Firefly luciferase exhibits bimodal action depending on the luciferin chirality
Firefly luciferase is able to convert l-luciferin into luciferyl-CoA even under ordinary aerobic luciferin–luciferase reaction conditions. The luciferase is able to recognize strictly the chirality of the luciferin structure, serving as the acyl-CoA synthetase for l-luciferin, whereas d-luciferin is...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2005-06, Vol.331 (2), p.471-475 |
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| container_end_page | 475 |
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| container_issue | 2 |
| container_start_page | 471 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 331 |
| creator | Nakamura, Mitsuhiro Maki, Shojiro Amano, Yoshiharu Ohkita, Yutaka Niwa, Kazuki Hirano, Takashi Ohmiya, Yoshihiro Niwa, Haruki |
| description | Firefly luciferase is able to convert
l-luciferin into luciferyl-CoA even under ordinary aerobic luciferin–luciferase reaction conditions. The luciferase is able to recognize strictly the chirality of the luciferin structure, serving as the acyl-CoA synthetase for
l-luciferin, whereas
d-luciferin is used for the bioluminescence reaction.
d-Luciferin inhibits the luciferyl-CoA synthetase activity of
l-luciferin, whereas
l-luciferin retards the bioluminescence reaction of
d-luciferin, meaning that both enzyme activities are prevented by the enantiomer of its own substrate. |
| doi_str_mv | 10.1016/j.bbrc.2005.03.202 |
| format | Article |
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l-luciferin into luciferyl-CoA even under ordinary aerobic luciferin–luciferase reaction conditions. The luciferase is able to recognize strictly the chirality of the luciferin structure, serving as the acyl-CoA synthetase for
l-luciferin, whereas
d-luciferin is used for the bioluminescence reaction.
d-Luciferin inhibits the luciferyl-CoA synthetase activity of
l-luciferin, whereas
l-luciferin retards the bioluminescence reaction of
d-luciferin, meaning that both enzyme activities are prevented by the enantiomer of its own substrate.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2005.03.202</identifier><identifier>PMID: 15850783</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acyl Coenzyme A - chemistry ; Acyl Coenzyme A - metabolism ; Animals ; Chiral recognition ; Chromatography, High Pressure Liquid ; CoA-ligase ; Coenzyme A - metabolism ; d-Luciferin ; Enantioselective ; Firefly luciferase ; Firefly Luciferin - chemistry ; Firefly Luciferin - metabolism ; l-Luciferin ; Luciferases, Firefly - metabolism ; Luminescence ; Luminescent Proteins ; Molecular Structure ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Stereoisomerism ; Substrate Specificity</subject><ispartof>Biochemical and biophysical research communications, 2005-06, Vol.331 (2), p.471-475</ispartof><rights>2005 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c420t-8337c259c08a41350dad38ea1056cdcb9d7adc3c71595e85a0327726f64388273</citedby><cites>FETCH-LOGICAL-c420t-8337c259c08a41350dad38ea1056cdcb9d7adc3c71595e85a0327726f64388273</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X05007047$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15850783$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nakamura, Mitsuhiro</creatorcontrib><creatorcontrib>Maki, Shojiro</creatorcontrib><creatorcontrib>Amano, Yoshiharu</creatorcontrib><creatorcontrib>Ohkita, Yutaka</creatorcontrib><creatorcontrib>Niwa, Kazuki</creatorcontrib><creatorcontrib>Hirano, Takashi</creatorcontrib><creatorcontrib>Ohmiya, Yoshihiro</creatorcontrib><creatorcontrib>Niwa, Haruki</creatorcontrib><title>Firefly luciferase exhibits bimodal action depending on the luciferin chirality</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Firefly luciferase is able to convert
l-luciferin into luciferyl-CoA even under ordinary aerobic luciferin–luciferase reaction conditions. The luciferase is able to recognize strictly the chirality of the luciferin structure, serving as the acyl-CoA synthetase for
l-luciferin, whereas
d-luciferin is used for the bioluminescence reaction.
d-Luciferin inhibits the luciferyl-CoA synthetase activity of
l-luciferin, whereas
l-luciferin retards the bioluminescence reaction of
d-luciferin, meaning that both enzyme activities are prevented by the enantiomer of its own substrate.</description><subject>Acyl Coenzyme A - chemistry</subject><subject>Acyl Coenzyme A - metabolism</subject><subject>Animals</subject><subject>Chiral recognition</subject><subject>Chromatography, High Pressure Liquid</subject><subject>CoA-ligase</subject><subject>Coenzyme A - metabolism</subject><subject>d-Luciferin</subject><subject>Enantioselective</subject><subject>Firefly luciferase</subject><subject>Firefly Luciferin - chemistry</subject><subject>Firefly Luciferin - metabolism</subject><subject>l-Luciferin</subject><subject>Luciferases, Firefly - metabolism</subject><subject>Luminescence</subject><subject>Luminescent Proteins</subject><subject>Molecular Structure</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Stereoisomerism</subject><subject>Substrate Specificity</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LAzEURYMotlb_gAuZlbsZX5LJZAbcSLEqFLpRcBcyyatNmY-aTMX-e1Nacefq8uDcC-8Qck0ho0CLu3VW195kDEBkwGOyEzKmUEHKKOSnZAwARcoq-j4iFyGsASjNi-qcjKgoBciSj8li5jwum13SbI1botcBE_xeudoNIald21vdJNoMru8SixvsrOs-kngMK_ztuC4xK-d144bdJTlb6ibg1TEn5G32-Dp9TueLp5fpwzw1OYMhLTmXhonKQKlzygVYbXmJmoIojDV1ZaW2hhtJRSWwFBo4k5IVyyLnZckkn5Dbw-7G959bDINqXTDYNLrDfhtUIaUUAiCC7AAa34cQf1Ub71rtd4qC2mtUa7XXqPYaFfCYLJZujuvbukX7Vzl6i8D9AcD445dDr4Jx2Bm0UacZlO3df_s_-KWDew</recordid><startdate>20050603</startdate><enddate>20050603</enddate><creator>Nakamura, Mitsuhiro</creator><creator>Maki, Shojiro</creator><creator>Amano, Yoshiharu</creator><creator>Ohkita, Yutaka</creator><creator>Niwa, Kazuki</creator><creator>Hirano, Takashi</creator><creator>Ohmiya, Yoshihiro</creator><creator>Niwa, Haruki</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>20050603</creationdate><title>Firefly luciferase exhibits bimodal action depending on the luciferin chirality</title><author>Nakamura, Mitsuhiro ; 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l-luciferin into luciferyl-CoA even under ordinary aerobic luciferin–luciferase reaction conditions. The luciferase is able to recognize strictly the chirality of the luciferin structure, serving as the acyl-CoA synthetase for
l-luciferin, whereas
d-luciferin is used for the bioluminescence reaction.
d-Luciferin inhibits the luciferyl-CoA synthetase activity of
l-luciferin, whereas
l-luciferin retards the bioluminescence reaction of
d-luciferin, meaning that both enzyme activities are prevented by the enantiomer of its own substrate.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15850783</pmid><doi>10.1016/j.bbrc.2005.03.202</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 2005-06, Vol.331 (2), p.471-475 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Acyl Coenzyme A - chemistry Acyl Coenzyme A - metabolism Animals Chiral recognition Chromatography, High Pressure Liquid CoA-ligase Coenzyme A - metabolism d-Luciferin Enantioselective Firefly luciferase Firefly Luciferin - chemistry Firefly Luciferin - metabolism l-Luciferin Luciferases, Firefly - metabolism Luminescence Luminescent Proteins Molecular Structure Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Stereoisomerism Substrate Specificity |
| title | Firefly luciferase exhibits bimodal action depending on the luciferin chirality |
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