Production of L-DOPA(3,4-dihydroxyphenyl-L-alanine) from benzene by using a hybrid pathway
As an alternative approach to the production of L‐DOPA from a cheap raw material, we constructed a hybrid pathway consisting of toluene dioxygenase, toluene cis‐glycol dehydrogenase, and tyrosine phenol‐lyase. In this pathway, catechol is formed from benzene through the sequential action of toluene...
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| Veröffentlicht in: | Biotechnology and bioengineering 1998-04, Vol.58 (2-3), p.339-343 |
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| container_title | Biotechnology and bioengineering |
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| creator | Park, Hee-Sung Lee, Jang-Young Kim, Hak-Sung |
| description | As an alternative approach to the production of L‐DOPA from a cheap raw material, we constructed a hybrid pathway consisting of toluene dioxygenase, toluene cis‐glycol dehydrogenase, and tyrosine phenol‐lyase. In this pathway, catechol is formed from benzene through the sequential action of toluene dioxygenase and toluene cis‐glycol dehydrogenase, and L‐DOPA is synthesized from the resulting catechol in the presence of pyruvate and ammonia by tyrosine phenol‐lyase cloned from Citrobacter freundii. When the hybrid pathway was expressed in E. coli, production of L‐DOPA was as low as 3 mM in 4 h due to the toxic effect of benzene on the cells. In order to reduce lysis of cells, Pseudomonas aeruginosa was employed as an alternative, which resulted in accumulation of about 14 mM L‐DOPA in 9 h, showing a stronger resistance to benzene. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 58:339–343, 1998. |
| doi_str_mv | 10.1002/(SICI)1097-0290(19980420)58:2/3<339::AID-BIT36>3.0.CO;2-4 |
| format | Article |
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In this pathway, catechol is formed from benzene through the sequential action of toluene dioxygenase and toluene cis‐glycol dehydrogenase, and L‐DOPA is synthesized from the resulting catechol in the presence of pyruvate and ammonia by tyrosine phenol‐lyase cloned from Citrobacter freundii. When the hybrid pathway was expressed in E. coli, production of L‐DOPA was as low as 3 mM in 4 h due to the toxic effect of benzene on the cells. In order to reduce lysis of cells, Pseudomonas aeruginosa was employed as an alternative, which resulted in accumulation of about 14 mM L‐DOPA in 9 h, showing a stronger resistance to benzene. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 58:339–343, 1998.</description><identifier>ISSN: 0006-3592</identifier><identifier>EISSN: 1097-0290</identifier><identifier>DOI: 10.1002/(SICI)1097-0290(19980420)58:2/3<339::AID-BIT36>3.0.CO;2-4</identifier><identifier>PMID: 10191414</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>4-dihydroxyphenyl-L-alanine ; Ammonia ; Antiparkinson Agents - metabolism ; Benzene ; Benzene - metabolism ; Cloning ; Coliform bacteria ; Drug products ; Enzymes ; Escherichia coli - enzymology ; Genetic Engineering ; hybrid pathway ; L-DOPA ; Levodopa - biosynthesis ; L‐DOPA(3,4‐dihydroxyphenyl‐L‐alanine) ; Oxidoreductases - genetics ; Oxidoreductases - metabolism ; Oxygenases - genetics ; Oxygenases - metabolism ; Pseudomonas aeruginosa - enzymology ; Salts ; toluene dioxygenase ; Transfection ; tyrosine phenol lyase ; Tyrosine Phenol-Lyase - genetics ; Tyrosine Phenol-Lyase - metabolism</subject><ispartof>Biotechnology and bioengineering, 1998-04, Vol.58 (2-3), p.339-343</ispartof><rights>Copyright © 1998 John Wiley & Sons, Inc.</rights><rights>Copyright 1998 John Wiley & Sons, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2F%28SICI%291097-0290%2819980420%2958%3A2%2F3%3C339%3A%3AAID-BIT36%3E3.0.CO%3B2-4$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2F%28SICI%291097-0290%2819980420%2958%3A2%2F3%3C339%3A%3AAID-BIT36%3E3.0.CO%3B2-4$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10191414$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Park, Hee-Sung</creatorcontrib><creatorcontrib>Lee, Jang-Young</creatorcontrib><creatorcontrib>Kim, Hak-Sung</creatorcontrib><title>Production of L-DOPA(3,4-dihydroxyphenyl-L-alanine) from benzene by using a hybrid pathway</title><title>Biotechnology and bioengineering</title><addtitle>Biotechnol. Bioeng</addtitle><description>As an alternative approach to the production of L‐DOPA from a cheap raw material, we constructed a hybrid pathway consisting of toluene dioxygenase, toluene cis‐glycol dehydrogenase, and tyrosine phenol‐lyase. In this pathway, catechol is formed from benzene through the sequential action of toluene dioxygenase and toluene cis‐glycol dehydrogenase, and L‐DOPA is synthesized from the resulting catechol in the presence of pyruvate and ammonia by tyrosine phenol‐lyase cloned from Citrobacter freundii. When the hybrid pathway was expressed in E. coli, production of L‐DOPA was as low as 3 mM in 4 h due to the toxic effect of benzene on the cells. In order to reduce lysis of cells, Pseudomonas aeruginosa was employed as an alternative, which resulted in accumulation of about 14 mM L‐DOPA in 9 h, showing a stronger resistance to benzene. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 58:339–343, 1998.</description><subject>4-dihydroxyphenyl-L-alanine</subject><subject>Ammonia</subject><subject>Antiparkinson Agents - metabolism</subject><subject>Benzene</subject><subject>Benzene - metabolism</subject><subject>Cloning</subject><subject>Coliform bacteria</subject><subject>Drug products</subject><subject>Enzymes</subject><subject>Escherichia coli - enzymology</subject><subject>Genetic Engineering</subject><subject>hybrid pathway</subject><subject>L-DOPA</subject><subject>Levodopa - biosynthesis</subject><subject>L‐DOPA(3,4‐dihydroxyphenyl‐L‐alanine)</subject><subject>Oxidoreductases - genetics</subject><subject>Oxidoreductases - metabolism</subject><subject>Oxygenases - genetics</subject><subject>Oxygenases - metabolism</subject><subject>Pseudomonas aeruginosa - enzymology</subject><subject>Salts</subject><subject>toluene dioxygenase</subject><subject>Transfection</subject><subject>tyrosine phenol lyase</subject><subject>Tyrosine Phenol-Lyase - genetics</subject><subject>Tyrosine Phenol-Lyase - metabolism</subject><issn>0006-3592</issn><issn>1097-0290</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkW9v0zAQhy0EYmXwFVBeoVbC3flP7LggpC6FEamiEwyB-uZkN84aSJOSNNrCpyeh28Q7Xlnne-6n0z2EzBlMGQA_G39J4mTCwGgK3MCYGROB5DAJoxk_E2-FMLPZPFnQ8-RKqHdiCtN49YZT-YiMHqYekxEAKCpCw0_Is6b50Zc6UuopOWHADJNMjsj6sq7SdnPIqzKosmBJF6vL-Vi8ljTNt11aV7fdfuvLrqBLagtb5qWfBFld7QLny9--9IHrgrbJy-vABtvO1Xka7O1he2O75-RJZovGv7h7T8nXD--v4o90ubpI4vmSXkthFNXcRsyCMtoooYwKOZd2o7ywdpM5xb2FlDPgzkSORZyrKDTac-tMppzSTJySV8fcfV39an1zwF3ebHzRb-urtkHOhOCR0f8FmZKh0DCAL-_A1u18ivs639m6w_uz9cD6CNzkhe_-6ePgDwd9OIjAQQTe68MwQo4Ce33Y28O_9voaMF71DXn86MPpMTxvDv72IdzWP1FpoUP89ukC14vPCsJzht_FHwA6nxM</recordid><startdate>19980420</startdate><enddate>19980420</enddate><creator>Park, Hee-Sung</creator><creator>Lee, Jang-Young</creator><creator>Kim, Hak-Sung</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>19980420</creationdate><title>Production of L-DOPA(3,4-dihydroxyphenyl-L-alanine) from benzene by using a hybrid pathway</title><author>Park, Hee-Sung ; Lee, Jang-Young ; Kim, Hak-Sung</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-g4396-72a81a06979636965224ac6e3aacfb62ea0d2102b98b182268597e2ab9f6b6713</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>4-dihydroxyphenyl-L-alanine</topic><topic>Ammonia</topic><topic>Antiparkinson Agents - metabolism</topic><topic>Benzene</topic><topic>Benzene - metabolism</topic><topic>Cloning</topic><topic>Coliform bacteria</topic><topic>Drug products</topic><topic>Enzymes</topic><topic>Escherichia coli - enzymology</topic><topic>Genetic Engineering</topic><topic>hybrid pathway</topic><topic>L-DOPA</topic><topic>Levodopa - biosynthesis</topic><topic>L‐DOPA(3,4‐dihydroxyphenyl‐L‐alanine)</topic><topic>Oxidoreductases - genetics</topic><topic>Oxidoreductases - metabolism</topic><topic>Oxygenases - genetics</topic><topic>Oxygenases - metabolism</topic><topic>Pseudomonas aeruginosa - enzymology</topic><topic>Salts</topic><topic>toluene dioxygenase</topic><topic>Transfection</topic><topic>tyrosine phenol lyase</topic><topic>Tyrosine Phenol-Lyase - genetics</topic><topic>Tyrosine Phenol-Lyase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Park, Hee-Sung</creatorcontrib><creatorcontrib>Lee, Jang-Young</creatorcontrib><creatorcontrib>Kim, Hak-Sung</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Biotechnology and bioengineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Park, Hee-Sung</au><au>Lee, Jang-Young</au><au>Kim, Hak-Sung</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Production of L-DOPA(3,4-dihydroxyphenyl-L-alanine) from benzene by using a hybrid pathway</atitle><jtitle>Biotechnology and bioengineering</jtitle><addtitle>Biotechnol. Bioeng</addtitle><date>1998-04-20</date><risdate>1998</risdate><volume>58</volume><issue>2-3</issue><spage>339</spage><epage>343</epage><pages>339-343</pages><issn>0006-3592</issn><eissn>1097-0290</eissn><abstract>As an alternative approach to the production of L‐DOPA from a cheap raw material, we constructed a hybrid pathway consisting of toluene dioxygenase, toluene cis‐glycol dehydrogenase, and tyrosine phenol‐lyase. In this pathway, catechol is formed from benzene through the sequential action of toluene dioxygenase and toluene cis‐glycol dehydrogenase, and L‐DOPA is synthesized from the resulting catechol in the presence of pyruvate and ammonia by tyrosine phenol‐lyase cloned from Citrobacter freundii. When the hybrid pathway was expressed in E. coli, production of L‐DOPA was as low as 3 mM in 4 h due to the toxic effect of benzene on the cells. In order to reduce lysis of cells, Pseudomonas aeruginosa was employed as an alternative, which resulted in accumulation of about 14 mM L‐DOPA in 9 h, showing a stronger resistance to benzene. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 58:339–343, 1998.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>10191414</pmid><doi>10.1002/(SICI)1097-0290(19980420)58:2/3<339::AID-BIT36>3.0.CO;2-4</doi><tpages>5</tpages></addata></record> |
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| ispartof | Biotechnology and bioengineering, 1998-04, Vol.58 (2-3), p.339-343 |
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| source | MEDLINE; Wiley Journals |
| subjects | 4-dihydroxyphenyl-L-alanine Ammonia Antiparkinson Agents - metabolism Benzene Benzene - metabolism Cloning Coliform bacteria Drug products Enzymes Escherichia coli - enzymology Genetic Engineering hybrid pathway L-DOPA Levodopa - biosynthesis L‐DOPA(3,4‐dihydroxyphenyl‐L‐alanine) Oxidoreductases - genetics Oxidoreductases - metabolism Oxygenases - genetics Oxygenases - metabolism Pseudomonas aeruginosa - enzymology Salts toluene dioxygenase Transfection tyrosine phenol lyase Tyrosine Phenol-Lyase - genetics Tyrosine Phenol-Lyase - metabolism |
| title | Production of L-DOPA(3,4-dihydroxyphenyl-L-alanine) from benzene by using a hybrid pathway |
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