Structure of catechol 2,3-dioxygenase gene encoded in chromosomal DNA of Pseudomonas putida KF715
A catechol 2,3-dioxygenase gene in chromosomal DNA of P. putida KF715 was cloned and its nucleotide sequence analyzed. The enzyme gene was composed of 924 base pairs with ATG initiation codon and TGA termination codon, which can encode a polypeptide of molecular weight 35 kDa containing 307 amino ac...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1996-07, Vol.224 (3), p.831-836 |
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| creator | Lee, J Oh, J Min, K R Kim, C K Min, K H Lee, K S Kim, Y C Lim, J Y Kim, Y |
| description | A catechol 2,3-dioxygenase gene in chromosomal DNA of P. putida KF715 was cloned and its nucleotide sequence analyzed. The enzyme gene was composed of 924 base pairs with ATG initiation codon and TGA termination codon, which can encode a polypeptide of molecular weight 35 kDa containing 307 amino acids. A promoter-like sequence and a ribosome-binding sequence were identified upstream the enzyme gene. A deduced amino acid sequence of the catechol 2,3-dioxygenase exhibited 94% identity with that of corresponding enzyme in TOL plasmid and 25% identity with that of 2,3-dihydroxybiphenyl 1,2-dioxygenase from the same strain. Furthermore, sequence comparison of the catechol 2,3-dioxygenase with other extradiol-type dioxygenases has led to identify evolutionally conserved amino acid residues whose possible catalytic roles are proposed. |
| doi_str_mv | 10.1006/bbrc.1996.1108 |
| format | Article |
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Kernforschungszentrum Karlsruhe GmbH (Germany). Projekt Europaeisches Forschungszentrum fuer Massnahmen zur Luftreinhaltung (PEF) ; Chungbuk National University, Cheongju, Korea</creatorcontrib><description>A catechol 2,3-dioxygenase gene in chromosomal DNA of P. putida KF715 was cloned and its nucleotide sequence analyzed. The enzyme gene was composed of 924 base pairs with ATG initiation codon and TGA termination codon, which can encode a polypeptide of molecular weight 35 kDa containing 307 amino acids. A promoter-like sequence and a ribosome-binding sequence were identified upstream the enzyme gene. A deduced amino acid sequence of the catechol 2,3-dioxygenase exhibited 94% identity with that of corresponding enzyme in TOL plasmid and 25% identity with that of 2,3-dihydroxybiphenyl 1,2-dioxygenase from the same strain. Furthermore, sequence comparison of the catechol 2,3-dioxygenase with other extradiol-type dioxygenases has led to identify evolutionally conserved amino acid residues whose possible catalytic roles are proposed.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.1996.1108</identifier><identifier>PMID: 8713131</identifier><language>eng</language><publisher>United States</publisher><subject>adn ; Amino Acid Sequence ; bacteria ; Base Sequence ; Catechol 2,3-Dioxygenase ; chemical composition ; chromosome ; chromosomes ; Chromosomes, Bacterial ; clone ; clones ; composicion quimica ; composition chimique ; cromosomas ; Dioxygenases ; dna ; DNA, Bacterial ; flora del suelo ; flore du sol ; gene ; genes ; Molecular Sequence Data ; nucleotide sequence ; oxidoreductases ; oxidorreductasas ; oxydoreductase ; Oxygenases - genetics ; Pseudomonas putida ; Pseudomonas putida - enzymology ; Pseudomonas putida - genetics ; secuencia nucleotidica ; Sequence Homology, Amino Acid ; sequence nucleotidique ; soil flora</subject><ispartof>Biochemical and biophysical research communications, 1996-07, Vol.224 (3), p.831-836</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8713131$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, J</creatorcontrib><creatorcontrib>Oh, J</creatorcontrib><creatorcontrib>Min, K R</creatorcontrib><creatorcontrib>Kim, C K</creatorcontrib><creatorcontrib>Min, K H</creatorcontrib><creatorcontrib>Lee, K S</creatorcontrib><creatorcontrib>Kim, Y C</creatorcontrib><creatorcontrib>Lim, J Y</creatorcontrib><creatorcontrib>Kim, Y</creatorcontrib><creatorcontrib>Fraunhofer Institut fuer Atmosphaerische Umweltforschung, Garmisch Partenkirchen (Germany). Kernforschungszentrum Karlsruhe GmbH (Germany). Projekt Europaeisches Forschungszentrum fuer Massnahmen zur Luftreinhaltung (PEF)</creatorcontrib><creatorcontrib>Chungbuk National University, Cheongju, Korea</creatorcontrib><title>Structure of catechol 2,3-dioxygenase gene encoded in chromosomal DNA of Pseudomonas putida KF715</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>A catechol 2,3-dioxygenase gene in chromosomal DNA of P. putida KF715 was cloned and its nucleotide sequence analyzed. The enzyme gene was composed of 924 base pairs with ATG initiation codon and TGA termination codon, which can encode a polypeptide of molecular weight 35 kDa containing 307 amino acids. A promoter-like sequence and a ribosome-binding sequence were identified upstream the enzyme gene. A deduced amino acid sequence of the catechol 2,3-dioxygenase exhibited 94% identity with that of corresponding enzyme in TOL plasmid and 25% identity with that of 2,3-dihydroxybiphenyl 1,2-dioxygenase from the same strain. Furthermore, sequence comparison of the catechol 2,3-dioxygenase with other extradiol-type dioxygenases has led to identify evolutionally conserved amino acid residues whose possible catalytic roles are proposed.</description><subject>adn</subject><subject>Amino Acid Sequence</subject><subject>bacteria</subject><subject>Base Sequence</subject><subject>Catechol 2,3-Dioxygenase</subject><subject>chemical composition</subject><subject>chromosome</subject><subject>chromosomes</subject><subject>Chromosomes, Bacterial</subject><subject>clone</subject><subject>clones</subject><subject>composicion quimica</subject><subject>composition chimique</subject><subject>cromosomas</subject><subject>Dioxygenases</subject><subject>dna</subject><subject>DNA, Bacterial</subject><subject>flora del suelo</subject><subject>flore du sol</subject><subject>gene</subject><subject>genes</subject><subject>Molecular Sequence Data</subject><subject>nucleotide sequence</subject><subject>oxidoreductases</subject><subject>oxidorreductasas</subject><subject>oxydoreductase</subject><subject>Oxygenases - genetics</subject><subject>Pseudomonas putida</subject><subject>Pseudomonas putida - enzymology</subject><subject>Pseudomonas putida - genetics</subject><subject>secuencia nucleotidica</subject><subject>Sequence Homology, Amino Acid</subject><subject>sequence nucleotidique</subject><subject>soil flora</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkb1PwzAQxS0EKqWwsoE8MZFyjhN_jFWhgKgAqVRiixzbaYOSutiJRP97jNod3fCke797wzuELgmMCQC7K0uvx0RKNiYExBEaEpCQpASyYzSESCSpJJ-n6CyELwBCMiYHaCA4oXGGSC063-uu9xa7CmvVWb12DU5vaWJq97Nb2Y0KFkex2G60M9bgeoP12rvWBdeqBt-_Tv5u34PtTVxGHm_7rjYKv8w4yc_RSaWaYC8OOkLL2cPH9CmZvz0-TyfzpEoZdAllRjJeakgFY5xSLqwUFkpOuWEgGU2jwaWseJYZnlOTgwCZmUhqIQDoCN3sc7feffc2dEVbB22bRm2s60PBBYkB2f8gyWVGRc4ieHUA-7K1ptj6ulV-VxzKi_713q-UK9TK16FYLuIrOECex9bpL9Tgdwk</recordid><startdate>19960725</startdate><enddate>19960725</enddate><creator>Lee, J</creator><creator>Oh, J</creator><creator>Min, K R</creator><creator>Kim, C K</creator><creator>Min, K H</creator><creator>Lee, K S</creator><creator>Kim, Y C</creator><creator>Lim, J Y</creator><creator>Kim, Y</creator><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19960725</creationdate><title>Structure of catechol 2,3-dioxygenase gene encoded in chromosomal DNA of Pseudomonas putida KF715</title><author>Lee, J ; Oh, J ; Min, K R ; Kim, C K ; Min, K H ; Lee, K S ; Kim, Y C ; Lim, J Y ; Kim, Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f260t-36d967bc0286673378e98e0b737d609632286799f744d753d508094d337c88003</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>adn</topic><topic>Amino Acid Sequence</topic><topic>bacteria</topic><topic>Base Sequence</topic><topic>Catechol 2,3-Dioxygenase</topic><topic>chemical composition</topic><topic>chromosome</topic><topic>chromosomes</topic><topic>Chromosomes, Bacterial</topic><topic>clone</topic><topic>clones</topic><topic>composicion quimica</topic><topic>composition chimique</topic><topic>cromosomas</topic><topic>Dioxygenases</topic><topic>dna</topic><topic>DNA, Bacterial</topic><topic>flora del suelo</topic><topic>flore du sol</topic><topic>gene</topic><topic>genes</topic><topic>Molecular Sequence Data</topic><topic>nucleotide sequence</topic><topic>oxidoreductases</topic><topic>oxidorreductasas</topic><topic>oxydoreductase</topic><topic>Oxygenases - genetics</topic><topic>Pseudomonas putida</topic><topic>Pseudomonas putida - enzymology</topic><topic>Pseudomonas putida - genetics</topic><topic>secuencia nucleotidica</topic><topic>Sequence Homology, Amino Acid</topic><topic>sequence nucleotidique</topic><topic>soil flora</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, J</creatorcontrib><creatorcontrib>Oh, J</creatorcontrib><creatorcontrib>Min, K R</creatorcontrib><creatorcontrib>Kim, C K</creatorcontrib><creatorcontrib>Min, K H</creatorcontrib><creatorcontrib>Lee, K S</creatorcontrib><creatorcontrib>Kim, Y C</creatorcontrib><creatorcontrib>Lim, J Y</creatorcontrib><creatorcontrib>Kim, Y</creatorcontrib><creatorcontrib>Fraunhofer Institut fuer Atmosphaerische Umweltforschung, Garmisch Partenkirchen (Germany). Kernforschungszentrum Karlsruhe GmbH (Germany). Projekt Europaeisches Forschungszentrum fuer Massnahmen zur Luftreinhaltung (PEF)</creatorcontrib><creatorcontrib>Chungbuk National University, Cheongju, Korea</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, J</au><au>Oh, J</au><au>Min, K R</au><au>Kim, C K</au><au>Min, K H</au><au>Lee, K S</au><au>Kim, Y C</au><au>Lim, J Y</au><au>Kim, Y</au><aucorp>Fraunhofer Institut fuer Atmosphaerische Umweltforschung, Garmisch Partenkirchen (Germany). Kernforschungszentrum Karlsruhe GmbH (Germany). Projekt Europaeisches Forschungszentrum fuer Massnahmen zur Luftreinhaltung (PEF)</aucorp><aucorp>Chungbuk National University, Cheongju, Korea</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure of catechol 2,3-dioxygenase gene encoded in chromosomal DNA of Pseudomonas putida KF715</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1996-07-25</date><risdate>1996</risdate><volume>224</volume><issue>3</issue><spage>831</spage><epage>836</epage><pages>831-836</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>A catechol 2,3-dioxygenase gene in chromosomal DNA of P. putida KF715 was cloned and its nucleotide sequence analyzed. The enzyme gene was composed of 924 base pairs with ATG initiation codon and TGA termination codon, which can encode a polypeptide of molecular weight 35 kDa containing 307 amino acids. A promoter-like sequence and a ribosome-binding sequence were identified upstream the enzyme gene. A deduced amino acid sequence of the catechol 2,3-dioxygenase exhibited 94% identity with that of corresponding enzyme in TOL plasmid and 25% identity with that of 2,3-dihydroxybiphenyl 1,2-dioxygenase from the same strain. Furthermore, sequence comparison of the catechol 2,3-dioxygenase with other extradiol-type dioxygenases has led to identify evolutionally conserved amino acid residues whose possible catalytic roles are proposed.</abstract><cop>United States</cop><pmid>8713131</pmid><doi>10.1006/bbrc.1996.1108</doi><tpages>6</tpages></addata></record> |
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| subjects | adn Amino Acid Sequence bacteria Base Sequence Catechol 2,3-Dioxygenase chemical composition chromosome chromosomes Chromosomes, Bacterial clone clones composicion quimica composition chimique cromosomas Dioxygenases dna DNA, Bacterial flora del suelo flore du sol gene genes Molecular Sequence Data nucleotide sequence oxidoreductases oxidorreductasas oxydoreductase Oxygenases - genetics Pseudomonas putida Pseudomonas putida - enzymology Pseudomonas putida - genetics secuencia nucleotidica Sequence Homology, Amino Acid sequence nucleotidique soil flora |
| title | Structure of catechol 2,3-dioxygenase gene encoded in chromosomal DNA of Pseudomonas putida KF715 |
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