Cloning and characterization of a chromosomal gene cluster, pah, that encodes the upper pathway for phenanthrene and naphthalene utilization by Pseudomonas putida OUS82

Kiyohara, Hohzoh; Torigoe, S; Kaida, N; Asaki, T; Iida, Toshiya; Hayashi, Hiroshi; Takizawa, Noboru

doi:10.1128/jb.176.8.2439-2443.1994

Cited by 131 publications

(82 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The resultants dihydrodiol is then sequentially attacked by dehydrogenase and meta-cleavage enzyme. These reaction are considered to yield 1-hydroxy 2-napthoic acid (Pinyakong et al, 2000;Kiyohara et al, 1994). These finding suggested that the same of the enzyme could convert chrysene via intial dioxygenation at 1,2 and 2,3-position to obtain isolated compound I. Fusarium sp.…”

Section: Evaluation Of Enzyme Activitymentioning

confidence: 89%

Simple Screening for Potential Chrysene Degrading Fungi

Hidayat¹,

Tachibana

2015

KLS

View full text Add to dashboard Cite

Chrysene is a class of organic compounds, arranged in four benzene rings, and a polycyclic aromatic hydrocarbon (PAH), It has been found to have a variety of toxicity, mutagenicity, teratogenicity, and carcinogenicity on microorganisms, plants and animals in environment. Nowadays, the most attention on degradation of PAHs is investigating degradation of high-molecular-weight molecules. However, microbes which have ability to degrade PAHs containing more than three benzene rings are more difficult to be obtained. In order to provide chrysene degrading fungi, this study was conducted for screening, and isolating the fungi from soil, and hence investigating the selected fungi having high chrysene degradation activity. From the 62 soil samples collected from Matsuyama-Japan, 92 isolates were found and 20 isolates of them grew well in Malt extract media contaminated with chrysene (covered up 90%). Among them, a fungus, Fusarium sp. has the highest activity to degrade chrysene compared to others screened fungi. This fungus was evaluated further on liquid medium from distilled water and sea water to confirm their validity in degrading chrysene. The result showed that Fusarium sp. F092 degraded 48% of chrysene, where the chrysene degradation showed no differences at salinity of 35 o / oo . The effect of variation of enzymes activities on incubation times was evaluated simultaneously. When the fungus was grown in a liquid culture, the highest activity of 1,2-dioxygenase reached 203.5 UL -1 were observed on 30 days incubation and 29.7 Ul -1 for 2,3-dioxygenase on 40 days incubation. The products of chrysene degradation by Fusarium sp. F092 are, 1-hydroxy 2-napthoic acid and catechol. In conclusion, Fusarium sp. F092 shows a high potential activity degrade PAHs contamination .

show abstract

Section: Evaluation Of Enzyme Activitymentioning

confidence: 89%

Simple Screening for Potential Chrysene Degrading Fungi

Hidayat¹,

Tachibana

2015

KLS

View full text Add to dashboard Cite

show abstract

“…High levels (Ϸ90%) of homology and a conserved gene arrangement are observed in the nah, ndo, pah, and dox sequences (63,64,147,333,355,601). In fact, it has been proposed that the dox plasmid, which encodes a dibenzothiophene (DBT) metabolic pathway analogous to the naphthalene catabolic pathway, may in fact be a naphthalene catabolic plasmid (163).…”

Section: Aerobic Pah Metabolismmentioning

confidence: 99%

Recent Advances in Petroleum Microbiology

Hamme¹,

Singh

Ward

2003

Microbiol Mol Biol Rev

1,193

640

View full text Add to dashboard Cite

Recent advances in molecular biology have extended our understanding of the metabolic processes related to microbial transformation of petroleum hydrocarbons. The physiological responses of microorganisms to the presence of hydrocarbons, including cell surface alterations and adaptive mechanisms for uptake and efflux of these substrates, have been characterized. New molecular techniques have enhanced our ability to investigate the dynamics of microbial communities in petroleum-impacted ecosystems. By establishing conditions which maximize rates and extents of microbial growth, hydrocarbon access, and transformation, highly accelerated and bioreactor-based petroleum waste degradation processes have been implemented. Biofilters capable of removing and biodegrading volatile petroleum contaminants in air streams with short substrate-microbe contact times (<60 s) are being used effectively. Microbes are being injected into partially spent petroleum reservoirs to enhance oil recovery. However, these microbial processes have not exhibited consistent and effective performance, primarily because of our inability to control conditions in the subsurface environment. Microbes may be exploited to break stable oilfield emulsions to produce pipeline quality oil. There is interest in replacing physical oil desulfurization processes with biodesulfurization methods through promotion of selective sulfur removal without degradation of associated carbon moieties. However, since microbes require an environment containing some water, a two-phase oil-water system must be established to optimize contact between the microbes and the hydrocarbon, and such an emulsion is not easily created with viscous crude oil. This challenge may be circumvented by application of the technology to more refined gasoline and diesel substrates, where aqueous-hydrocarbon emulsions are more easily generated. Molecular approaches are being used to broaden the substrate specificity and increase the rates and extents of desulfurization. Bacterial processes are being commercialized for removal of H2S and sulfoxides from petrochemical waste streams. Microbes also have potential for use in removal of nitrogen from crude oil leading to reduced nitric oxide emissions provided that technical problems similar to those experienced in biodesulfurization can be solved. Enzymes are being exploited to produce added-value products from petroleum substrates, and bacterial biosensors are being used to analyze petroleum-contaminated environments

show abstract

“…Salicylate and 1-hydroxy-2-naphthoate are further degraded by other catabolic enzymes. The enzymes in the upper pathway have broad substrate specificities, and various polycyclic aromatic hydrocarbons other than naphthalene and phenanthrene are oxidized by a high-density suspension of OUS82 cells (9).…”

mentioning

confidence: 99%

“…tac promoter expression vector pKK223-3 (1) was purchased from Pharmacia LKB Biotechnology, Uppsala, Sweden. The rich medium (LB) and the minimal medium used in this study were described previously (9). SMT medium was the minimal medium plus 0.3% disodium succinate and 30 ,g of tryptophan per ml.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Identification and characterization of genes encoding polycyclic aromatic hydrocarbon dioxygenase and polycyclic aromatic hydrocarbon dihydrodiol dehydrogenase in Pseudomonas putida OUS82

et al. 1994

Self Cite

View full text Add to dashboard Cite

Naphthalene and phenanthrene are transformed by enzymes encoded by the pah gene cluster ofPseudomonas putida OUS82. The pahA and pahB genes, which encode the first and second enzymes, dioxygenase and cis-dihydrodiol dehydrogenase, respectively, were identified and sequenced. The DNA sequences showed that pahA and pahB were clustered and that pah/A consisted of four cistrons, pah/Aa paMAb, pahAc, and pahAd, which encode ferredoxin reductase, ferredoxin, and two subunits of the iron-sulfur protein, respectively.Pseudomonas putida OUS82 can assimilate naphthalene and phenanthrene as its sole carbon sources. The strain converts naphthalene and phenanthrene to salicylate and 1-hydroxy-2-naphthoate, respectively, by a shared catabolic pathway (the upper pathway; Fig. 1). Salicylate and 1-hydroxy-2-naphthoate are further degraded by other catabolic enzymes. The enzymes in the upper pathway have broad substrate specificities, and various polycyclic aromatic hydrocarbons other than naphthalene and phenanthrene are oxidized by a high-density suspension of OUS82 cells (9).Previously, we cloned the gene cluster encoding the enzymes of the upper pathway and named it pah (polycyclic aromatic hydrocarbon; 9). The pah region strongly hybridized to a corresponding region of plasmid NAH7 of P. putida G7, which degrades naphthalene (4). All recombinant plasmids carrying pahA have 6.5-and 3.0-kb Sall fragments. The two fragments were seen to be necessary for the dioxygenase phenotype (PahA). A restriction endonuclease map of a region in the fragments resembles that of the nahA region of NAH7 and pDTG1 in P. putida G7 and NCIB 9816-4, which degrade naphthalene (2, 4, 23). The pahA gene was expected to be in that region.Here, we describe the identification and characterization of the pahA and pahB genes, which encode dioxygenase PahA, which is the first enzyme of the pathway and converts polycyclic aromatic hydrocarbon (PAH) to the corresponding cis-dihydrodiol, and dehydrogenase PahB, the second enzyme of the pathway, which converts the product of PahA to the corresponding diol. P. putida OUS8211 (trp-82 Apah-821), a derivative of strain OUS82 that is defective in naphthalene and phenanthrene utilization, and plasmid pDIl, which carries the pahAB gene cluster, were described previously (9). Plasmid NAH7 was described elsewhere (4, 5). Escherichia coli JM109 and plasmid pUC119 were described by Yanisch-Perron et al. (21)

show abstract

Cloning and characterization of a chromosomal gene cluster, pah, that encodes the upper pathway for phenanthrene and naphthalene utilization by Pseudomonas putida OUS82

Cited by 131 publications

References 30 publications

Simple Screening for Potential Chrysene Degrading Fungi

Simple Screening for Potential Chrysene Degrading Fungi

Recent Advances in Petroleum Microbiology

Identification and characterization of genes encoding polycyclic aromatic hydrocarbon dioxygenase and polycyclic aromatic hydrocarbon dihydrodiol dehydrogenase in Pseudomonas putida OUS82

Contact Info

Product

Resources

About