- 1) Sato, S., Nam, J.-W., Kasuga, K., Nojiri, H., Yamane, H., and Omori, T., Identification and characterization of genes encoding carbazole 1,9a-dioxygenase in Pseudomonas sp. strain CA10. J. Bacteriol., 179, 4850-4858 (1997).
- 2) Nojiri, H., Nam, J.-W., Kosaka, M., Morii, K., Takemura, T., Furihata, K., Yamane, H., and Omori, T., Diverse oxygenations catalyzed by carbazole 1,9a-dioxygenase from Pseudomonas sp. strain CA10. J. Bacteriol., 181, 3105-3113 (1999).
- 3) Batie, C.J., Ballou, D.P., and Correll, C.C., Phthalate dioxygenase reductase and related flavin-iron-sulfur containing electron transferases. Chemistry and Biochemistry of Flavoenzymes, 3, 543-556 (1991).
- 4) Mason, J.R. and Cammack, R., The electron-transport proteins of hydroxylating bacterial dioxygenases. Annu. Rev. Microbiol., 46, 277-305 (1992).
- 5) Batie, C.J., LaHaie, E., and Ballou, D.P., Purification and characterization of phthalate oxygenase and phthalate oxygenase reductase from Pseudomonas cepacia. J. Biol. Chem., 262, 1510-1518 (1987).
- 6) Dehmel, U., Engesser, K.H., Timmis, K.N., and Dwyer, D.F., Cloning, nucleotide sequence, and expression of the gene encoding a novel dioxygenase involved in metabolism of carboxydiphenyl ethers in Pseudomonas pseudoalcaligenes POB310. Arch. Microbiol., 163, 35-41 (1995).
- 7) Nakatsu, C.D., Straus, N.A., and Wyndham, R.C., The nucleotide sequence of the Tn5271 3-chlorobenzoate 3,4-dioxygenase genes (cbaAB) unites the class IA oxygenases in a single lineage. Microbiology, 141, 485-495 (1995).
- 8) Neidle, E.L., Harnett, C., Ornston, L.N., Bairoch, A., Rekik, M., and Harayama, S., Nucleotide sequences of the Acinetobacter calcoaceticus benABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among multicomponent oxygenases. J. Bacteriol., 173, 5385-5395 (1991).
- 9) Harayama, S., Rekik, M., and Timmis, K.N., Genetic analysis of a relaxed substrate specificity aromatic ring dioxygenase, toluate 1,2-dioxygenase, encoded by TOL plasmid pWW0 of Pseudomonas putida. Mol. Gen. Genet., 202, 226-234 (1986).
- 10) Bundy, B.M., Campbell, A.L., and Neidle, E.L., Similarities between the antABC-encoded anthranilate dioxygenase and the benABC-encoded benzoate dioxygenase of Acinetobacter sp. strain ADP1. J. Bacteriol., 180, 4466-4476 (1998).
- 11) Rosche, B., Tshisuaka, B., Fetzner, S., and Lingens, F., 2-Oxo-1,2-dihydroquinoline 8-monooxygenase, a two-component enzyme system from Pseudonomas putida 86. J. Biol. Chem., 270, 17836-17842 (1995).
- 12) Bünz, P.V. and Cook, A.M., Dibenzofuran 4,4a-dioxygenase from Sphingomonas sp. strain RW1-Angular dioxygenation by a three component enzyme system. J. Bacteriol., 175, 6467-6475 (1993).
- 13) Sauber, K., Frohner, C., Rosenberg, G., Eberspacher, J., and Lingens, F., Purification and properties of pyrazon dioxygenase from pyrazon-degrading bacteria. Eur. J. Biochem., 74, 89-97 (1977).
- 14) Shepherd, J.M. and Lloyd-Jones, G., Novel carbazole degradation genes of Sphingomonas CB3: sequence analysis, transcription, and molecular ecology. Biochem. Biophys. Res. Commun., 247, 129-135 (1998).
- 15) Subramanian, V., Liu, T.-N., Yeh, W.K., and Gibson, D.T., Toluene dioxygenase: purification of an iron-sulphur protein by affinity chromatography. Biochem. Biophys. Res. Commun., 91, 1131-39 (1979).
- 16) Irie, S., Doi, S., Yorifuji, T., Takagi, M., and Yano, K., Nucleotide sequencing and characterization of the genes encoding benzene oxidation enzymes of Pseudomonas putida. J. Bacteriol., 169, 5174-5179 (1987).
- 17) Erickson, B.D. and Mondello, F.J., Nucleotide sequencing and transcriptional mapping of the genes encoding biphenyl dioxygenase, a multicomponent polychlorinated biphenyl-degrading enzyme in Pseudomonas strain LB400.J. Bacteriol., 174, 2903-2912 (1992).
- 18) Fukuda, M., Yasukochi, Y., Kikuchi, Y., Nagata, Y., Kimbara, K., Horiuchi, H., Takagi, M., and Yano, K., Identification of the bphA and bphB genes of Pseudomonas sp. strain KKS102 involved in degradation of biphenyl and polychlorinated biphenyls. Biochem, Biophys. Res. Commun., 202, 850-856 (1994).
- 19) Werlen, C., Kohler, H.-P.E., and van der Meer, J.R., The broad substrate chlorobenzene dioxygenase and cis-chlorobenzene dihydrodiol dehydrogenase of Pseudonomas sp. strain P51 are linked evolutionarily to the enzymes for benzene and toluene degradation. J. Biol. Chem., 271, 4009-4016 (1996).
- 20) Ensley, B.D. and Haigler, B.E., Naphthalene dioxygenase from Pseudomonas NCIB 9816. Methods Enzymol., 188, 46-52 (1990).
- 21) Simon, M.J., Osslund, T.D., Saunders, R., Ensley, B.D., Suggs, S., Harcourt, A., Suen, W.C., Cruden, D.L., Gibson, D.T., and Zylstra, G.J., Sequences of genes encoding naphthalene dioxygenase in Pseudomonas putida strains G7 and NCIB 9816-4. Gene, 127, 31-37 (1993).
- 22) Denome, S.A., Stanley, D.C., Olson, E.S., and Young, K.D., Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains: complete DNA sequence of an upper naphthalene catabolic pathway. J. Bacteriol., 175, 6890-6901 (1993).
- 23) Laurie, A.D. and Lloyd-Jones, G., The phn genes of Burkholderia sp. strain RP007 constitute a divergent gene cluster for polycyclic aromatic hydrocarbon catabolism. J. Bacteriol., 181, 531-540 (1999).
- 24) Takizawa, N., Kaida, N., Torigoe, S., Moritani, T., Sawada, T., Satoh, S., and Kiyohara, H., Identification and characterization of genes encoding polycyclic aromatic hydrocarbon dioxygenase and polycyclic aromatic hydrocarbon dihydrodiol dehydrogenase in Pseudomonas putida OUS82. J. Bacterial., 176, 2444-2449 (1994).
- 25) Parales, J.V., Kumar, A., Parales, R.E., and Gibson, D.T., Cloning and sequencing of the genesencoding 2-nitrotoluene dioxygenase from Pseudomonas sp. JS42. Gene, 181, 57-61 (1996).
- 26) Rosche, B., Tshisuaka, B., Hauer, B., Lingens, F., and Fetzner, S., 2-Oxo-1,2-dihydroquinoline 8-monooxygenase: phylogenetic relationship to other multicomponent nonheme iron oxygenases. J. Bacteriol., 179, 3549-3554 (1997).
- 27) Thompson, J.D., Higgins, D.G., and Gibson, T.J., CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acid Res., 22, 4673-4680 (1994).
- 28) Carredano, E., Karlsson, A., Kauppi, B., Choudhury D., Parales, R.E., Parales, J.V., Lee, K., Gibson, D.T., Eklund, H., and Ramaswamy, S., Substrate binding site of naphthalene 1,2-dioxygenase: Functional implications of indole binding. J. Mol. Biol., 296, 701-712 (2000).
- 29) Parales, J.V., Parales, R.E., Resnick, S.M., and Gibson, D.T., Enzyme specificity of 2-nitrotoluene 2,3-dioxygenase from Pseudomonas sp. strain JS42 is determined by the C-terminal region of the α subunit of the oxygenase component. J. Bacteriol., 180, 1194-1199 (1998).
- 30) Parales, R.E., Emig, M.D., Lynch, N.A., and Gibson, D.T., Substrate specificities of hybrid naphthalene and 2,4-dinitrotoluene dioxygenase enzyme systems. J. Bacteriol., 180, 2337-2344 (1998).
- 31) Chebrou, H., Hurtubise, Y., Barriault, D., and Sylvestre, M., Heterologous expression and characterization of the purified oxygenase component of Rhodococcus globerulus P6 biphenyl dioxygenase and of chimeras derived from it. J. Bacteriol., 181, 4805-4811 (1999).
- 32) Hirose, J., Suyama, A., Hayashida, S., and Furukawa, K., Construction of hybrid biphenyl (bph) and toluene (tod) genes for functional analysis of aromatic ring dioxygenases. Gene, 138, 27-33 (1994).
- 33) Hurtubise, Y., Barriault, D., and Sylvestre, M., Involvement of the terminal oxygenase β subunit in the biphenyl dioxygenase reactivity pattern toward chlorobiphenyls. J. Bacteriol., 180, 5828-5835 (1998).
- 34) Kauppi, B., Lee, K., Carredano, E., Parales, R.E., Gibson, D.T., Eklund, H., and Ramaswamy, S., Structure of an aromatic ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase. Structure, 6, 571-586 (1998).
- 35) Fukumori, F. and Saint, C.P., Nucleotide sequences and regulational analysis of genes involved in conversion of aniline to catechol in Pseudomonas putida UCC22 (pTDN1). J. Bacteroil., 179, 399-405 (1997).
- 36) Takeo, M., Fujii, T., and Maeda, Y., Sequence analysis of the genes encoding a multicomponent dioxygenase involved in oxidation of aniline and o-toluidine in Acinetobacter sp. strain YAA. J. Ferment. Bioeng., 85, 17-24 (1998).
- 37) Martin, V.J.J. and Mohn, W.W., A novel aromatic-ring-hydroxylating dioxygenase from the diterpenoid degrading bacterium Pseudomonas abietaniphila BKME-9. J. Bacteriol., 181, 2675-2682 (1999).
- 38) Subramanian, V., Liu, T.-N., Yeh, W.K., Sendar, C.M., Wackett, L.P., and Gibson, D.T., Purification and properties of ferredoxinTOL. A component of toluene dioxygenase from Pseudomonas putida F1. J. Biol. Chem., 260, 2355-2363 (1985).
- 39) Chang,H.K. and Zylstra, G.J., Novel organization of the genes for phthalate degradation from Burkholderia cepacia DBO1. J. Bacteriol., 180, 6529-6537 (1998).
- 40) Armengaud, J., Happe, B., and Timmis, K. N., Genetic analysis of dioxin dioxygenase of Sphingomonas sp. strain RW1: Catabolic genes dispersed on the genome. J. Bacteriol., 180, 3954-3966 (1998).
Full access
New Classification System for Oxygenase Components Involved in Ring-Hydroxylating Oxygenations
Reprints and Corporate Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
To request a reprint or corporate permissions for this article, please click on the relevant link below:
Academic Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
Obtain permissions instantly via Rightslink by clicking on the button below:
If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.
Related research
People also read lists articles that other readers of this article have read.
Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.
Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.