One Assay for All: Exploring Small Molecule Phosphorylation Using Amylose–Polyiodide Complexes
We present a generic method for screening small molecule kinases for their acceptor specificity. The release of the reaction byproduct adenosine diphosphate (ADP) triggers a concentration-dependent formation of amylose from sucrose, by using the combined enzymatic action of sucrose synthase and glyc...
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| Veröffentlicht in: | Analytical chemistry (Washington) 2015-10, Vol.87 (19), p.9546-9550 |
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| container_title | Analytical chemistry (Washington) |
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| creator | Duan, Xu C. Chen, Huan Liu, Fang F. Conway, Louis Wei, Shuang Cai, Zhi P. Liu, Li Voglmeir, Josef |
| description | We present a generic method for screening small molecule kinases for their acceptor specificity. The release of the reaction byproduct adenosine diphosphate (ADP) triggers a concentration-dependent formation of amylose from sucrose, by using the combined enzymatic action of sucrose synthase and glycogen synthase. Kinase activities could be quantified photometrically after the formation of a dark-blue amylose–polyiodide complex. We demonstrate that this method can be used to profile both known and novel nucleotide- and sugar-kinases for their substrate specificity. Using a facile and widely available methodology, the amylose–polyiodide small-molecule kinase assay presented herein has the potential to perform substrate screenings of small molecule kinases in a high-throughput manner. |
| doi_str_mv | 10.1021/acs.analchem.5b02247 |
| format | Article |
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The release of the reaction byproduct adenosine diphosphate (ADP) triggers a concentration-dependent formation of amylose from sucrose, by using the combined enzymatic action of sucrose synthase and glycogen synthase. Kinase activities could be quantified photometrically after the formation of a dark-blue amylose–polyiodide complex. We demonstrate that this method can be used to profile both known and novel nucleotide- and sugar-kinases for their substrate specificity. Using a facile and widely available methodology, the amylose–polyiodide small-molecule kinase assay presented herein has the potential to perform substrate screenings of small molecule kinases in a high-throughput manner.</description><identifier>ISSN: 0003-2700</identifier><identifier>EISSN: 1520-6882</identifier><identifier>DOI: 10.1021/acs.analchem.5b02247</identifier><identifier>PMID: 26308083</identifier><identifier>CODEN: ANCHAM</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Adenosine diphosphate ; Amylose - chemistry ; Amylose - metabolism ; Assaying ; Bioassays ; Byproducts ; Colorimetry ; Formations ; Iodine - chemistry ; Iodine - metabolism ; Kinases ; Molecules ; Phosphorylation ; Phosphotransferases - analysis ; Phosphotransferases - metabolism ; Photometry ; Screening ; Sucrose</subject><ispartof>Analytical chemistry (Washington), 2015-10, Vol.87 (19), p.9546-9550</ispartof><rights>Copyright © 2015 American Chemical Society</rights><rights>Copyright American Chemical Society Oct 6, 2015</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a409t-a4ed56ad424ed4b80dc847419a185152d8b3b020835ecb4ed8a79ee401f592bf3</citedby><cites>FETCH-LOGICAL-a409t-a4ed56ad424ed4b80dc847419a185152d8b3b020835ecb4ed8a79ee401f592bf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/acs.analchem.5b02247$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/acs.analchem.5b02247$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26308083$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Duan, Xu C.</creatorcontrib><creatorcontrib>Chen, Huan</creatorcontrib><creatorcontrib>Liu, Fang F.</creatorcontrib><creatorcontrib>Conway, Louis</creatorcontrib><creatorcontrib>Wei, Shuang</creatorcontrib><creatorcontrib>Cai, Zhi P.</creatorcontrib><creatorcontrib>Liu, Li</creatorcontrib><creatorcontrib>Voglmeir, Josef</creatorcontrib><title>One Assay for All: Exploring Small Molecule Phosphorylation Using Amylose–Polyiodide Complexes</title><title>Analytical chemistry (Washington)</title><addtitle>Anal. Chem</addtitle><description>We present a generic method for screening small molecule kinases for their acceptor specificity. The release of the reaction byproduct adenosine diphosphate (ADP) triggers a concentration-dependent formation of amylose from sucrose, by using the combined enzymatic action of sucrose synthase and glycogen synthase. Kinase activities could be quantified photometrically after the formation of a dark-blue amylose–polyiodide complex. We demonstrate that this method can be used to profile both known and novel nucleotide- and sugar-kinases for their substrate specificity. Using a facile and widely available methodology, the amylose–polyiodide small-molecule kinase assay presented herein has the potential to perform substrate screenings of small molecule kinases in a high-throughput manner.</description><subject>Adenosine diphosphate</subject><subject>Amylose - chemistry</subject><subject>Amylose - metabolism</subject><subject>Assaying</subject><subject>Bioassays</subject><subject>Byproducts</subject><subject>Colorimetry</subject><subject>Formations</subject><subject>Iodine - chemistry</subject><subject>Iodine - metabolism</subject><subject>Kinases</subject><subject>Molecules</subject><subject>Phosphorylation</subject><subject>Phosphotransferases - analysis</subject><subject>Phosphotransferases - metabolism</subject><subject>Photometry</subject><subject>Screening</subject><subject>Sucrose</subject><issn>0003-2700</issn><issn>1520-6882</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkcFO3DAURa2KqgzQP6gqS2zYzPQ9x0mc7kYjoJVAILWsg5O8dIKcOLUnEtnxD_whX4KjGYrUBWJje3HusZ8vY18QFggCv-nSL3SnTbmmdhEXIIRMP7AZxgLmiVJij80AIJqLFGCfHXh_B4AImHxi-yKJQIGKZuz2qiO-9F6PvLaOL435zk_ve2Nd0_3hv1ptDL-0hsrBEL9eW9-vrRuN3jS24zd-gpbtaKynp4fHa2vGxlZNRXxl297QPfkj9rHWxtPn3X7Ibs5Of69-zC-uzn-ulhdzLSHbhJWqONGVFOEgCwVVqWQqMdOo4jBTpYoozBjeHFNZBEbpNCOSgHWciaKODtnJ1ts7-3cgv8nbxpdkjO7IDj7HNBGImMnsHSiqDINaBfT4P_TODi78-kSJYJNCTUK5pUpnvXdU571rWu3GHCGfyspDWflLWfmurBD7upMPRUvVv9BLOwGALTDFXy9-y_kMPEij-w</recordid><startdate>20151006</startdate><enddate>20151006</enddate><creator>Duan, Xu C.</creator><creator>Chen, Huan</creator><creator>Liu, Fang F.</creator><creator>Conway, Louis</creator><creator>Wei, Shuang</creator><creator>Cai, Zhi P.</creator><creator>Liu, Li</creator><creator>Voglmeir, Josef</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7U5</scope><scope>7U7</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20151006</creationdate><title>One Assay for All: Exploring Small Molecule Phosphorylation Using Amylose–Polyiodide Complexes</title><author>Duan, Xu C. ; 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Chem</addtitle><date>2015-10-06</date><risdate>2015</risdate><volume>87</volume><issue>19</issue><spage>9546</spage><epage>9550</epage><pages>9546-9550</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><coden>ANCHAM</coden><abstract>We present a generic method for screening small molecule kinases for their acceptor specificity. The release of the reaction byproduct adenosine diphosphate (ADP) triggers a concentration-dependent formation of amylose from sucrose, by using the combined enzymatic action of sucrose synthase and glycogen synthase. Kinase activities could be quantified photometrically after the formation of a dark-blue amylose–polyiodide complex. We demonstrate that this method can be used to profile both known and novel nucleotide- and sugar-kinases for their substrate specificity. Using a facile and widely available methodology, the amylose–polyiodide small-molecule kinase assay presented herein has the potential to perform substrate screenings of small molecule kinases in a high-throughput manner.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>26308083</pmid><doi>10.1021/acs.analchem.5b02247</doi><tpages>5</tpages></addata></record> |
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| source | American Chemical Society; MEDLINE |
| subjects | Adenosine diphosphate Amylose - chemistry Amylose - metabolism Assaying Bioassays Byproducts Colorimetry Formations Iodine - chemistry Iodine - metabolism Kinases Molecules Phosphorylation Phosphotransferases - analysis Phosphotransferases - metabolism Photometry Screening Sucrose |
| title | One Assay for All: Exploring Small Molecule Phosphorylation Using Amylose–Polyiodide Complexes |
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