Cloning, Nucleotide Sequence, and Characterization of the Genes Encoding Enzymes Involved in the Degradation of Cumene to 2-Hydroxy-6-Oxo-7-Methylocta-2,4-Dienoic Acid in Pseudomonas fluorescens IP01
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概要
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A gene cluster encoding cumene (isopropylbenzene-degrading enzymes was cloned in Escherichia coli JM109 from newly isolated Pseudomonas fluorescens strain IP01. E. coli cells containing pIP103 (10.8-kb insert) converted cumene, orther monocyclic aromatic hydrocarbons and biphenyl into the meta-cleaved compounds, whereas the cells containing pIP107D (4.8-kb insert) formed the cis-dihydrodiol compounds, and the cells containing pIP107 (5.2-kb insert) formed the catechol derivatives. We proved that this oxidation system degrades cumene using three enzymes, aromatic-ring dioxygenase, dihydrodiol dehydrogenase, and extradiol dioxygenase. Moreover we determined the nucleotide sequence of a 6,508-bp region encoding aromatic-ring dioxygenase, dihydrodiol dehydrogenase, and extradiol dioxygenase, which subsequently led to identification of six out of seven open reading frames (ORFs) from P. fluorescens IP01. The nucleotide and deduced amino acid sequences for ORF1,2,4 and 5,designated cumA1A2A3A4,were found to be similar to those for known multicomponent dioxygenase systems : todC1C2BA from Pseudomonas putida F1 (51-65% amino acid sequence identity) and bphA1A2A3A4 from Pseudomonas pseudoalcaligenes KF707 (59-78%). Two Cys-His pairs in the large subunit of iron-sulfur proteins were conserved in CumA1,and a similar Cys-His pair, conserved in the ferredoxin component of other dioxygenase systems, was found in CumA3. ORF6,designated cumB, was homologous to the dihydrodiol dehydrogenase gene of the tod (58%) and bph (73%) systems, while ORF7,designated cumC, was homologous to todE (47%) and bphC (57%) which encode the meta-cleavage enzymes. Analysis of strain IP01's nucleotide sequence revealed an overall G+C content of 53% for the cum gene cluster, less than the general G+C content of the chromosome of P. fluorescens.
- 社団法人日本生物工学会の論文
- 1996-03-25
著者
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KODAMA Tohru
Department of Textile Science and Technology, Shinshu University
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YAMANE Hisakazu
Biotechnology Research Center, The University of Tokyo
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OMORI TOSHIO
Biotechnology Research Center, The University of Tokyo
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Omori T
Coll. Of Systems Engineering And Sci. Dep. Of Bioscience And Engineering Shibaura Inst. Of Technol.
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HABE HIROSHI
Biotechnology Research Center, The University of Tokyo
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KIMURA TOSHIAKI
Biotechnology Research Center, The University of Tokyo
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AOKI HIROBUMI
Biochemistry Department, Central Research Laboratory, Showa Denko Co. Ltd.,
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Omori Toshio
Biotechnoiogy Researchcenter The University Of Tokyo
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Yamane Hisakazu
Biotechnology Res. Center The Univ. Of Tokyo
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Yamane Hisakazu
Biotechnology Res. Center Univ. Of Tokyo
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Yamane Hisakazu
Biotech. Res. Ctr. The Univ. Of Tokyo
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Habe Hiroshi
Biotechnology Research Center University Of Tokyo
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Kodama T
Department Of Biotechnology The University Of Tokyo:(present Address)faculty Of Textile Science And
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Kodama Tohru
Department Of Agricultural Chemistry The University Of Tokyo
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Kokubo Tetsuro
Department Of Biotechnology The University Of Tokyo:(present Address)division Of Gene Function In An
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Kimura Toshiaki
Biotechnology Development Department Of Production Shionogi & Co. Ltd.
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Habe H
Research Institute For Innovations In Sustainable Chemistry National Institute Of Advanced Industria
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Kodama Tohru
Department Of Agricultural Chemistry Faculty Of Agriculture The University Of Tokyo
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Aoki H
Biochemistry Department Central Research Laboratory Showa Denko Co. Ltd.
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Yada H
Biotechnology Research Center University Of Tokyo
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YAMANE Hisakazu
Biotech. Res. Ctr. , The Univ. of Tokyo
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