Substrate specificities of wild and mutated farnesyl diphosphate synthases from Bacillus stearothermophilus with artificial substrates
To determine the substrate specificities of wild and mutated types of farnesyl diphosphate (FPP) synthases from Bacillus stearothermophilus, we examined the reactivities of 8-hydroxygeranyl diphosphate (HOGPP) and 8-methoxygeranyl diphosphate (CH3OGPP) as allylic substrate homologs. The wild-type FP...
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| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2007-07, Vol.71 (7), p.1657-1662 |
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| creator | Nagaki, M.(Hirosaki Univ., Aomori (Japan). Faculty of Science and Technology) Nakada, M Musashi, T Kawakami, J Ohya, N Kurihara, M Maki, Y Nishino, T Koyama, T |
| description | To determine the substrate specificities of wild and mutated types of farnesyl diphosphate (FPP) synthases from Bacillus stearothermophilus, we examined the reactivities of 8-hydroxygeranyl diphosphate (HOGPP) and 8-methoxygeranyl diphosphate (CH3OGPP) as allylic substrate homologs. The wild-type FPP synthase reaction of HOGPP (and CH3OGPP) with isopentenyl diphosphate (IPP) gave hydroxyfarnesyl-(and methoxyfarnesyl-) diphosphates that stopped at the first stage of condensation. On the other hand, with mutated type FPP synthase (Y81S), the former gave hydroxygeranylgeranyl diphosphate as the main double-condensation product together with hydroxyfarnesyl diphosphate as a single-condensation product and a small amount of hydroxygeranylfarnesyl diphosphate as a triple-condensation product. Moreover, the latter gave a double-condensation product, methoxygeranylgeranyl diphosphate, as the main product and only a trace of methoxyfarnesyl diphosphate was obtained. |
| doi_str_mv | 10.1271/bbb.70067 |
| format | Article |
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Faculty of Science and Technology) ; Nakada, M ; Musashi, T ; Kawakami, J ; Ohya, N ; Kurihara, M ; Maki, Y ; Nishino, T ; Koyama, T</creator><creatorcontrib>Nagaki, M.(Hirosaki Univ., Aomori (Japan). Faculty of Science and Technology) ; Nakada, M ; Musashi, T ; Kawakami, J ; Ohya, N ; Kurihara, M ; Maki, Y ; Nishino, T ; Koyama, T</creatorcontrib><description>To determine the substrate specificities of wild and mutated types of farnesyl diphosphate (FPP) synthases from Bacillus stearothermophilus, we examined the reactivities of 8-hydroxygeranyl diphosphate (HOGPP) and 8-methoxygeranyl diphosphate (CH3OGPP) as allylic substrate homologs. The wild-type FPP synthase reaction of HOGPP (and CH3OGPP) with isopentenyl diphosphate (IPP) gave hydroxyfarnesyl-(and methoxyfarnesyl-) diphosphates that stopped at the first stage of condensation. On the other hand, with mutated type FPP synthase (Y81S), the former gave hydroxygeranylgeranyl diphosphate as the main double-condensation product together with hydroxyfarnesyl diphosphate as a single-condensation product and a small amount of hydroxygeranylfarnesyl diphosphate as a triple-condensation product. Moreover, the latter gave a double-condensation product, methoxygeranylgeranyl diphosphate, as the main product and only a trace of methoxyfarnesyl diphosphate was obtained.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.70067</identifier><identifier>PMID: 17617711</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>8-hydroxygeranyl and 8-methoxygeranyl diphosphates ; Amino Acid Substitution - genetics ; BACILLUS STEAROTHERMOPHILUS ; Biological and medical sciences ; CULTURE MEDIA ; Diphosphates - metabolism ; Diterpenes - metabolism ; ENZIMAS ; ENZYME ; ENZYMES ; Fundamental and applied biological sciences. Psychology ; Geobacillus stearothermophilus - enzymology ; Geobacillus stearothermophilus - genetics ; Geranyltranstransferase - genetics ; Geranyltranstransferase - physiology ; homologs of isopentenyl diphosphate ; ISOPRENOIDE ; ISOPRENOIDES ; ISOPRENOIDS ; MEDIO DE CULTIVO ; MILIEU DE CULTURE ; MUTANT ; MUTANTES ; MUTANTS ; substrate specificity ; Substrate Specificity - physiology ; wild and mutated farnesyl diphosphate synthases</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2007-07, Vol.71 (7), p.1657-1662</ispartof><rights>2007 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 2007</rights><rights>2007 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c439t-f4fc3fa9d1255c21cbe510a16472a616ff37d3df0cb795bdd6170acd06eda5183</citedby><cites>FETCH-LOGICAL-c439t-f4fc3fa9d1255c21cbe510a16472a616ff37d3df0cb795bdd6170acd06eda5183</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19034740$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17617711$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nagaki, M.(Hirosaki Univ., Aomori (Japan). Faculty of Science and Technology)</creatorcontrib><creatorcontrib>Nakada, M</creatorcontrib><creatorcontrib>Musashi, T</creatorcontrib><creatorcontrib>Kawakami, J</creatorcontrib><creatorcontrib>Ohya, N</creatorcontrib><creatorcontrib>Kurihara, M</creatorcontrib><creatorcontrib>Maki, Y</creatorcontrib><creatorcontrib>Nishino, T</creatorcontrib><creatorcontrib>Koyama, T</creatorcontrib><title>Substrate specificities of wild and mutated farnesyl diphosphate synthases from Bacillus stearothermophilus with artificial substrates</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>To determine the substrate specificities of wild and mutated types of farnesyl diphosphate (FPP) synthases from Bacillus stearothermophilus, we examined the reactivities of 8-hydroxygeranyl diphosphate (HOGPP) and 8-methoxygeranyl diphosphate (CH3OGPP) as allylic substrate homologs. The wild-type FPP synthase reaction of HOGPP (and CH3OGPP) with isopentenyl diphosphate (IPP) gave hydroxyfarnesyl-(and methoxyfarnesyl-) diphosphates that stopped at the first stage of condensation. On the other hand, with mutated type FPP synthase (Y81S), the former gave hydroxygeranylgeranyl diphosphate as the main double-condensation product together with hydroxyfarnesyl diphosphate as a single-condensation product and a small amount of hydroxygeranylfarnesyl diphosphate as a triple-condensation product. Moreover, the latter gave a double-condensation product, methoxygeranylgeranyl diphosphate, as the main product and only a trace of methoxyfarnesyl diphosphate was obtained.</description><subject>8-hydroxygeranyl and 8-methoxygeranyl diphosphates</subject><subject>Amino Acid Substitution - genetics</subject><subject>BACILLUS STEAROTHERMOPHILUS</subject><subject>Biological and medical sciences</subject><subject>CULTURE MEDIA</subject><subject>Diphosphates - metabolism</subject><subject>Diterpenes - metabolism</subject><subject>ENZIMAS</subject><subject>ENZYME</subject><subject>ENZYMES</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Geobacillus stearothermophilus - enzymology</subject><subject>Geobacillus stearothermophilus - genetics</subject><subject>Geranyltranstransferase - genetics</subject><subject>Geranyltranstransferase - physiology</subject><subject>homologs of isopentenyl diphosphate</subject><subject>ISOPRENOIDE</subject><subject>ISOPRENOIDES</subject><subject>ISOPRENOIDS</subject><subject>MEDIO DE CULTIVO</subject><subject>MILIEU DE CULTURE</subject><subject>MUTANT</subject><subject>MUTANTES</subject><subject>MUTANTS</subject><subject>substrate specificity</subject><subject>Substrate Specificity - physiology</subject><subject>wild and mutated farnesyl diphosphate synthases</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0tuKFDEQBuBGFHdcvfABlIAoeDFrqpNOpi918ciCgnrdVOdgZ0l3epM0w7yAz23msCyI4FWg-P5UikpVPQV6AbWEN33fX0hKhbxXrYBxuRYtl_erFW1BrDe8gbPqUUrXlJZCAw-rM5ACpARYVb-_L33KEbMhaTbKWadcdiaRYMnWeU1w0mRccgGaWIyTSTtPtJuHkObhENtNecBUIjaGkbxD5bxfEknZYAx5MHEM8-D2pa3LA8GYD13Qk3TbOz2uHlj0yTw5nefVzw_vf1x-Wl99_fj58u3VWnHW5rXlVjGLrYa6aVQNqjcNUATBZY0ChLVMaqYtVb1sm17rMiZFpakwGhvYsPPq1fHeOYabxaTcjS4p4z1OJiypk1QyWbP2v7CmjaCMiwJf_AWvwxKnMkQHnLcbEPVmr14flYohpWhsN0c3Ytx1QLv9Druyw-6ww2Kfn25c-tHoO3laWgEvTwCTQm8jTsqlO9eWh0lOi-NH5yYb4ojbEL3uMu58iLch9q_-z44xi6HDX7GoL99qSjfl_9TQsD8Y6sIx</recordid><startdate>20070701</startdate><enddate>20070701</enddate><creator>Nagaki, M.(Hirosaki Univ., Aomori (Japan). 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Faculty of Science and Technology) ; Nakada, M ; Musashi, T ; Kawakami, J ; Ohya, N ; Kurihara, M ; Maki, Y ; Nishino, T ; Koyama, T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-f4fc3fa9d1255c21cbe510a16472a616ff37d3df0cb795bdd6170acd06eda5183</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>8-hydroxygeranyl and 8-methoxygeranyl diphosphates</topic><topic>Amino Acid Substitution - genetics</topic><topic>BACILLUS STEAROTHERMOPHILUS</topic><topic>Biological and medical sciences</topic><topic>CULTURE MEDIA</topic><topic>Diphosphates - metabolism</topic><topic>Diterpenes - metabolism</topic><topic>ENZIMAS</topic><topic>ENZYME</topic><topic>ENZYMES</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Geobacillus stearothermophilus - enzymology</topic><topic>Geobacillus stearothermophilus - genetics</topic><topic>Geranyltranstransferase - genetics</topic><topic>Geranyltranstransferase - physiology</topic><topic>homologs of isopentenyl diphosphate</topic><topic>ISOPRENOIDE</topic><topic>ISOPRENOIDES</topic><topic>ISOPRENOIDS</topic><topic>MEDIO DE CULTIVO</topic><topic>MILIEU DE CULTURE</topic><topic>MUTANT</topic><topic>MUTANTES</topic><topic>MUTANTS</topic><topic>substrate specificity</topic><topic>Substrate Specificity - physiology</topic><topic>wild and mutated farnesyl diphosphate synthases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nagaki, M.(Hirosaki Univ., Aomori (Japan). Faculty of Science and Technology)</creatorcontrib><creatorcontrib>Nakada, M</creatorcontrib><creatorcontrib>Musashi, T</creatorcontrib><creatorcontrib>Kawakami, J</creatorcontrib><creatorcontrib>Ohya, N</creatorcontrib><creatorcontrib>Kurihara, M</creatorcontrib><creatorcontrib>Maki, Y</creatorcontrib><creatorcontrib>Nishino, T</creatorcontrib><creatorcontrib>Koyama, T</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</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>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nagaki, M.(Hirosaki Univ., Aomori (Japan). Faculty of Science and Technology)</au><au>Nakada, M</au><au>Musashi, T</au><au>Kawakami, J</au><au>Ohya, N</au><au>Kurihara, M</au><au>Maki, Y</au><au>Nishino, T</au><au>Koyama, T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Substrate specificities of wild and mutated farnesyl diphosphate synthases from Bacillus stearothermophilus with artificial substrates</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2007-07-01</date><risdate>2007</risdate><volume>71</volume><issue>7</issue><spage>1657</spage><epage>1662</epage><pages>1657-1662</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>To determine the substrate specificities of wild and mutated types of farnesyl diphosphate (FPP) synthases from Bacillus stearothermophilus, we examined the reactivities of 8-hydroxygeranyl diphosphate (HOGPP) and 8-methoxygeranyl diphosphate (CH3OGPP) as allylic substrate homologs. The wild-type FPP synthase reaction of HOGPP (and CH3OGPP) with isopentenyl diphosphate (IPP) gave hydroxyfarnesyl-(and methoxyfarnesyl-) diphosphates that stopped at the first stage of condensation. On the other hand, with mutated type FPP synthase (Y81S), the former gave hydroxygeranylgeranyl diphosphate as the main double-condensation product together with hydroxyfarnesyl diphosphate as a single-condensation product and a small amount of hydroxygeranylfarnesyl diphosphate as a triple-condensation product. Moreover, the latter gave a double-condensation product, methoxygeranylgeranyl diphosphate, as the main product and only a trace of methoxyfarnesyl diphosphate was obtained.</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>17617711</pmid><doi>10.1271/bbb.70067</doi><tpages>6</tpages></addata></record> |
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| source | J-STAGE Free; Oxford University Press Journals All Titles (1996-Current); MEDLINE; Freely Accessible Japanese Titles; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | 8-hydroxygeranyl and 8-methoxygeranyl diphosphates Amino Acid Substitution - genetics BACILLUS STEAROTHERMOPHILUS Biological and medical sciences CULTURE MEDIA Diphosphates - metabolism Diterpenes - metabolism ENZIMAS ENZYME ENZYMES Fundamental and applied biological sciences. Psychology Geobacillus stearothermophilus - enzymology Geobacillus stearothermophilus - genetics Geranyltranstransferase - genetics Geranyltranstransferase - physiology homologs of isopentenyl diphosphate ISOPRENOIDE ISOPRENOIDES ISOPRENOIDS MEDIO DE CULTIVO MILIEU DE CULTURE MUTANT MUTANTES MUTANTS substrate specificity Substrate Specificity - physiology wild and mutated farnesyl diphosphate synthases |
| title | Substrate specificities of wild and mutated farnesyl diphosphate synthases from Bacillus stearothermophilus with artificial substrates |
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