Asymmetric Bioreduction of CC Bonds using Enoate Reductases OPR1, OPR3 and YqjM: Enzyme-Based Stereocontrol
Three cloned enoate reductases from the “old yellow enzyme” family of flavoproteins were investigated in the asymmetric bioreduction of activated alkenes. 12‐Oxophytodienoate reductase isoenzymes OPR1 and OPR3 from Lycopersicon esculentum (tomato), and YqjM from Bacillus subtilis displayed a remarka...
Gespeichert in:
| Veröffentlicht in: | Advanced synthesis & catalysis 2008-02, Vol.350 (3), p.411-418 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 418 |
|---|---|
| container_issue | 3 |
| container_start_page | 411 |
| container_title | Advanced synthesis & catalysis |
| container_volume | 350 |
| creator | Hall, Mélanie Stueckler, Clemens Ehammer, Heidemarie Pointner, Eva Oberdorfer, Gustav Gruber, Karl Hauer, Bernard Stuermer, Rainer Kroutil, Wolfgang Macheroux, Peter Faber, Kurt |
| description | Three cloned enoate reductases from the “old yellow enzyme” family of flavoproteins were investigated in the asymmetric bioreduction of activated alkenes. 12‐Oxophytodienoate reductase isoenzymes OPR1 and OPR3 from Lycopersicon esculentum (tomato), and YqjM from Bacillus subtilis displayed a remarkably broad substrate spectrum by reducing α,β‐unsaturated aldehydes, ketones, maleimides and nitroalkenes. The reaction proceeded with absolute chemoselectivity – only the conjugated CC bond was reduced, while isolated olefins and carbonyl groups remained intact – with excellent stereoselectivities (ees up to >99%). Upon reduction of a nitroalkene, the stereochemical outcome could be determined via choice of the appropriate enzyme (OPR1 versus OPR3 or YqjM), which furnished the corresponding enantiomeric nitroalkanes in excellent ee. Molecular modelling suggests that this “enzyme‐based stereocontrol” is caused by subtle differences within the active site geometries. |
| doi_str_mv | 10.1002/adsc.200700458 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_32130212</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>32130212</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4248-49c14edd4e5b22f17176831474ba39888f64742ba39886780afd827d0629efcc3</originalsourceid><addsrcrecordid>eNqFkMtOwzAQRSMEEs8ta69YkWI7Tuywa8NTgoJKEYKNZewJCiRxa6eC8jv8B7_EL5ASVLFjM3NHOmcWNwh2Ce4RjOmBMl73KMYcYxaLlWCDJCQOGUnS1WWO8Xqw6f0zxoQLzjeCuu_nVQWNKzQaFNaBmemmsDWyOcq-Pj4zNLC18Wjmi_oJHddWNYBGP5Ty4NHV9YjsL2aEVG3Q_fT58rDF3ucVhIOWMOimAQdW27pxttwO1nJVetj53VvB7cnxODsLL65Oz7P-RagZZSJkqSYMjGEQP1KaE054IiLCOHtUUSqEyJM20-5IuMAqN4JygxOaQq51tBXsdX8nzk5n4BtZFV5DWaoa7MzLiJIIU0JbsNeB2lnvHeRy4opKubkkWC5qlYta5bLWVkg74bUoYf4PLftHN9lfN-zcwjfwtnSVe5EJj3gs74ancvwwGsacCDmIvgE3AIse</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>32130212</pqid></control><display><type>article</type><title>Asymmetric Bioreduction of CC Bonds using Enoate Reductases OPR1, OPR3 and YqjM: Enzyme-Based Stereocontrol</title><source>Wiley Online Library All Journals</source><creator>Hall, Mélanie ; Stueckler, Clemens ; Ehammer, Heidemarie ; Pointner, Eva ; Oberdorfer, Gustav ; Gruber, Karl ; Hauer, Bernard ; Stuermer, Rainer ; Kroutil, Wolfgang ; Macheroux, Peter ; Faber, Kurt</creator><creatorcontrib>Hall, Mélanie ; Stueckler, Clemens ; Ehammer, Heidemarie ; Pointner, Eva ; Oberdorfer, Gustav ; Gruber, Karl ; Hauer, Bernard ; Stuermer, Rainer ; Kroutil, Wolfgang ; Macheroux, Peter ; Faber, Kurt</creatorcontrib><description>Three cloned enoate reductases from the “old yellow enzyme” family of flavoproteins were investigated in the asymmetric bioreduction of activated alkenes. 12‐Oxophytodienoate reductase isoenzymes OPR1 and OPR3 from Lycopersicon esculentum (tomato), and YqjM from Bacillus subtilis displayed a remarkably broad substrate spectrum by reducing α,β‐unsaturated aldehydes, ketones, maleimides and nitroalkenes. The reaction proceeded with absolute chemoselectivity – only the conjugated CC bond was reduced, while isolated olefins and carbonyl groups remained intact – with excellent stereoselectivities (ees up to >99%). Upon reduction of a nitroalkene, the stereochemical outcome could be determined via choice of the appropriate enzyme (OPR1 versus OPR3 or YqjM), which furnished the corresponding enantiomeric nitroalkanes in excellent ee. Molecular modelling suggests that this “enzyme‐based stereocontrol” is caused by subtle differences within the active site geometries.</description><identifier>ISSN: 1615-4150</identifier><identifier>EISSN: 1615-4169</identifier><identifier>DOI: 10.1002/adsc.200700458</identifier><language>eng</language><publisher>Weinheim: WILEY-VCH Verlag</publisher><subject>asymmetric bioreduction ; enoate reductase ; nitroalkenes ; old yellow enzyme ; stereocomplementary process ; α,β‐unsaturated carbonyl compounds ; β-unsaturated carbonyl compounds</subject><ispartof>Advanced synthesis & catalysis, 2008-02, Vol.350 (3), p.411-418</ispartof><rights>Copyright © 2008 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4248-49c14edd4e5b22f17176831474ba39888f64742ba39886780afd827d0629efcc3</citedby><cites>FETCH-LOGICAL-c4248-49c14edd4e5b22f17176831474ba39888f64742ba39886780afd827d0629efcc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fadsc.200700458$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fadsc.200700458$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids></links><search><creatorcontrib>Hall, Mélanie</creatorcontrib><creatorcontrib>Stueckler, Clemens</creatorcontrib><creatorcontrib>Ehammer, Heidemarie</creatorcontrib><creatorcontrib>Pointner, Eva</creatorcontrib><creatorcontrib>Oberdorfer, Gustav</creatorcontrib><creatorcontrib>Gruber, Karl</creatorcontrib><creatorcontrib>Hauer, Bernard</creatorcontrib><creatorcontrib>Stuermer, Rainer</creatorcontrib><creatorcontrib>Kroutil, Wolfgang</creatorcontrib><creatorcontrib>Macheroux, Peter</creatorcontrib><creatorcontrib>Faber, Kurt</creatorcontrib><title>Asymmetric Bioreduction of CC Bonds using Enoate Reductases OPR1, OPR3 and YqjM: Enzyme-Based Stereocontrol</title><title>Advanced synthesis & catalysis</title><addtitle>Adv. Synth. Catal</addtitle><description>Three cloned enoate reductases from the “old yellow enzyme” family of flavoproteins were investigated in the asymmetric bioreduction of activated alkenes. 12‐Oxophytodienoate reductase isoenzymes OPR1 and OPR3 from Lycopersicon esculentum (tomato), and YqjM from Bacillus subtilis displayed a remarkably broad substrate spectrum by reducing α,β‐unsaturated aldehydes, ketones, maleimides and nitroalkenes. The reaction proceeded with absolute chemoselectivity – only the conjugated CC bond was reduced, while isolated olefins and carbonyl groups remained intact – with excellent stereoselectivities (ees up to >99%). Upon reduction of a nitroalkene, the stereochemical outcome could be determined via choice of the appropriate enzyme (OPR1 versus OPR3 or YqjM), which furnished the corresponding enantiomeric nitroalkanes in excellent ee. Molecular modelling suggests that this “enzyme‐based stereocontrol” is caused by subtle differences within the active site geometries.</description><subject>asymmetric bioreduction</subject><subject>enoate reductase</subject><subject>nitroalkenes</subject><subject>old yellow enzyme</subject><subject>stereocomplementary process</subject><subject>α,β‐unsaturated carbonyl compounds</subject><subject>β-unsaturated carbonyl compounds</subject><issn>1615-4150</issn><issn>1615-4169</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><recordid>eNqFkMtOwzAQRSMEEs8ta69YkWI7Tuywa8NTgoJKEYKNZewJCiRxa6eC8jv8B7_EL5ASVLFjM3NHOmcWNwh2Ce4RjOmBMl73KMYcYxaLlWCDJCQOGUnS1WWO8Xqw6f0zxoQLzjeCuu_nVQWNKzQaFNaBmemmsDWyOcq-Pj4zNLC18Wjmi_oJHddWNYBGP5Ty4NHV9YjsL2aEVG3Q_fT58rDF3ucVhIOWMOimAQdW27pxttwO1nJVetj53VvB7cnxODsLL65Oz7P-RagZZSJkqSYMjGEQP1KaE054IiLCOHtUUSqEyJM20-5IuMAqN4JygxOaQq51tBXsdX8nzk5n4BtZFV5DWaoa7MzLiJIIU0JbsNeB2lnvHeRy4opKubkkWC5qlYta5bLWVkg74bUoYf4PLftHN9lfN-zcwjfwtnSVe5EJj3gs74ancvwwGsacCDmIvgE3AIse</recordid><startdate>20080222</startdate><enddate>20080222</enddate><creator>Hall, Mélanie</creator><creator>Stueckler, Clemens</creator><creator>Ehammer, Heidemarie</creator><creator>Pointner, Eva</creator><creator>Oberdorfer, Gustav</creator><creator>Gruber, Karl</creator><creator>Hauer, Bernard</creator><creator>Stuermer, Rainer</creator><creator>Kroutil, Wolfgang</creator><creator>Macheroux, Peter</creator><creator>Faber, Kurt</creator><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><scope>BSCLL</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7U5</scope><scope>8FD</scope><scope>L7M</scope></search><sort><creationdate>20080222</creationdate><title>Asymmetric Bioreduction of CC Bonds using Enoate Reductases OPR1, OPR3 and YqjM: Enzyme-Based Stereocontrol</title><author>Hall, Mélanie ; Stueckler, Clemens ; Ehammer, Heidemarie ; Pointner, Eva ; Oberdorfer, Gustav ; Gruber, Karl ; Hauer, Bernard ; Stuermer, Rainer ; Kroutil, Wolfgang ; Macheroux, Peter ; Faber, Kurt</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4248-49c14edd4e5b22f17176831474ba39888f64742ba39886780afd827d0629efcc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>asymmetric bioreduction</topic><topic>enoate reductase</topic><topic>nitroalkenes</topic><topic>old yellow enzyme</topic><topic>stereocomplementary process</topic><topic>α,β‐unsaturated carbonyl compounds</topic><topic>β-unsaturated carbonyl compounds</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hall, Mélanie</creatorcontrib><creatorcontrib>Stueckler, Clemens</creatorcontrib><creatorcontrib>Ehammer, Heidemarie</creatorcontrib><creatorcontrib>Pointner, Eva</creatorcontrib><creatorcontrib>Oberdorfer, Gustav</creatorcontrib><creatorcontrib>Gruber, Karl</creatorcontrib><creatorcontrib>Hauer, Bernard</creatorcontrib><creatorcontrib>Stuermer, Rainer</creatorcontrib><creatorcontrib>Kroutil, Wolfgang</creatorcontrib><creatorcontrib>Macheroux, Peter</creatorcontrib><creatorcontrib>Faber, Kurt</creatorcontrib><collection>Istex</collection><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Advanced synthesis & catalysis</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hall, Mélanie</au><au>Stueckler, Clemens</au><au>Ehammer, Heidemarie</au><au>Pointner, Eva</au><au>Oberdorfer, Gustav</au><au>Gruber, Karl</au><au>Hauer, Bernard</au><au>Stuermer, Rainer</au><au>Kroutil, Wolfgang</au><au>Macheroux, Peter</au><au>Faber, Kurt</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Asymmetric Bioreduction of CC Bonds using Enoate Reductases OPR1, OPR3 and YqjM: Enzyme-Based Stereocontrol</atitle><jtitle>Advanced synthesis & catalysis</jtitle><addtitle>Adv. Synth. Catal</addtitle><date>2008-02-22</date><risdate>2008</risdate><volume>350</volume><issue>3</issue><spage>411</spage><epage>418</epage><pages>411-418</pages><issn>1615-4150</issn><eissn>1615-4169</eissn><abstract>Three cloned enoate reductases from the “old yellow enzyme” family of flavoproteins were investigated in the asymmetric bioreduction of activated alkenes. 12‐Oxophytodienoate reductase isoenzymes OPR1 and OPR3 from Lycopersicon esculentum (tomato), and YqjM from Bacillus subtilis displayed a remarkably broad substrate spectrum by reducing α,β‐unsaturated aldehydes, ketones, maleimides and nitroalkenes. The reaction proceeded with absolute chemoselectivity – only the conjugated CC bond was reduced, while isolated olefins and carbonyl groups remained intact – with excellent stereoselectivities (ees up to >99%). Upon reduction of a nitroalkene, the stereochemical outcome could be determined via choice of the appropriate enzyme (OPR1 versus OPR3 or YqjM), which furnished the corresponding enantiomeric nitroalkanes in excellent ee. Molecular modelling suggests that this “enzyme‐based stereocontrol” is caused by subtle differences within the active site geometries.</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><doi>10.1002/adsc.200700458</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1615-4150 |
| ispartof | Advanced synthesis & catalysis, 2008-02, Vol.350 (3), p.411-418 |
| issn | 1615-4150 1615-4169 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_32130212 |
| source | Wiley Online Library All Journals |
| subjects | asymmetric bioreduction enoate reductase nitroalkenes old yellow enzyme stereocomplementary process α,β‐unsaturated carbonyl compounds β-unsaturated carbonyl compounds |
| title | Asymmetric Bioreduction of CC Bonds using Enoate Reductases OPR1, OPR3 and YqjM: Enzyme-Based Stereocontrol |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-06T00%3A19%3A48IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Asymmetric%20Bioreduction%20of%20C%EF%A3%BEC%20Bonds%20using%20Enoate%20Reductases%20OPR1,%20OPR3%20and%20YqjM:%20Enzyme-Based%20Stereocontrol&rft.jtitle=Advanced%20synthesis%20&%20catalysis&rft.au=Hall,%20M%C3%A9lanie&rft.date=2008-02-22&rft.volume=350&rft.issue=3&rft.spage=411&rft.epage=418&rft.pages=411-418&rft.issn=1615-4150&rft.eissn=1615-4169&rft_id=info:doi/10.1002/adsc.200700458&rft_dat=%3Cproquest_cross%3E32130212%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=32130212&rft_id=info:pmid/&rfr_iscdi=true |