Development of an R-Selective Amine Oxidase with Broad Substrate Specificity and High Enantioselectivity
Amine oxidases are useful bio‐catalysts for the synthesis of enantiomerically pure 1°, 2° and 3° chiral amines. Enzymes in this class (e.g., MAO‐N from Aspergillus niger) reported previously have been shown to be highly S selective. Herein we report the development of an enantiocomplementary R‐selec...
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| Veröffentlicht in: | ChemCatChem 2014-04, Vol.6 (4), p.996-1002 |
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| creator | Heath, Rachel S. Pontini, Marta Bechi, Beatrice Turner, Nicholas J. |
| description | Amine oxidases are useful bio‐catalysts for the synthesis of enantiomerically pure 1°, 2° and 3° chiral amines. Enzymes in this class (e.g., MAO‐N from Aspergillus niger) reported previously have been shown to be highly S selective. Herein we report the development of an enantiocomplementary R‐selective amine oxidase based on 6‐hydroxy‐D‐nicotine oxidase (6‐HDNO) with broadened substrate scope and high enantioselectivity. The engineered 6‐HDNO enzyme has been applied to the preparative deracemisation of a range of racemic amines to yield S‐configured products, for example, (S)‐nicotine, in high ee.
Nicotine rush: An R‐selective amine oxidase based on 6‐hydroxy‐D‐nicotine oxidase (6‐HDNO) with broadened substrate scope and high enantioselectivity has been developed. The engineered 6‐HDNO enzyme is applied to the preparative deracemization of a range of racemic amines to yield S‐configured products, for example, (S)‐nicotine, in high ee. |
| doi_str_mv | 10.1002/cctc.201301008 |
| format | Article |
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Nicotine rush: An R‐selective amine oxidase based on 6‐hydroxy‐D‐nicotine oxidase (6‐HDNO) with broadened substrate scope and high enantioselectivity has been developed. The engineered 6‐HDNO enzyme is applied to the preparative deracemization of a range of racemic amines to yield S‐configured products, for example, (S)‐nicotine, in high ee.</description><identifier>ISSN: 1867-3880</identifier><identifier>EISSN: 1867-3899</identifier><identifier>DOI: 10.1002/cctc.201301008</identifier><language>eng</language><publisher>Weinheim: WILEY-VCH Verlag</publisher><subject>Amines ; biocatalysis ; Chemical synthesis ; Enantiomers ; enantioselectivity ; enzymes ; mutagenesis ; Nicotine ; Oxidase ; Substrates</subject><ispartof>ChemCatChem, 2014-04, Vol.6 (4), p.996-1002</ispartof><rights>2014 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>Copyright Wiley Subscription Services, Inc. Apr 2014</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3838-b9a5386f0ef6f2261c46011d593b27c2a1a457a5daa29c7318a60433dbe3d30a3</citedby><cites>FETCH-LOGICAL-c3838-b9a5386f0ef6f2261c46011d593b27c2a1a457a5daa29c7318a60433dbe3d30a3</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%2Fcctc.201301008$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fcctc.201301008$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids></links><search><creatorcontrib>Heath, Rachel S.</creatorcontrib><creatorcontrib>Pontini, Marta</creatorcontrib><creatorcontrib>Bechi, Beatrice</creatorcontrib><creatorcontrib>Turner, Nicholas J.</creatorcontrib><title>Development of an R-Selective Amine Oxidase with Broad Substrate Specificity and High Enantioselectivity</title><title>ChemCatChem</title><addtitle>ChemCatChem</addtitle><description>Amine oxidases are useful bio‐catalysts for the synthesis of enantiomerically pure 1°, 2° and 3° chiral amines. Enzymes in this class (e.g., MAO‐N from Aspergillus niger) reported previously have been shown to be highly S selective. Herein we report the development of an enantiocomplementary R‐selective amine oxidase based on 6‐hydroxy‐D‐nicotine oxidase (6‐HDNO) with broadened substrate scope and high enantioselectivity. The engineered 6‐HDNO enzyme has been applied to the preparative deracemisation of a range of racemic amines to yield S‐configured products, for example, (S)‐nicotine, in high ee.
Nicotine rush: An R‐selective amine oxidase based on 6‐hydroxy‐D‐nicotine oxidase (6‐HDNO) with broadened substrate scope and high enantioselectivity has been developed. The engineered 6‐HDNO enzyme is applied to the preparative deracemization of a range of racemic amines to yield S‐configured products, for example, (S)‐nicotine, in high ee.</description><subject>Amines</subject><subject>biocatalysis</subject><subject>Chemical synthesis</subject><subject>Enantiomers</subject><subject>enantioselectivity</subject><subject>enzymes</subject><subject>mutagenesis</subject><subject>Nicotine</subject><subject>Oxidase</subject><subject>Substrates</subject><issn>1867-3880</issn><issn>1867-3899</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><recordid>eNqFkc1PAjEQxTdGE_Hj6rmJ58V-7HbbIyyIJkSiaDw2pTsrRdjFtiD89y6BEE96mpnM-71J3kTRDcFtgjG9MyaYNsWE4WYUJ1GLCJ7FTEh5euwFPo8uvJ9hzCXL0lY07cEa5vVyAVVAdYl0hV7iMczBBLsG1FnYCtBoYwvtAX3bMEVdV-sCjVcTH5wOgMZLMLa0xoZtQxfowX5MUb_SVbC1Pxg1u6vorNRzD9eHehm93fdf84d4OBo85p1hbJhgIp5InTLBSwwlLynlxCQcE1Kkkk1oZqgmOkkznRZaU2kyRoTmOGGsmAArGNbsMrrd-y5d_bUCH9SsXrmqOakoFiwjCef8LxVJSZIwmUraqNp7lXG19w5KtXR2od1WEax2matd5uqYeQPIPfBt57D9R63y_DX_zcZ71voAmyOr3afiWfMr9f40UFR0X4a9bqqe2Q-lCZPj</recordid><startdate>201404</startdate><enddate>201404</enddate><creator>Heath, Rachel S.</creator><creator>Pontini, Marta</creator><creator>Bechi, Beatrice</creator><creator>Turner, Nicholas J.</creator><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>201404</creationdate><title>Development of an R-Selective Amine Oxidase with Broad Substrate Specificity and High Enantioselectivity</title><author>Heath, Rachel S. ; Pontini, Marta ; Bechi, Beatrice ; Turner, Nicholas J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3838-b9a5386f0ef6f2261c46011d593b27c2a1a457a5daa29c7318a60433dbe3d30a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amines</topic><topic>biocatalysis</topic><topic>Chemical synthesis</topic><topic>Enantiomers</topic><topic>enantioselectivity</topic><topic>enzymes</topic><topic>mutagenesis</topic><topic>Nicotine</topic><topic>Oxidase</topic><topic>Substrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Heath, Rachel S.</creatorcontrib><creatorcontrib>Pontini, Marta</creatorcontrib><creatorcontrib>Bechi, Beatrice</creatorcontrib><creatorcontrib>Turner, Nicholas J.</creatorcontrib><collection>Istex</collection><collection>CrossRef</collection><jtitle>ChemCatChem</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Heath, Rachel S.</au><au>Pontini, Marta</au><au>Bechi, Beatrice</au><au>Turner, Nicholas J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Development of an R-Selective Amine Oxidase with Broad Substrate Specificity and High Enantioselectivity</atitle><jtitle>ChemCatChem</jtitle><addtitle>ChemCatChem</addtitle><date>2014-04</date><risdate>2014</risdate><volume>6</volume><issue>4</issue><spage>996</spage><epage>1002</epage><pages>996-1002</pages><issn>1867-3880</issn><eissn>1867-3899</eissn><abstract>Amine oxidases are useful bio‐catalysts for the synthesis of enantiomerically pure 1°, 2° and 3° chiral amines. Enzymes in this class (e.g., MAO‐N from Aspergillus niger) reported previously have been shown to be highly S selective. Herein we report the development of an enantiocomplementary R‐selective amine oxidase based on 6‐hydroxy‐D‐nicotine oxidase (6‐HDNO) with broadened substrate scope and high enantioselectivity. The engineered 6‐HDNO enzyme has been applied to the preparative deracemisation of a range of racemic amines to yield S‐configured products, for example, (S)‐nicotine, in high ee.
Nicotine rush: An R‐selective amine oxidase based on 6‐hydroxy‐D‐nicotine oxidase (6‐HDNO) with broadened substrate scope and high enantioselectivity has been developed. The engineered 6‐HDNO enzyme is applied to the preparative deracemization of a range of racemic amines to yield S‐configured products, for example, (S)‐nicotine, in high ee.</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><doi>10.1002/cctc.201301008</doi><tpages>7</tpages></addata></record> |
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| source | Wiley Online Library Journals Frontfile Complete |
| subjects | Amines biocatalysis Chemical synthesis Enantiomers enantioselectivity enzymes mutagenesis Nicotine Oxidase Substrates |
| title | Development of an R-Selective Amine Oxidase with Broad Substrate Specificity and High Enantioselectivity |
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