourceid><addsrcrecordid>eNpFj0tLAzEURoMoWKsb90L-wOhNbh6TpRRrhVZFui_pJGPjIxmSKMy_tz7A1XcWhwMfIecMLhmguXIYXwCU4P6ATBgq0xiu2OGemRANSKGOyUkpe4cxrdiEzFcphppyiM809XTYpTLsbLXFUxsdfQ3xB7saPkMd6Uf5Fh_p_eqJlsF3NafSpWE8JUe9fSv-7G-nZD2_Wc8WzfLh9m52vWyy4bVBaFvttqBQW4DWOrASsTPOKqY98C13DqQyLTqnReu84QgcjPaSKdkLnJKL32wu3WbI4d3mcfP_Gb8AOXVJ-Q</addsrcrecordid><sourcetype>Publisher</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Monitoring of phosphatase and kinase activity using P NMR spectroscopy</title><source>Royal Society Of Chemistry Journals 2008-</source><source>Alma/SFX Local Collection</source><creator>Guo, Xiaofan ; Han, Bowen ; Qiu, Wenhan ; Deng, Peiran ; Fu, Songsen ; Ying, Jianxi ; Zhao, Yufen</creator><creatorcontrib>Guo, Xiaofan ; Han, Bowen ; Qiu, Wenhan ; Deng, Peiran ; Fu, Songsen ; Ying, Jianxi ; Zhao, Yufen</creatorcontrib><description>Traditionally, enzymatic assays require the addition of labels or exogenous supplementation sources. Phosphorus-31 nuclear magnetic resonance ( 31 P NMR) spectroscopy has proven to be a powerful and reliable tool, but it is scarcely employed to evaluate enzymatic activity. Herein, we provide a versatile method to directly characterize phosphatase and kinase activities by exploiting the apparently differential 31 P NMR shifts between substrates and products, without requiring tags or additional reagents. The utility of this method for inhibitor identification is also presented. We provide a new method for the direct identification of enzyme activity based on signal changes of phosphorus-containing small molecules in 31 P NMR spectroscopy.</description><identifier>ISSN: 1144-0546</identifier><identifier>EISSN: 1369-9261</identifier><identifier>DOI: 10.1039/d3nj00642e</identifier><language>eng</language><ispartof>New journal of chemistry, 2023-09, Vol.47 (35), p.16631-16635</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids></links><search><creatorcontrib>Guo, Xiaofan</creatorcontrib><creatorcontrib>Han, Bowen</creatorcontrib><creatorcontrib>Qiu, Wenhan</creatorcontrib><creatorcontrib>Deng, Peiran</creatorcontrib><creatorcontrib>Fu, Songsen</creatorcontrib><creatorcontrib>Ying, Jianxi</creatorcontrib><creatorcontrib>Zhao, Yufen</creatorcontrib><title>Monitoring of phosphatase and kinase activity using P NMR spectroscopy</title><title>New journal of chemistry</title><description>Traditionally, enzymatic assays require the addition of labels or exogenous supplementation sources. Phosphorus-31 nuclear magnetic resonance ( 31 P NMR) spectroscopy has proven to be a powerful and reliable tool, but it is scarcely employed to evaluate enzymatic activity. Herein, we provide a versatile method to directly characterize phosphatase and kinase activities by exploiting the apparently differential 31 P NMR shifts between substrates and products, without requiring tags or additional reagents. The utility of this method for inhibitor identification is also presented. We provide a new method for the direct identification of enzyme activity based on signal changes of phosphorus-containing small molecules in 31 P NMR spectroscopy.</description><issn>1144-0546</issn><issn>1369-9261</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid/><recordid>eNpFj0tLAzEURoMoWKsb90L-wOhNbh6TpRRrhVZFui_pJGPjIxmSKMy_tz7A1XcWhwMfIecMLhmguXIYXwCU4P6ATBgq0xiu2OGemRANSKGOyUkpe4cxrdiEzFcphppyiM809XTYpTLsbLXFUxsdfQ3xB7saPkMd6Uf5Fh_p_eqJlsF3NafSpWE8JUe9fSv-7G-nZD2_Wc8WzfLh9m52vWyy4bVBaFvttqBQW4DWOrASsTPOKqY98C13DqQyLTqnReu84QgcjPaSKdkLnJKL32wu3WbI4d3mcfP_Gb8AOXVJ-Q</recordid><startdate>20230911</startdate><enddate>20230911</enddate><creator>Guo, Xiaofan</creator><creator>Han, Bowen</creator><creator>Qiu, Wenhan</creator><creator>Deng, Peiran</creator><creator>Fu, Songsen</creator><creator>Ying, Jianxi</creator><creator>Zhao, Yufen</creator><scope/></search><sort><creationdate>20230911</creationdate><title>Monitoring of phosphatase and kinase activity using P NMR spectroscopy</title><author>Guo, Xiaofan ; Han, Bowen ; Qiu, Wenhan ; Deng, Peiran ; Fu, Songsen ; Ying, Jianxi ; Zhao, Yufen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-r92t-30887db0637a008ad0a533c9da617e02b2dd056983dd748de92302097e5165f43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Guo, Xiaofan</creatorcontrib><creatorcontrib>Han, Bowen</creatorcontrib><creatorcontrib>Qiu, Wenhan</creatorcontrib><creatorcontrib>Deng, Peiran</creatorcontrib><creatorcontrib>Fu, Songsen</creatorcontrib><creatorcontrib>Ying, Jianxi</creatorcontrib><creatorcontrib>Zhao, Yufen</creatorcontrib><jtitle>New journal of chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Guo, Xiaofan</au><au>Han, Bowen</au><au>Qiu, Wenhan</au><au>Deng, Peiran</au><au>Fu, Songsen</au><au>Ying, Jianxi</au><au>Zhao, Yufen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Monitoring of phosphatase and kinase activity using P NMR spectroscopy</atitle><jtitle>New journal of chemistry</jtitle><date>2023-09-11</date><risdate>2023</risdate><volume>47</volume><issue>35</issue><spage>16631</spage><epage>16635</epage><pages>16631-16635</pages><issn>1144-0546</issn><eissn>1369-9261</eissn><abstract>Traditionally, enzymatic assays require the addition of labels or exogenous supplementation sources. Phosphorus-31 nuclear magnetic resonance ( 31 P NMR) spectroscopy has proven to be a powerful and reliable tool, but it is scarcely employed to evaluate enzymatic activity. Herein, we provide a versatile method to directly characterize phosphatase and kinase activities by exploiting the apparently differential 31 P NMR shifts between substrates and products, without requiring tags or additional reagents. The utility of this method for inhibitor identification is also presented. We provide a new method for the direct identification of enzyme activity based on signal changes of phosphorus-containing small molecules in 31 P NMR spectroscopy.</abstract><doi>10.1039/d3nj00642e</doi><tpages>5</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1144-0546
ispartof New journal of chemistry, 2023-09, Vol.47 (35), p.16631-16635
issn 1144-0546
1369-9261
language eng
recordid cdi_rsc_primary_d3nj00642e
source Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection
title Monitoring of phosphatase and kinase activity using P NMR spectroscopy
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-17T17%3A47%3A19IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-rsc&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Monitoring%20of%20phosphatase%20and%20kinase%20activity%20using%20P%20NMR%20spectroscopy&rft.jtitle=New%20journal%20of%20chemistry&rft.au=Guo,%20Xiaofan&rft.date=2023-09-11&rft.volume=47&rft.issue=35&rft.spage=16631&rft.epage=16635&rft.pages=16631-16635&rft.issn=1144-0546&rft.eissn=1369-9261&rft_id=info:doi/10.1039/d3nj00642e&rft_dat=%3Crsc%3Ed3nj00642e%3C/rsc%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true