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One-Pot Multi-Enzymatic Production of Purine Derivatives with Application in Pharmaceutical and Food Industry
Biocatalysis reproduce nature’s synthetic strategies in order to synthesize different organic compounds. Natural metabolic pathways usually involve complex networks to support cellular growth and survival. In this regard, multi-enzymatic systems are valuable tools for the production of a wide variet...
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Published in: | Catalysts 2018-01, Vol.8 (1), p.9 |
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creator | Acosta, Javier del Arco, Jon Martinez-Pascual, Sara Clemente-Suárez, Vicente Fernández-Lucas, Jesús |
description | Biocatalysis reproduce nature’s synthetic strategies in order to synthesize different organic compounds. Natural metabolic pathways usually involve complex networks to support cellular growth and survival. In this regard, multi-enzymatic systems are valuable tools for the production of a wide variety of organic compounds. Methods: The production of different purine nucleosides and nucleoside-5′-monophosphates has been performed for first time, catalyzed by the sequential action of 2′-deoxyribosyltransferase from Lactobacillus delbrueckii (LdNDT) and hypoxanthine-guanine-xanthine phosphoribosyltransferase from Thermus themophilus HB8 (TtHGXPRT). Results: The biochemical characterization of LdNDT reveals that the enzyme is active and stable in a broad range of pH, temperature, and ionic strength. Substrate specificity studies showed a high promiscuity in the recognition of purine analogues. Finally, the enzymatic production of different purine derivatives was performed to evaluate the efficiency of multi-enzymatic system LdNDT/TtHGXPRT. Conclusions: The production of different therapeutic purine nucleosides was efficiently catalyzed by LdNDT/TtHGXPRT. In addition, the resulting by-products were converted to IMP and GMP. Taking all of these features, this bioprocess entails an efficient, sustainable, and economical alternative to chemical synthetic methods. |
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Natural metabolic pathways usually involve complex networks to support cellular growth and survival. In this regard, multi-enzymatic systems are valuable tools for the production of a wide variety of organic compounds. Methods: The production of different purine nucleosides and nucleoside-5′-monophosphates has been performed for first time, catalyzed by the sequential action of 2′-deoxyribosyltransferase from Lactobacillus delbrueckii (LdNDT) and hypoxanthine-guanine-xanthine phosphoribosyltransferase from Thermus themophilus HB8 (TtHGXPRT). Results: The biochemical characterization of LdNDT reveals that the enzyme is active and stable in a broad range of pH, temperature, and ionic strength. Substrate specificity studies showed a high promiscuity in the recognition of purine analogues. Finally, the enzymatic production of different purine derivatives was performed to evaluate the efficiency of multi-enzymatic system LdNDT/TtHGXPRT. Conclusions: The production of different therapeutic purine nucleosides was efficiently catalyzed by LdNDT/TtHGXPRT. In addition, the resulting by-products were converted to IMP and GMP. Taking all of these features, this bioprocess entails an efficient, sustainable, and economical alternative to chemical synthetic methods.</description><identifier>ISSN: 2073-4344</identifier><identifier>EISSN: 2073-4344</identifier><identifier>DOI: 10.3390/catal8010009</identifier><language>eng</language><publisher>Basel: MDPI AG</publisher><subject>Catalysts ; Cellular communication ; Chemical reactions ; Derivatives ; Food processing industry ; Hypoxanthine ; Lactobacilli ; Nucleosides ; Organic compounds ; Production methods ; Substrates</subject><ispartof>Catalysts, 2018-01, Vol.8 (1), p.9</ispartof><rights>Copyright MDPI AG 2018</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c301t-2649f23fe280244c8b26c4c36f50da1768b5e7d27054268b734fb99de2c4e4ba3</citedby><cites>FETCH-LOGICAL-c301t-2649f23fe280244c8b26c4c36f50da1768b5e7d27054268b734fb99de2c4e4ba3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2002909426/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2002909426?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,25753,27924,27925,37012,44590,75126</link.rule.ids></links><search><creatorcontrib>Acosta, Javier</creatorcontrib><creatorcontrib>del Arco, Jon</creatorcontrib><creatorcontrib>Martinez-Pascual, Sara</creatorcontrib><creatorcontrib>Clemente-Suárez, Vicente</creatorcontrib><creatorcontrib>Fernández-Lucas, Jesús</creatorcontrib><title>One-Pot Multi-Enzymatic Production of Purine Derivatives with Application in Pharmaceutical and Food Industry</title><title>Catalysts</title><description>Biocatalysis reproduce nature’s synthetic strategies in order to synthesize different organic compounds. Natural metabolic pathways usually involve complex networks to support cellular growth and survival. In this regard, multi-enzymatic systems are valuable tools for the production of a wide variety of organic compounds. Methods: The production of different purine nucleosides and nucleoside-5′-monophosphates has been performed for first time, catalyzed by the sequential action of 2′-deoxyribosyltransferase from Lactobacillus delbrueckii (LdNDT) and hypoxanthine-guanine-xanthine phosphoribosyltransferase from Thermus themophilus HB8 (TtHGXPRT). Results: The biochemical characterization of LdNDT reveals that the enzyme is active and stable in a broad range of pH, temperature, and ionic strength. Substrate specificity studies showed a high promiscuity in the recognition of purine analogues. Finally, the enzymatic production of different purine derivatives was performed to evaluate the efficiency of multi-enzymatic system LdNDT/TtHGXPRT. Conclusions: The production of different therapeutic purine nucleosides was efficiently catalyzed by LdNDT/TtHGXPRT. In addition, the resulting by-products were converted to IMP and GMP. Taking all of these features, this bioprocess entails an efficient, sustainable, and economical alternative to chemical synthetic methods.</description><subject>Catalysts</subject><subject>Cellular communication</subject><subject>Chemical reactions</subject><subject>Derivatives</subject><subject>Food processing industry</subject><subject>Hypoxanthine</subject><subject>Lactobacilli</subject><subject>Nucleosides</subject><subject>Organic compounds</subject><subject>Production methods</subject><subject>Substrates</subject><issn>2073-4344</issn><issn>2073-4344</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><recordid>eNpNkEtPwzAQhC0EElXpjR9giSuB9SOvY1XaUqmoOcA5chxHdZXYwXaKyq8nVTn0tLuab2ekQeiRwAtjObxKEUSbAQGA_AZNKKQs4ozz26v9Hs28P8AZISwj8QR1O6Oiwgb8MbRBR0vze-pE0BIXztaDDNoabBtcDE4bhd-U08dRPiqPf3TY43nft3pMPmPa4GIvXCekGkYH0WJharyytsYbUw8-uNMDumtE69Xsf07R12r5uXiPtrv1ZjHfRpIBCRFNeN5Q1iiaAeVcZhVNJJcsaWKoBUmTrIpVWtMUYk7HI2W8qfK8VlRyxSvBpujp4ts7-z0oH8qDHZwZI0sKQHPIx7-Rer5Q0lnvnWrK3ulOuFNJoDx3Wl53yv4A4Vpqqg</recordid><startdate>20180101</startdate><enddate>20180101</enddate><creator>Acosta, Javier</creator><creator>del Arco, Jon</creator><creator>Martinez-Pascual, Sara</creator><creator>Clemente-Suárez, Vicente</creator><creator>Fernández-Lucas, Jesús</creator><general>MDPI AG</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>KB.</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope></search><sort><creationdate>20180101</creationdate><title>One-Pot Multi-Enzymatic Production of Purine Derivatives with Application in Pharmaceutical and Food Industry</title><author>Acosta, Javier ; del Arco, Jon ; Martinez-Pascual, Sara ; Clemente-Suárez, Vicente ; Fernández-Lucas, Jesús</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c301t-2649f23fe280244c8b26c4c36f50da1768b5e7d27054268b734fb99de2c4e4ba3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Catalysts</topic><topic>Cellular communication</topic><topic>Chemical reactions</topic><topic>Derivatives</topic><topic>Food processing industry</topic><topic>Hypoxanthine</topic><topic>Lactobacilli</topic><topic>Nucleosides</topic><topic>Organic compounds</topic><topic>Production methods</topic><topic>Substrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Acosta, Javier</creatorcontrib><creatorcontrib>del Arco, Jon</creatorcontrib><creatorcontrib>Martinez-Pascual, Sara</creatorcontrib><creatorcontrib>Clemente-Suárez, Vicente</creatorcontrib><creatorcontrib>Fernández-Lucas, Jesús</creatorcontrib><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central</collection><collection>SciTech Premium Collection</collection><collection>Materials Research Database</collection><collection>https://resources.nclive.org/materials</collection><collection>Materials science collection</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><jtitle>Catalysts</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Acosta, Javier</au><au>del Arco, Jon</au><au>Martinez-Pascual, Sara</au><au>Clemente-Suárez, Vicente</au><au>Fernández-Lucas, Jesús</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>One-Pot Multi-Enzymatic Production of Purine Derivatives with Application in Pharmaceutical and Food Industry</atitle><jtitle>Catalysts</jtitle><date>2018-01-01</date><risdate>2018</risdate><volume>8</volume><issue>1</issue><spage>9</spage><pages>9-</pages><issn>2073-4344</issn><eissn>2073-4344</eissn><abstract>Biocatalysis reproduce nature’s synthetic strategies in order to synthesize different organic compounds. Natural metabolic pathways usually involve complex networks to support cellular growth and survival. In this regard, multi-enzymatic systems are valuable tools for the production of a wide variety of organic compounds. Methods: The production of different purine nucleosides and nucleoside-5′-monophosphates has been performed for first time, catalyzed by the sequential action of 2′-deoxyribosyltransferase from Lactobacillus delbrueckii (LdNDT) and hypoxanthine-guanine-xanthine phosphoribosyltransferase from Thermus themophilus HB8 (TtHGXPRT). Results: The biochemical characterization of LdNDT reveals that the enzyme is active and stable in a broad range of pH, temperature, and ionic strength. Substrate specificity studies showed a high promiscuity in the recognition of purine analogues. Finally, the enzymatic production of different purine derivatives was performed to evaluate the efficiency of multi-enzymatic system LdNDT/TtHGXPRT. Conclusions: The production of different therapeutic purine nucleosides was efficiently catalyzed by LdNDT/TtHGXPRT. In addition, the resulting by-products were converted to IMP and GMP. Taking all of these features, this bioprocess entails an efficient, sustainable, and economical alternative to chemical synthetic methods.</abstract><cop>Basel</cop><pub>MDPI AG</pub><doi>10.3390/catal8010009</doi><oa>free_for_read</oa></addata></record> |
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subjects | Catalysts Cellular communication Chemical reactions Derivatives Food processing industry Hypoxanthine Lactobacilli Nucleosides Organic compounds Production methods Substrates |
title | One-Pot Multi-Enzymatic Production of Purine Derivatives with Application in Pharmaceutical and Food Industry |
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