Purification and characterization of a highly enantioselective epoxide hydrolase from Aspergillus niger
The epoxide hydrolase from Aspergillus niger was purified to homogeneity using a four‐step procedure and p‐nitrostyrene oxide (pNSO) as substrate. The enzyme was purified 246‐fold with 4% activity yield. The protein is a tetramer composed of four identical subunits of molecular mass 45 kDa. Maximum...
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| Veröffentlicht in: | European journal of biochemistry 1999-07, Vol.263 (2), p.386-395 |
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| container_title | European journal of biochemistry |
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| creator | Morisseau, C Archelas, A Guitton, C Faucher, D Furstoss, R Baratti, J.C |
| description | The epoxide hydrolase from Aspergillus niger was purified to homogeneity using a four‐step procedure and p‐nitrostyrene oxide (pNSO) as substrate. The enzyme was purified 246‐fold with 4% activity yield. The protein is a tetramer composed of four identical subunits of molecular mass 45 kDa. Maximum activity was observed at 40 °C, pH 7.0, and with dimethylformamide as cosolvent to dissolve pNSO. Hydrolysis of pNSO was highly enantioselective, with an E value (i.e. enantiomeric ratio) of 40 and a high regioselectivity (97%) for the less hindered carbon atom of the epoxide. This enzyme may be a good biocatalyst for the preparation of enantiopure epoxides or diols. |
| doi_str_mv | 10.1046/j.1432-1327.1999.00519.x |
| format | Article |
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The enzyme was purified 246‐fold with 4% activity yield. The protein is a tetramer composed of four identical subunits of molecular mass 45 kDa. Maximum activity was observed at 40 °C, pH 7.0, and with dimethylformamide as cosolvent to dissolve pNSO. Hydrolysis of pNSO was highly enantioselective, with an E value (i.e. enantiomeric ratio) of 40 and a high regioselectivity (97%) for the less hindered carbon atom of the epoxide. 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The enzyme was purified 246‐fold with 4% activity yield. The protein is a tetramer composed of four identical subunits of molecular mass 45 kDa. Maximum activity was observed at 40 °C, pH 7.0, and with dimethylformamide as cosolvent to dissolve pNSO. Hydrolysis of pNSO was highly enantioselective, with an E value (i.e. enantiomeric ratio) of 40 and a high regioselectivity (97%) for the less hindered carbon atom of the epoxide. This enzyme may be a good biocatalyst for the preparation of enantiopure epoxides or diols.</description><subject>Amino Acid Sequence</subject><subject>Amino Acids - chemistry</subject><subject>Aspergillus niger</subject><subject>Aspergillus niger - enzymology</subject><subject>Base Sequence</subject><subject>diols</subject><subject>Dose-Response Relationship, Drug</subject><subject>enantioselectivity</subject><subject>epoxide hydrolase</subject><subject>Epoxide Hydrolases - chemistry</subject><subject>Epoxide Hydrolases - isolation & purification</subject><subject>Epoxy Compounds - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Models, Chemical</subject><subject>Molecular Sequence Data</subject><subject>plant biochemistry</subject><subject>plant physiology</subject><subject>regioselectivity</subject><subject>Temperature</subject><subject>Time Factors</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUFv1DAQhS0EokvLXwCfuCWM48SODxxK1QJSpSK1PVuOPcl6lY0XewO7_Hq8pAdu9OTR-HvP1nuEUAYlg1p83JSs5lXBeCVLppQqARqmysMLslougPOXZAXA6qJSjTgjb1LaAIBQQr4mZ9kkj7VYkeH7HH3vrdn7MFEzOWrXJhq7x-h_L8vQU0PXfliPR4qTmfIy4Yh2738ixV04eId0fXQxjCYh7WPY0su0wzj4cZwTnfyA8YK86s2Y8O3TeU4eb64frr4Wt3dfvl1d3ha2rkAVyBvBqg7Q8M46pTqnbIMdSAmyx0bUtoUWleuqLoOtQawZQykdV6wT6Pg5-bD47mL4MWPa661PFsfRTBjmpIVqFUhe_RdksgYlgWWwXUAbQ0oRe72LfmviUTPQpzb0Rp9C16c29KkN_bcNfcjSd09vzN0W3T_CJf4MfFqAX37E47ON9c315_s8Zf37Rd-boM0QfdKP91X-NFQqJyKA_wESLqQg</recordid><startdate>199907</startdate><enddate>199907</enddate><creator>Morisseau, C</creator><creator>Archelas, A</creator><creator>Guitton, C</creator><creator>Faucher, D</creator><creator>Furstoss, R</creator><creator>Baratti, J.C</creator><general>Blackwell Science Ltd</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>199907</creationdate><title>Purification and characterization of a highly enantioselective epoxide hydrolase from Aspergillus niger</title><author>Morisseau, C ; Archelas, A ; Guitton, C ; Faucher, D ; Furstoss, R ; Baratti, J.C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4209-e35612b0ea3bcd99bd9c5eb07707fe564c808e9db2b5618aee411e77d391b6ed3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acids - chemistry</topic><topic>Aspergillus niger</topic><topic>Aspergillus niger - enzymology</topic><topic>Base Sequence</topic><topic>diols</topic><topic>Dose-Response Relationship, Drug</topic><topic>enantioselectivity</topic><topic>epoxide hydrolase</topic><topic>Epoxide Hydrolases - chemistry</topic><topic>Epoxide Hydrolases - isolation & purification</topic><topic>Epoxy Compounds - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Models, Chemical</topic><topic>Molecular Sequence Data</topic><topic>plant biochemistry</topic><topic>plant physiology</topic><topic>regioselectivity</topic><topic>Temperature</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Morisseau, C</creatorcontrib><creatorcontrib>Archelas, A</creatorcontrib><creatorcontrib>Guitton, C</creatorcontrib><creatorcontrib>Faucher, D</creatorcontrib><creatorcontrib>Furstoss, R</creatorcontrib><creatorcontrib>Baratti, J.C</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Morisseau, C</au><au>Archelas, A</au><au>Guitton, C</au><au>Faucher, D</au><au>Furstoss, R</au><au>Baratti, J.C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of a highly enantioselective epoxide hydrolase from Aspergillus niger</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1999-07</date><risdate>1999</risdate><volume>263</volume><issue>2</issue><spage>386</spage><epage>395</epage><pages>386-395</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>The epoxide hydrolase from Aspergillus niger was purified to homogeneity using a four‐step procedure and p‐nitrostyrene oxide (pNSO) as substrate. The enzyme was purified 246‐fold with 4% activity yield. The protein is a tetramer composed of four identical subunits of molecular mass 45 kDa. Maximum activity was observed at 40 °C, pH 7.0, and with dimethylformamide as cosolvent to dissolve pNSO. Hydrolysis of pNSO was highly enantioselective, with an E value (i.e. enantiomeric ratio) of 40 and a high regioselectivity (97%) for the less hindered carbon atom of the epoxide. This enzyme may be a good biocatalyst for the preparation of enantiopure epoxides or diols.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>10406946</pmid><doi>10.1046/j.1432-1327.1999.00519.x</doi><tpages>10</tpages></addata></record> |
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| ispartof | European journal of biochemistry, 1999-07, Vol.263 (2), p.386-395 |
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| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Amino Acids - chemistry Aspergillus niger Aspergillus niger - enzymology Base Sequence diols Dose-Response Relationship, Drug enantioselectivity epoxide hydrolase Epoxide Hydrolases - chemistry Epoxide Hydrolases - isolation & purification Epoxy Compounds - metabolism Hydrogen-Ion Concentration Kinetics Models, Chemical Molecular Sequence Data plant biochemistry plant physiology regioselectivity Temperature Time Factors |
| title | Purification and characterization of a highly enantioselective epoxide hydrolase from Aspergillus niger |
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