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References
Ishigooka, H.; Yoshida, Y.; Omori, T.; Minoda, Y.: Enzymatic dioxygenation of biphenyl-2,3-diol and 3-isopropylcatechol. Agric. Biol. Chem., 50, 1045–1046 (1986)
Furukawa, K.; Arimura, N.; Miyazaki, T.: Nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase gene of Pseudomonas pseudoalcaligenes. J. Bacteriol., 169, 427–429 (1987)
Khan, A.; Tewari, R.; Walia, S.: Molecular cloning of 3-phenylcatechol dioxygenase involved in the catabolic pathway of chlorinated biphenyl from Pseudomonas putida and its expression in Escherichia coil. Appl. Environ. Microbiol., 54, 2664–2671 (1988)
Ahmad, D.; Masse, R.; Sylvestre, M.: Cloning and expression of genes involved in 4-chlorobiphenyl transformation by Pseudomonas testosteroni: homology to polychlorobiphenyl-degrading genes in other bacteria. Gene, 86, 53–61 (1990)
Hayase, N.; Taira, K.; Furukawa, K.: Pseudomonas putida KF715 bphABCD operon encoding biphenyl and polychlorinated biphenyl degradation: cloning, analysis, and expression in soil bacteria. J. Bacteriol., 172, 1160–1164 (1990)
Eltis, L.D.; Hofmann, B.; Hecht, H.J.; Luensdorf, H.; Timmis, K.N.: Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase. J. Biol. Chem., 268, 2727–2732 (1993)
Asturias, J.A.; Eltis, L.D.; Prucha, M.; Timmis, K.N.: Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rhodococcus globerulus P6. Identification of a new family of extradiol dioxygenases. J. Biol. Chem., 269, 7807–7815 (1994)
Lee, J.; Sung, T.K.; Moon, J.; Min, K.R.; Kim, C.K.; Kim, Y.: Comparison of enzymic and immunochemical properties of 2,3-dihydroxybiphenyl-1,2-dioxygenases from four Pseudomonas strains. FEMS Microbiol. Lett., 120, 355–362 (1994)
Kim, E.; Zylstra, G.I.: Molecular and biochemical characterization of two meta-cleavage dioxygenases involved in biphenyl and m-xylene degradation by Beijerinckia sp. strain B1. J. Bacteriol., 177, 3095–3103 (1995)
Lloyd-Jones, G.; Ogden, R.C.; Williams, P.A.: Inactivation of 2,3-dihydroxybiphenyl 1,2-dioxygenase from Pseudomonas sp. strain CB406 by 3,4-dihydroxybiphenyl (4-phenylcatechol). Biodegradation, 6, 11–17 (1995)
Hauschild, J.E.; Masai, E.; Sugiyama, K.; Hatta, T.; Kimbara, K.; Fukuda, M.; Yano, K.: Identification of an alternative 2,3-dihydroxybiphenyl 1,2-dioxygenase in Rhodococcus sp. strain RHA1 and cloning of the gene. Appl. Environ. Microbiol., 62, 2940–2946 (1996)
Khan, A.A.; Wang, R.F.; Nawaz, M.S.; Cao, W.W.; Cerniglia, C.E.: Purification of 2,3-dihydroxybiphenyl 1,2-dioxygenase from Pseudomonas putida OU83 and characterization of the gene (bphC). Appl. Environ. Microbiol., 62, 1825–1830 (1996)
Khan, A.A.; Nawaz, M.S.; Cerniglia, C.E.: Rapid purification of an active recombinant His-tagged 2,3-dihydroxybiphenyl 1,2-dioxygenase from Pseudomonas putida OU83. FEMS Microbiol. Lett., 152, 23–29 (1997)
Vaillancourt, F.H.; Han, S.; Fortin, P.D.; Bolin, J.T.; Eltis, L.D.: Molecular basis for the stabilization and inhibition of 2,3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol. J. Biol. Chem., 273, 34887–34895 (1998)
Kim, S.J.; Shin, H.J.; Park, Y.C.; Kim, Y.; Min, K.H.; Kim, Y.C.: The 2,3-dihydroxybiphenyl 1,2-dioxygenase gene (phnQ) of Pseudomonas sp. DJ77: nucleotide sequence, enzyme assay, and comparison with isofunctional dioxygenases. J. Biochem. Mol. Biol., 32, 399–404 (1999)
Riegert, U.; Heiss, G.; Kuhm, A.E.; Mueller, C.; Contzen, M.; Knackmuss, H.J.; Stolz, A.: Catalytic properties of the 3-chlorocatechol-oxidizing 2,3-dihydroxybiphenyl 1,2-dioxygenase from Sphingomonas sp. strain BN6. J. Bacteriol., 181, 4812–4817 (1999)
Imbeault, N.Y.; Powlowski, J.B.; Colbert, C.L.; Bolin, J.T.; Eltis, L.D.: Steadystate kinetic characterization and crystallization of a polychlorinated biphenyl-transforming dioxygenase. J. Biol. Chem., 275, 12430–12437 (2000)
Seeger, M.; Camara, B.; Hofer, B.: Dehalogenation, denitration, dehydroxylation, and angular attack on substituted biphenyls and related compounds by a biphenyl dioxygenase. J. Bacteriol., 183, 3548–3555 (2001)
Vaillancourt, F.H.; Labbe, G.; Drouin, N.M.; Fortin, P.D.; Eltis, L.D.: The mechanism-based inactivation of 2,3-dihydroxybiphenyl 1,2-dioxygenase by catecholic substrates. J. Biol. Chem., 277, 2019–2027 (2002)
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(2006). Biphenyl-2,3-diol 1,2-dioxygenase. In: Schomburg, D., Schomburg, I. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 25. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-37704-2_85
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DOI: https://doi.org/10.1007/3-540-37704-2_85
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