Purification and molecular cloning of an intracellular 3-hydroxybutyrate-oligomer hydrolase from Paucimonas lemoignei
An intracellular 3-hydroxybutyrate-oligomer hydrolase was purified from a poly(3-hydroxybutyrate)-degrading bacterium, Paucimonas lemoignei. It hydrolyzed the 3-hydroxybutyrate dimer with the highest specific activity of any of the enzymes reported so far. The gene was cloned and sequenced. The dedu...
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Veröffentlicht in: | Journal of bioscience and bioengineering 2007-09, Vol.104 (3), p.224-226 |
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container_title | Journal of bioscience and bioengineering |
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creator | Uchino, Keiichi Katsumata, Yoko Takeda, Tomoko Arai, Hiroki Shiraki, Mari Saito, Terumi |
description | An intracellular 3-hydroxybutyrate-oligomer hydrolase was purified from a poly(3-hydroxybutyrate)-degrading bacterium,
Paucimonas lemoignei. It hydrolyzed the 3-hydroxybutyrate dimer with the highest specific activity of any of the enzymes reported so far. The gene was cloned and sequenced. The deduced amino acid sequence showed that the enzyme is a homolog of the PhaZc of
Ralstonia eutropha H16. |
doi_str_mv | 10.1263/jbb.104.224 |
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Paucimonas lemoignei. It hydrolyzed the 3-hydroxybutyrate dimer with the highest specific activity of any of the enzymes reported so far. The gene was cloned and sequenced. The deduced amino acid sequence showed that the enzyme is a homolog of the PhaZc of
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Paucimonas lemoignei. It hydrolyzed the 3-hydroxybutyrate dimer with the highest specific activity of any of the enzymes reported so far. The gene was cloned and sequenced. The deduced amino acid sequence showed that the enzyme is a homolog of the PhaZc of
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Psychology</subject><subject>gene cloning</subject><subject>HIDROLASAS</subject><subject>HYDROLASE</subject><subject>HYDROLASES</subject><subject>Hydrolases - chemistry</subject><subject>Hydrolases - genetics</subject><subject>MOLECULAR CLONING</subject><subject>Paucimonas lemoignei</subject><subject>PhaZc</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>Ralstonia eutropha</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>SECUENCIAS DE AMINOACIDOS</subject><subject>SEQUENCE D'ACIDES AMINES</subject><subject>Substrate Specificity</subject><subject>Transfection - methods</subject><issn>1389-1723</issn><issn>1347-4421</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc2LFDEQxYMo7jp68qw0iF6WHjsf3Z0cl8WPlQXnoOdQnVSPGdLJmnSL899vZmdgQYQ9VcH7Ubx6j5DXtFlT1vGPu2FY00asGRNPyDnloq-FYPTpYZeqpj3jZ-RFzrumoX3T0-fkjPaqE0LKc7JsluRGZ2B2MVQQbDVFj2bxkCrjY3BhW8WxCJULcwKD3t9rvP61tyn-3Q_LvE8wYx2928YJU3UveMhYjSlO1QYW46YYIFcep-i2Ad1L8mwEn_HVaa7Iz8-fflx9rW--f7m-urypTcvbue4Hw83QD20D1FrLgUup2kGxwXY9s0IxNKxvUVguKDNdM1orBecNSNMpbviKfDjevU3x94J51pPLhx8gYFyy7mRJinXtoyAr2UmqugK--wfcxSWF8oSmQlDOSrCqUBdHyqSYc8JR3yY3Qdpr2uhDabqUVnahS2mFfnu6uQwT2gf21FIB3p8AyAb8mCAYlx84RXkr2wP35siNEDVsU2G-bYp1WdyLAq1Ie9SxZP7HYdLZOAwGrUtoZm2j-6_BO-C6u6Q</recordid><startdate>20070901</startdate><enddate>20070901</enddate><creator>Uchino, Keiichi</creator><creator>Katsumata, Yoko</creator><creator>Takeda, Tomoko</creator><creator>Arai, Hiroki</creator><creator>Shiraki, Mari</creator><creator>Saito, Terumi</creator><general>Elsevier B.V</general><general>Elsevier Science</general><general>Elsevier Limited</general><scope>FBQ</scope><scope>IQODW</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>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20070901</creationdate><title>Purification and molecular cloning of an intracellular 3-hydroxybutyrate-oligomer hydrolase from Paucimonas lemoignei</title><author>Uchino, Keiichi ; Katsumata, Yoko ; Takeda, Tomoko ; Arai, Hiroki ; Shiraki, Mari ; Saito, Terumi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c535t-7bc3cb7b50a1ddd3a38895b92bd672d492ec275e4d3412c60fdd84330a8c693c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>3-hydroxybutyrate-oligomer hydrolase</topic><topic>3-Hydroxybutyric Acid - chemistry</topic><topic>AMINO ACID SEQUENCES</topic><topic>BACTERIA</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Burkholderia - enzymology</topic><topic>Burkholderia - genetics</topic><topic>CLONACION MOLECULAR</topic><topic>CLONAGE MOLECULAIRE</topic><topic>Cloning, Molecular - methods</topic><topic>Dimerization</topic><topic>Enzyme Activation</topic><topic>Enzyme Stability</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. 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Paucimonas lemoignei. It hydrolyzed the 3-hydroxybutyrate dimer with the highest specific activity of any of the enzymes reported so far. The gene was cloned and sequenced. The deduced amino acid sequence showed that the enzyme is a homolog of the PhaZc of
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subjects | 3-hydroxybutyrate-oligomer hydrolase 3-Hydroxybutyric Acid - chemistry AMINO ACID SEQUENCES BACTERIA Biological and medical sciences Biotechnology Burkholderia - enzymology Burkholderia - genetics CLONACION MOLECULAR CLONAGE MOLECULAIRE Cloning, Molecular - methods Dimerization Enzyme Activation Enzyme Stability Escherichia coli - enzymology Escherichia coli - genetics Fundamental and applied biological sciences. Psychology gene cloning HIDROLASAS HYDROLASE HYDROLASES Hydrolases - chemistry Hydrolases - genetics MOLECULAR CLONING Paucimonas lemoignei PhaZc PURIFICACION PURIFICATION Ralstonia eutropha Recombinant Proteins - chemistry Recombinant Proteins - metabolism SECUENCIAS DE AMINOACIDOS SEQUENCE D'ACIDES AMINES Substrate Specificity Transfection - methods |
title | Purification and molecular cloning of an intracellular 3-hydroxybutyrate-oligomer hydrolase from Paucimonas lemoignei |
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