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...
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Veröffentlicht in: | New journal of chemistry 2023-09, Vol.47 (35), p.16631-16635 |
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container_issue | 35 |
container_start_page | 16631 |
container_title | New journal of chemistry |
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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 |
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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
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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> |
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source | Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
title | Monitoring of phosphatase and kinase activity using P NMR spectroscopy |
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