Complex of Burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane: biocatalytic, structural and modelling study
In a series of four racemic phenoxyalkyl-alkyl carbinols, 1-phenoxy-2-hydroxybutane (1) is enantioselectively acetylated by Burkholderia cepacia (formerly Pseudomonas cepacia) lipase with an E value > or = 200, whereas for the other three racemates E was found to be < or = 4. To explain the hi...
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| Veröffentlicht in: | European journal of biochemistry 2001-07, Vol.268 (14), p.3964-3973 |
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| container_title | European journal of biochemistry |
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| creator | Luić, M Tomić, S Lescić, I Ljubović, E Sepac, D Sunjić, V Vitale, L Saenger, W Kojic-Prodić, B |
| description | In a series of four racemic phenoxyalkyl-alkyl carbinols, 1-phenoxy-2-hydroxybutane (1) is enantioselectively acetylated by Burkholderia cepacia (formerly Pseudomonas cepacia) lipase with an E value > or = 200, whereas for the other three racemates E was found to be < or = 4. To explain the high preference of B. cepacia lipase for (R)-(+)-1, a precursor of its transition state analogue with a tetrahedral P-atom, (R(P),S(P))-O-(2R)-(1-phenoxybut-2-yl)methylphosphonic acid chloride was prepared and crystallized in complex with B. cepacia lipase. The X-ray structure of the complex was determined, allowing to compare the conformation of the inhibitor with results of molecular modelling. |
| doi_str_mv | 10.1046/j.1432-1327.2001.02303.x |
| format | Article |
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To explain the high preference of B. cepacia lipase for (R)-(+)-1, a precursor of its transition state analogue with a tetrahedral P-atom, (R(P),S(P))-O-(2R)-(1-phenoxybut-2-yl)methylphosphonic acid chloride was prepared and crystallized in complex with B. cepacia lipase. 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To explain the high preference of B. cepacia lipase for (R)-(+)-1, a precursor of its transition state analogue with a tetrahedral P-atom, (R(P),S(P))-O-(2R)-(1-phenoxybut-2-yl)methylphosphonic acid chloride was prepared and crystallized in complex with B. cepacia lipase. The X-ray structure of the complex was determined, allowing to compare the conformation of the inhibitor with results of molecular modelling.</description><subject>Burkholderia cepacia - enzymology</subject><subject>Catalysis</subject><subject>Crystallography, X-Ray</subject><subject>Hydrogen Bonding</subject><subject>Lipase - antagonists & inhibitors</subject><subject>Lipase - chemistry</subject><subject>Lipase - metabolism</subject><subject>Models, Molecular</subject><subject>Organophosphorus Compounds - metabolism</subject><subject>Stereoisomerism</subject><subject>Substrate Specificity</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFu1DAURa0KRKeFX6i8YkWCn52xE3YwailSJTawtl4cp-MhiYPtiJm_4JNxmJFYsnqW7j32kw8hFFgJrJLvDyVUghcguCo5Y1AyLpgoj1dkcw6YEC_IJidVwZutvCY3MR4YY7KR6hW5Bqi2omnYhvze-XEe7JH6nn5awo-9HzobHFJjZzR5Dm7GaOkvl_Y0BZyiS85PNCZMluKEg39e7EpDMe_t5I-nghdobMqndkk42Q-0dd5gwuGUnHmX0bCYtAQcMt_R0Xd2GNz0nIOlO70mL3scon1zmbfk-8P9t91j8fT185fdx6fC8FqlwijZGth2toMeKwlGCai3spccTf4B3vbYg5IKaylNi6oSvZQArW1U1wslxC15e753Dv7nYmPSo4smb5I39kvUChhIXv-_CLVs6rpWuVifiyb4GIPt9RzciOGkgelVmz7o1Y5etelVm_6rTR8zend5Y2lH2_0DL57EH8wdl1g</recordid><startdate>20010701</startdate><enddate>20010701</enddate><creator>Luić, M</creator><creator>Tomić, S</creator><creator>Lescić, I</creator><creator>Ljubović, E</creator><creator>Sepac, D</creator><creator>Sunjić, V</creator><creator>Vitale, L</creator><creator>Saenger, W</creator><creator>Kojic-Prodić, B</creator><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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20010701</creationdate><title>Complex of Burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane: biocatalytic, structural and modelling study</title><author>Luić, M ; Tomić, S ; Lescić, I ; Ljubović, E ; Sepac, D ; Sunjić, V ; Vitale, L ; Saenger, W ; Kojic-Prodić, B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c287t-c76bc15ded1fa461c731856f62ac4322bfaf1767a866cba743f6611be97df3733</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Burkholderia cepacia - enzymology</topic><topic>Catalysis</topic><topic>Crystallography, X-Ray</topic><topic>Hydrogen Bonding</topic><topic>Lipase - antagonists & inhibitors</topic><topic>Lipase - chemistry</topic><topic>Lipase - metabolism</topic><topic>Models, Molecular</topic><topic>Organophosphorus Compounds - metabolism</topic><topic>Stereoisomerism</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Luić, M</creatorcontrib><creatorcontrib>Tomić, S</creatorcontrib><creatorcontrib>Lescić, I</creatorcontrib><creatorcontrib>Ljubović, E</creatorcontrib><creatorcontrib>Sepac, D</creatorcontrib><creatorcontrib>Sunjić, V</creatorcontrib><creatorcontrib>Vitale, L</creatorcontrib><creatorcontrib>Saenger, W</creatorcontrib><creatorcontrib>Kojic-Prodić, B</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Luić, M</au><au>Tomić, S</au><au>Lescić, I</au><au>Ljubović, E</au><au>Sepac, D</au><au>Sunjić, V</au><au>Vitale, L</au><au>Saenger, W</au><au>Kojic-Prodić, B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Complex of Burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane: biocatalytic, structural and modelling study</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>2001-07-01</date><risdate>2001</risdate><volume>268</volume><issue>14</issue><spage>3964</spage><epage>3973</epage><pages>3964-3973</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>In a series of four racemic phenoxyalkyl-alkyl carbinols, 1-phenoxy-2-hydroxybutane (1) is enantioselectively acetylated by Burkholderia cepacia (formerly Pseudomonas cepacia) lipase with an E value > or = 200, whereas for the other three racemates E was found to be < or = 4. To explain the high preference of B. cepacia lipase for (R)-(+)-1, a precursor of its transition state analogue with a tetrahedral P-atom, (R(P),S(P))-O-(2R)-(1-phenoxybut-2-yl)methylphosphonic acid chloride was prepared and crystallized in complex with B. cepacia lipase. The X-ray structure of the complex was determined, allowing to compare the conformation of the inhibitor with results of molecular modelling.</abstract><cop>England</cop><pmid>11453990</pmid><doi>10.1046/j.1432-1327.2001.02303.x</doi><tpages>10</tpages></addata></record> |
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| ispartof | European journal of biochemistry, 2001-07, Vol.268 (14), p.3964-3973 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Burkholderia cepacia - enzymology Catalysis Crystallography, X-Ray Hydrogen Bonding Lipase - antagonists & inhibitors Lipase - chemistry Lipase - metabolism Models, Molecular Organophosphorus Compounds - metabolism Stereoisomerism Substrate Specificity |
| title | Complex of Burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane: biocatalytic, structural and modelling study |
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