Diverse reactions catalyzed by naphthalene dioxygenase fromPseudomonas sp strain NCIB 9816

Resnick, Sol M.; Lee, K; Gibson, D T

doi:10.1007/bf01574775

Cited by 284 publications

(175 citation statements)

References 84 publications

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“…However, there were very significant positive correlations between the abundances of both nah and pdo1 genes and total PAH content. Naphthalene dioxygenase (NDO) encoded by the nah gene has a relaxed substrate specificity and catalyzes the dioxygenation of many related two-and three-ring PAHs such as naphthalene, phenanthrene, anthracene, acenaphthylene, fluorene, and so on to their respective cis-dihydrodiols (Resnick et al 1996). The pdo1 gene sequences detected showed high levels of similarity with pdo1 genes identified from Mycobacterium which is involved in degradation of two-, three-, and four-ring PAHs including naphthalene, phena n t h r e n e , f l u o r a n t h e n e , p y r e n e , c h r y s e n e , a n d benz(a)anthracene as well as even five-ring PAHs e.g., benz(a)pyrene with the presence of pyrene as co-metabolite (Schneider et al 1996;Johnsen et al 2006;Zhang et al 2006).…”

Section: N4(6)mentioning

confidence: 99%

Response of bacterial pdo1, nah, and C12O genes to aged soil PAH pollution in a coke factory area

Han

Liu

Zheng

et al. 2014

Environ Sci Pollut Res

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Soil pollution caused by polycyclic aromatic hydrocarbons (PAHs) is threatening human health and environmental safety. Investigating the relative prevalence of different PAH-degrading genes in PAH-polluted soils and searching for potential bioindicators reflecting the impact of PAH pollution on microbial communities are useful for microbial monitoring, risk evaluation, and potential bioremediation of soils polluted by PAHs. In this study, three functional genes, pdo1, nah, and C12O, which might be involved in the degradation of PAHs from a coke factory, were investigated by realtime quantitative PCR (qPCR) and clone library approaches. The results showed that the pdo1 and C12O genes were more abundant than the nah gene in the soils. There was a significantly positive relationship between the nah or pdo1 gene abundances and PAH content, while there was no correlation between C12O gene abundance and PAH content. Analyses of clone libraries showed that all the pdo1 sequences were grouped into Mycobacterium, while all the nah sequences were classified into three groups: Pseudomonas, Comamonas, and Polaromonas. These results indicated that the abundances of nah and pdo1 genes were positively influenced by levels of PAHs in soil and could be potential microbial indicators reflecting the impact of soil PAH pollution and that Mycobacteria were one of the most prevalent PAHs degraders in these PAH-polluted soils. Principal component analysis (PCA) and correlation analyses between microbial parameters and environmental factors revealed that total carbon (TC), total nitrogen (TN), and dissolved organic carbon (DOC) had positive effects on the abundances of all PAH-degrading genes. It suggests that increasing TC, TN, and DOC inputs could be a useful way to remediate PAH-polluted soils.

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Section: N4(6)mentioning

confidence: 99%

Response of bacterial pdo1, nah, and C12O genes to aged soil PAH pollution in a coke factory area

Han

Liu

Zheng

et al. 2014

Environ Sci Pollut Res

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“…Bacterial ARHDOs are quite versatile, both in terms of the substrates they accept and the oxidations they catalyse. Thus, even small aliphatic compounds such as trichloroethylene may serve as substrates (Wackett & Gibson, 1988;Furukawa et al, 1994) and different types of oxidations including dehydrogenation of vicinal carbons and mono-oxygenation of carbons and hetero atoms have been observed (Resnick et al, 1996;Boyd & Sheldrake, 1998). The subunit characteristics and compositions of such dioxygenase systems vary considerably.…”

Section: Introductionmentioning

confidence: 99%

A genetic system for the rapid isolation of aromatic-ring-hydroxylating dioxygenase activities

Kahl

Höfer

2003

Microbiology

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Aromatic-ring-hydroxylating dioxygenases (ARHDOs) are key enzymes in the aerobic bacterial metabolism of aromatic compounds. They are of biotechnological importance as they function as biocatalysts in the stereospecific synthesis of chiral synthons and the degradation of aromatic pollutants. This report describes the development and validation of a system for the rapid isolation and characterization of specific ARHDO activities. The system is based on the identification of ARHDO gene segments that encode the enzymes' major functional determinants, on consensus primers for the direct amplification of such partial genes and on a 'recipient' ARHDO gene cluster for the insertion of the amplified segments. Previously, it has been shown that neither the N-nor the C-terminal portions but only the core region of the large or a-subunit of a class II ARHDO significantly influence substrate and product spectra. On the basis of these observations, consensus primers were designed for the amplification of the gene segment encoding the catalytic core of the large subunit. These primers were tested on 11 bacterial isolates known to metabolize aromatic compounds. In 10 cases, a gene fragment of expected length was amplified. DNA sequencing confirmed similarity to ARHDO a-subunit gene cores. The heterologously well-expressible bphA gene cluster of Burkholderia sp. strain LB400 was modified to facilitate the in-frame insertion of amplified segments. It was used successfully to express the resulting hybrid gene clusters and to form catalytically active chimaeric ARHDOs. The metabolic properties of these enzymes differed significantly from each other and from the parental ARHDO of strain LB400. These results indicate that the system described here can be used to rapidly isolate and functionally characterize ARHDO activities, starting from isolated strains, mixtures of organisms or samples of nucleic acids. Applications of the system range from the recruitment of novel ARHDO activities to an improved characterization of natural ARHDO diversity.

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“…By these means it converts different isomers of dimethylbenzene into dimethyl phenols and isomers of nitrotoluene into nitobenzyl alcohols and nitophenols [31,34]. Allylic methyl group monooxygenation can be seen with different halo-propene and halo-butene isomers which are converted into butene-1-ol and propene-1-ol, respectively [35]. 2,3-Dichloro-1-propene is a substrate for monooxygenation with allylic rearrangement and gets converted into 2,3-dichloro-2-propene-1-ol [35].…”

Section: Dioxygenases: Tod (Ec 11412)mentioning

confidence: 99%

“…Allylic methyl group monooxygenation can be seen with different halo-propene and halo-butene isomers which are converted into butene-1-ol and propene-1-ol, respectively [35]. 2,3-Dichloro-1-propene is a substrate for monooxygenation with allylic rearrangement and gets converted into 2,3-dichloro-2-propene-1-ol [35].…”

Section: Dioxygenases: Tod (Ec 11412)mentioning

confidence: 99%

The enzymatic basis for pesticide bioremediation

et al. 2008

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Diverse reactions catalyzed by naphthalene dioxygenase fromPseudomonas sp strain NCIB 9816

Cited by 284 publications

References 84 publications

Response of bacterial pdo1, nah, and C12O genes to aged soil PAH pollution in a coke factory area

Response of bacterial pdo1, nah, and C12O genes to aged soil PAH pollution in a coke factory area

A genetic system for the rapid isolation of aromatic-ring-hydroxylating dioxygenase activities

The enzymatic basis for pesticide bioremediation

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