Pyrophosphate and tripolyphosphate affect firefly luciferase luminescence because they act as substrates and not as allosteric effectors
The activating and stabilizing effects of inorganic pyrophosphate, tripolyphosphate and nucleoside triphosphates on firefly luciferase bioluminescence were studied. The results obtained show that those effects are a consequence of the luciferase-catalyzed splitting of dehydroluciferyl-adenylate, a p...
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| Veröffentlicht in: | The FEBS journal 2008-04, Vol.275 (7), p.1500-1509 |
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| creator | Fontes, Rui Fernandes, Diogo Peralta, Filipe Fraga, Hugo Maio, Inês Esteves da Silva, Joaquim C.G |
| description | The activating and stabilizing effects of inorganic pyrophosphate, tripolyphosphate and nucleoside triphosphates on firefly luciferase bioluminescence were studied. The results obtained show that those effects are a consequence of the luciferase-catalyzed splitting of dehydroluciferyl-adenylate, a powerful inhibitor formed as a side product in the course of the bioluminescence reaction. Inorganic pyrophosphate, tripolyphosphate, CTP and UTP antagonize the inhibitory effect of dehydroluciferyl-adenylate because they react with it giving rise to products that are, at least, less powerful inhibitors. Moreover, we demonstrate that the antagonizing effects depended on the rate of the splitting reactions being higher in the cases of inorganic pyrophosphate and tripolyphosphate and lower in the cases of CTP and UTP. In the case of inorganic pyrophosphate, the correlation between the rate of dehydroluciferyl-adenylate pyrophosphorolysis and the activating effect on bioluminescence only occurs for low concentrations because inorganic pyrophosphate is, simultaneously, an inhibitor of the bioluminescence reaction. Our results demonstrate that previous reports concerning the activating effects of several nucleotides (including some that do not react with dehydroluciferyl-adenylate) on bioluminescence were caused by the presence of inorganic pyrophosphate contamination in the preparations used. |
| doi_str_mv | 10.1111/j.1742-4658.2008.06309.x |
| format | Article |
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The results obtained show that those effects are a consequence of the luciferase-catalyzed splitting of dehydroluciferyl-adenylate, a powerful inhibitor formed as a side product in the course of the bioluminescence reaction. Inorganic pyrophosphate, tripolyphosphate, CTP and UTP antagonize the inhibitory effect of dehydroluciferyl-adenylate because they react with it giving rise to products that are, at least, less powerful inhibitors. Moreover, we demonstrate that the antagonizing effects depended on the rate of the splitting reactions being higher in the cases of inorganic pyrophosphate and tripolyphosphate and lower in the cases of CTP and UTP. In the case of inorganic pyrophosphate, the correlation between the rate of dehydroluciferyl-adenylate pyrophosphorolysis and the activating effect on bioluminescence only occurs for low concentrations because inorganic pyrophosphate is, simultaneously, an inhibitor of the bioluminescence reaction. Our results demonstrate that previous reports concerning the activating effects of several nucleotides (including some that do not react with dehydroluciferyl-adenylate) on bioluminescence were caused by the presence of inorganic pyrophosphate contamination in the preparations used.</description><identifier>ISSN: 1742-464X</identifier><identifier>EISSN: 1742-4658</identifier><identifier>DOI: 10.1111/j.1742-4658.2008.06309.x</identifier><identifier>PMID: 18279384</identifier><language>eng</language><publisher>Oxford, UK: Oxford, UK : Blackwell Publishing Ltd</publisher><subject>Allosteric Regulation - physiology ; Animals ; Biochemistry ; Bioluminescence ; Catalysis ; dehydroluciferyl‐adenylate ; dinucleoside polyphosphates ; Diphosphates - chemistry ; Diphosphates - metabolism ; Fireflies - enzymology ; firefly luciferase ; Insects ; Luciferases, Firefly - chemistry ; Luciferases, Firefly - metabolism ; Luminescence ; Luminescent Agents - chemistry ; Luminescent Agents - metabolism ; Polyphosphates - chemistry ; Polyphosphates - metabolism ; Pyrophosphatases - chemistry ; Pyrophosphatases - physiology ; pyrophosphate ; Substrate Specificity - physiology ; Substrates ; tripolyphosphate</subject><ispartof>The FEBS journal, 2008-04, Vol.275 (7), p.1500-1509</ispartof><rights>2008 The Authors</rights><rights>Journal compilation © 2008 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4699-98d405f3e3e69a960361cfaac55dce250594da83d7628162bb9135def45d6ef53</citedby><cites>FETCH-LOGICAL-c4699-98d405f3e3e69a960361cfaac55dce250594da83d7628162bb9135def45d6ef53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1742-4658.2008.06309.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1742-4658.2008.06309.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18279384$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fontes, Rui</creatorcontrib><creatorcontrib>Fernandes, Diogo</creatorcontrib><creatorcontrib>Peralta, Filipe</creatorcontrib><creatorcontrib>Fraga, Hugo</creatorcontrib><creatorcontrib>Maio, Inês</creatorcontrib><creatorcontrib>Esteves da Silva, Joaquim C.G</creatorcontrib><title>Pyrophosphate and tripolyphosphate affect firefly luciferase luminescence because they act as substrates and not as allosteric effectors</title><title>The FEBS journal</title><addtitle>FEBS J</addtitle><description>The activating and stabilizing effects of inorganic pyrophosphate, tripolyphosphate and nucleoside triphosphates on firefly luciferase bioluminescence were studied. The results obtained show that those effects are a consequence of the luciferase-catalyzed splitting of dehydroluciferyl-adenylate, a powerful inhibitor formed as a side product in the course of the bioluminescence reaction. Inorganic pyrophosphate, tripolyphosphate, CTP and UTP antagonize the inhibitory effect of dehydroluciferyl-adenylate because they react with it giving rise to products that are, at least, less powerful inhibitors. Moreover, we demonstrate that the antagonizing effects depended on the rate of the splitting reactions being higher in the cases of inorganic pyrophosphate and tripolyphosphate and lower in the cases of CTP and UTP. In the case of inorganic pyrophosphate, the correlation between the rate of dehydroluciferyl-adenylate pyrophosphorolysis and the activating effect on bioluminescence only occurs for low concentrations because inorganic pyrophosphate is, simultaneously, an inhibitor of the bioluminescence reaction. Our results demonstrate that previous reports concerning the activating effects of several nucleotides (including some that do not react with dehydroluciferyl-adenylate) on bioluminescence were caused by the presence of inorganic pyrophosphate contamination in the preparations used.</description><subject>Allosteric Regulation - physiology</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Bioluminescence</subject><subject>Catalysis</subject><subject>dehydroluciferyl‐adenylate</subject><subject>dinucleoside polyphosphates</subject><subject>Diphosphates - chemistry</subject><subject>Diphosphates - metabolism</subject><subject>Fireflies - enzymology</subject><subject>firefly luciferase</subject><subject>Insects</subject><subject>Luciferases, Firefly - chemistry</subject><subject>Luciferases, Firefly - metabolism</subject><subject>Luminescence</subject><subject>Luminescent Agents - chemistry</subject><subject>Luminescent Agents - metabolism</subject><subject>Polyphosphates - chemistry</subject><subject>Polyphosphates - metabolism</subject><subject>Pyrophosphatases - chemistry</subject><subject>Pyrophosphatases - physiology</subject><subject>pyrophosphate</subject><subject>Substrate Specificity - physiology</subject><subject>Substrates</subject><subject>tripolyphosphate</subject><issn>1742-464X</issn><issn>1742-4658</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkctu1DAUhiMEohf6CmCxYDfB18TeINGqLUiVWqlU6s5ynGMmI08c7EQ0b8Bj48yMCmKFNz46_s7nxH9RIIJLktfHTUlqTle8ErKkGMsSVwyr8ulFcfx88PK55o9HxUlKG4yZ4Eq9Lo6IpLVikh8Xv-7mGIZ1SMPajIBM36IxdkPw819N58COyHURnJ-Rn2znIJoEudx2PSQLvQXUgDVTbo5rmJHJAyahNDVpjFmSduo-7LrG-5BGiJ1FsHOHmN4Ur5zxCc4O-2nxcHX57eLL6ub2-uvF55uV5ZVSKyVbjoVjwKBSRlWYVcQ6Y6wQrQUqsFC8NZK1dUUlqWjTKMJEC46LtgIn2GnxYe8dYvgxQRr1tss_4L3pIUxJ15gpLJXM4Pt_wE2YYp-_TVPMCc034wzJPWRjSCm_jx5itzVx1gTrJSq90UsKeklEL1HpXVT6KY--PfinZgvtn8FDNhn4tAd-dh7m_xbrq8vz-6XMgnd7gTNBm--xS_rhnmLCMl1jzgn7DSemruI</recordid><startdate>200804</startdate><enddate>200804</enddate><creator>Fontes, Rui</creator><creator>Fernandes, Diogo</creator><creator>Peralta, Filipe</creator><creator>Fraga, Hugo</creator><creator>Maio, Inês</creator><creator>Esteves da Silva, Joaquim C.G</creator><general>Oxford, UK : Blackwell Publishing Ltd</general><general>Blackwell Publishing Ltd</general><scope>FBQ</scope><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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200804</creationdate><title>Pyrophosphate and tripolyphosphate affect firefly luciferase luminescence because they act as substrates and not as allosteric effectors</title><author>Fontes, Rui ; Fernandes, Diogo ; Peralta, Filipe ; Fraga, Hugo ; Maio, Inês ; Esteves da Silva, Joaquim C.G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4699-98d405f3e3e69a960361cfaac55dce250594da83d7628162bb9135def45d6ef53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Allosteric Regulation - physiology</topic><topic>Animals</topic><topic>Biochemistry</topic><topic>Bioluminescence</topic><topic>Catalysis</topic><topic>dehydroluciferyl‐adenylate</topic><topic>dinucleoside polyphosphates</topic><topic>Diphosphates - chemistry</topic><topic>Diphosphates - metabolism</topic><topic>Fireflies - enzymology</topic><topic>firefly luciferase</topic><topic>Insects</topic><topic>Luciferases, Firefly - chemistry</topic><topic>Luciferases, Firefly - metabolism</topic><topic>Luminescence</topic><topic>Luminescent Agents - chemistry</topic><topic>Luminescent Agents - metabolism</topic><topic>Polyphosphates - chemistry</topic><topic>Polyphosphates - metabolism</topic><topic>Pyrophosphatases - chemistry</topic><topic>Pyrophosphatases - physiology</topic><topic>pyrophosphate</topic><topic>Substrate Specificity - physiology</topic><topic>Substrates</topic><topic>tripolyphosphate</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fontes, Rui</creatorcontrib><creatorcontrib>Fernandes, Diogo</creatorcontrib><creatorcontrib>Peralta, Filipe</creatorcontrib><creatorcontrib>Fraga, Hugo</creatorcontrib><creatorcontrib>Maio, Inês</creatorcontrib><creatorcontrib>Esteves da Silva, Joaquim C.G</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The FEBS journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fontes, Rui</au><au>Fernandes, Diogo</au><au>Peralta, Filipe</au><au>Fraga, Hugo</au><au>Maio, Inês</au><au>Esteves da Silva, Joaquim C.G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Pyrophosphate and tripolyphosphate affect firefly luciferase luminescence because they act as substrates and not as allosteric effectors</atitle><jtitle>The FEBS journal</jtitle><addtitle>FEBS J</addtitle><date>2008-04</date><risdate>2008</risdate><volume>275</volume><issue>7</issue><spage>1500</spage><epage>1509</epage><pages>1500-1509</pages><issn>1742-464X</issn><eissn>1742-4658</eissn><abstract>The activating and stabilizing effects of inorganic pyrophosphate, tripolyphosphate and nucleoside triphosphates on firefly luciferase bioluminescence were studied. The results obtained show that those effects are a consequence of the luciferase-catalyzed splitting of dehydroluciferyl-adenylate, a powerful inhibitor formed as a side product in the course of the bioluminescence reaction. Inorganic pyrophosphate, tripolyphosphate, CTP and UTP antagonize the inhibitory effect of dehydroluciferyl-adenylate because they react with it giving rise to products that are, at least, less powerful inhibitors. Moreover, we demonstrate that the antagonizing effects depended on the rate of the splitting reactions being higher in the cases of inorganic pyrophosphate and tripolyphosphate and lower in the cases of CTP and UTP. In the case of inorganic pyrophosphate, the correlation between the rate of dehydroluciferyl-adenylate pyrophosphorolysis and the activating effect on bioluminescence only occurs for low concentrations because inorganic pyrophosphate is, simultaneously, an inhibitor of the bioluminescence reaction. Our results demonstrate that previous reports concerning the activating effects of several nucleotides (including some that do not react with dehydroluciferyl-adenylate) on bioluminescence were caused by the presence of inorganic pyrophosphate contamination in the preparations used.</abstract><cop>Oxford, UK</cop><pub>Oxford, UK : Blackwell Publishing Ltd</pub><pmid>18279384</pmid><doi>10.1111/j.1742-4658.2008.06309.x</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Allosteric Regulation - physiology Animals Biochemistry Bioluminescence Catalysis dehydroluciferyl‐adenylate dinucleoside polyphosphates Diphosphates - chemistry Diphosphates - metabolism Fireflies - enzymology firefly luciferase Insects Luciferases, Firefly - chemistry Luciferases, Firefly - metabolism Luminescence Luminescent Agents - chemistry Luminescent Agents - metabolism Polyphosphates - chemistry Polyphosphates - metabolism Pyrophosphatases - chemistry Pyrophosphatases - physiology pyrophosphate Substrate Specificity - physiology Substrates tripolyphosphate |
| title | Pyrophosphate and tripolyphosphate affect firefly luciferase luminescence because they act as substrates and not as allosteric effectors |
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