Cloning and Expression of the Gene Encoding the Thermophilic NAD(P)H-FMN Oxidoreductase Coupling with the Desulfurization Enzymes from Paenibacillus sp.A11-2

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概要

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• The gene encoding the NAD(P)H-flavin oxidoreductase(flavin reductase) which couples with the thermophilic dibenzothiophene(DBT)-desulfurizing monooxygenases of Paenibacillus sp.A11-2 was cloned in Escherichia coli and designated tdsD. Nucleotide sequence analysis suggested that the gene product consisted of 200 amino acids and showed about 30%, 27% and 26% amino acid sequence similarity to the major flavin reductase of Vibrio fisheri, the NADH dehydrogenase of Thermus thermophilus and several oxygen-insensitive NAD(P)H nitroreductases in the Enterobacteriaceae family, respectively. Both the growing and resting recombinant E.coli, in which tdsD was coexpressed with a set of desulfurizing genes, showed a rate of DBT removal about 5 times higher than the recombinants lacking tdsD. Maximal desulfurization was observed close to 45℃ and 55℃ in the resting cells and in cell-free extraction reaction with the tdsD-coexpressing recombinants, respectively. In an organic/aqueous biphasic system, the coexpression of tdsD also markedly enhanced the rate of DBT removal.

• 社団法人日本生物工学会の論文
• 2000-12-25

著者

• ISHII YOSHITAKA

  Bio-Refining Process Laboratory, Japan Cooperation Center, Petroleum

• MARUHASHI KENJI

  Bio-Refining Process Laboratory, Japan Cooperation Center, Petroleum

• SUZUKI MASANORI

  Bio-Refining Process Laboratory, Advanced Technology and Research Institute, Petroleum Energy Center

• Konishi Jin

  Bio-refining Process Laboratory Advanced Technology And Research Institute Petroleum Energy Center

• Maruhashi Kenji

  Bio-refining Process Laboratory Technical Cooperation Department Japan Cooperation Center

• Suzuki M

  Bio-refining Process Laboratory Advanced Technology And Research Institute Petroleum Energy Center

• Suzuki Masanori

  Bio-refining Process Laboratory Advanced Technology And Research Institute Petroleum Energy Center

• Ishii Yoshitaka

  Bio-refining Process Laboratory Advanced Technology And Research Institute Petroleum Energy Center

関連論文

• Characterization of a flavin reductase from a thermophilic dibenzothiophene-desulfurizing bacterium, Bacillus subtilis WU-S2B(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
• Dibenzothiophene Desulfurizing Enzymes from Moderately Thermophilic Bacterium Bacillus subtilis WU-S2B : Purification, Characterization and Overexpression(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
• Gene Cloning and Characterization of Mycobacterium phlei Flavin Reductase Involved in Dibenzothiophene Desulfurization(Enzymology, Protein Engineering, and Enzyme Technology)
• Thermostable Flavin Reductase That Couples with Dibenzothiophene Monooxygenase, from Thermophilic Bacillus sp. DSM411 : Purification, Characterization, and Gene Cloning
• Enhancement and Stabilization of Desulfurization Activity of Rhodococcus erythropolis KA2-5-1 by Feeding Ethanol and Sulfur Components(BIOCHEMICAL ENGINEERING)
• Cloning and Expression of Aspergillus niger icdA Gene Encoding Mitochondrial NADP^+-Specific Isocitrate Dehydrogenase
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• Identification of the Gene Encoding a NAD(P)H-Flavin Oxidoreductase Coupling with Dibenzothiophene (DBT)-Desulfurizing Enzymes from the DBT-Nondesulfurizing Bacterium Paenibacillus polymyxa A-1
• Determination of Nucleotide Sequence Related to the Plasmid Replication Region in Enterococcus faecalis and Its Application to a New Shuttle Vector
• Analysis of Dibenzothiophene Metabolic Pathway in Mycobacterium Strain G3
• Analyses of Substrate Specificity of the Desulfurizing Bacterium Mycobacterium sp. G3
• Kinetic Analysis of Microbial Desulfurization of Model and Light Gas Oils Containing Multiple Alkyl Dibenzothiophenes
• Improvement of Desulfurization Activity in Rhodococcus erythropolis KA2-5-1 by Genetic Engineering
• Application of solid-phase extraction to the analysis of the isomers generated in biodesulfurization against methylated dibenzothiophenes
• Alkylated Benzothiophene Desulfurization by Rhodococcus sp. Strain T09
• Isolation of the Pseudomonas aeruginosa Gene Affecting Uptake of Dibenzothiophene in n-Tetradecane
• Isolation of a Recombinant Desulfurizing 4,6-Dipropyl Dibenzothiophene in n-Tetradecane
• Purification and Characterization of Dibenzothiophene Sulfone Monooxygenase and FMN-Dependent NADH Oxidoreductase from the Thermophilic Bacterium Paenibacillus sp.Strain A11-2
• Cloning and Expression of the Gene Encoding the Thermophilic NAD(P)H-FMN Oxidoreductase Coupling with the Desulfurization Enzymes from Paenibacillus sp.A11-2
• Selective Cleavage of the Two C-S Bonds in Asymmetrically Alkylated Dibenzothiophenes by Rhodococcus erythropolis KA2-5-1
• Novel Reactivity of Dibenzothiophene Monooxygenase from Bacillus subtilis WU-S2B
• Desulfurization Characteristics of Thermophilic Paenibacillus sp.Strain A11-2 against Asymmetrically Alkylated Dibenzothiophenes
• A Highly Active Producer of Coproporphyrin III and Uroporphyrin III
• Identification of Porphyrins Produced from Isopropanol by Arthrobacter hyalinus

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