Comamonas testosteroni

Locher HH, T Leisinger, AM Cook (1991a) 4-Sulfobenzoate 3,4-dioxygenase. Purification and properties of a desulfonative two-component system from Comamonas testosteroni T-2. Biochem J 274 833-842. 

Schach S, B Tshisuaka, S Fetzner, F Lingens F (1995) Quinoline 2-oxidoreductase and 2-oxo-l,2-dihydro-quinoline 5,6-dioxygenase from Comamonas testosteroni 63. The first two enzymes in quinoline and 3-methylquinoline degradation. EurJ Biochem 232 536-544. 

The enzymes from Comamonas testosteroni for hydroxylation of quinoline to quinol-2-one (quinoline 2-oxidoreductase) and the dioxygenase responsible for the introduction of oxygen into the benzenoid ring (2-oxo-l,2-dihydroquinoline 5,6-dioxygenase) have been described (Schach et al. 1995). 

The transport of toluene-4-sulfonate into Comamonas testosteroni has been examined (Locher et al. 1993), and rapid uptake required growth of the cells with toluene-4-sulfonate or 4-methylbenzoate. From the results of experiments with various inhibitors, it was concluded that a toluenesulfonate anion/proton symport system operates rather than transport driven by a difference in electrical potential (A (/), and uptake could not take place under anaerobic conditions unless an electron acceptor such as nitrate was present. 

Mobus E, M Jahn, R Schmid, D Jahn, E Maser (1997) Testosterone-regulated expression of enzymes involved in steroid and aromatic hydrocarbon catabolism in Comamonas testosteroni. J Bacteriol 179 5951-5955. 

Horinouchi M, T Hayashi, H Koshino, T Kurita, T Kudo (2005) Identification of 9,17-dioxo-l,2,3,4,10,11, 19-hexanorandrostan-5-oic acid, 4-hydroxy-2-oxohexanoic acid, and 2-hydroxyhexa-2,4-dienoic acid and related enzymes involved in testosterone degradation in Comamonas testosteroni TA441. Appl Environ Microbiol 71 5275-5281. 

Goyal AK, GJ Zylstra (1996) Molecular cloning of novel genes for polycyclic aromatic hydrocarbon degradation from Comamonas testosteroni. Appl Environ Microbiol 62 230-236. 

Hurtubise Y, D Barriault, J Powlowski, M Sylvestre (1995) Purification and characterization of the Comamonas testosteroni B-356 biphenyl dioxygenase components. J Bacteriol 111 6610-6618. 

Provident MA, JM O Brien, J Ruff, AM Cook, IB Lambert (2006) Metabolism of isovanillate, vanillate, and veratrate by Comamonas testosteroni strain BR6020. J Bacteriol 188 3862-3869. 

Schlafli HR, MA Weiss, T Leisinger, AM Cook (1994) Terephthalate 1,2-dioxygenase system from Comamonas testosteroni T-2 purification and some properties of the oxygenase component. J Bacteriol 176 6644-6652. 

Junker F, R Kiewitz, AM Cook (1997) Characterization of the / -toluenesulfonate operon tsaMBCD and tsaR in Comamonas testosteroni T-2. J Bacteriol 179 919-927. 

Hollender J, W Dott, J Hopp (1994) Regulation of chloro- and methylphenol degradation in Comamonas testosteroni JH5. Appl Environ Microbiol 60 2330-2338. 

Sylvestre M (1995) Biphenyl/chlorobiphenyls catabolic pathway of Comamonas testosteroni B-356 prospect for use in bioremediation. Int Biodet Biodeg 35 189-211. 

Oubrie A, Rozeboom HJ, Kalk KH, Huizinga EG, Dijkstra BW. 2002. Crystal structure of qui-nohemoprotein alcohol dehydrogenase from Comamonas testosteroni Structural basis for substrate oxidation and electron transfer. J Biol Chem 211 3727-3732. 

A thermally stable NHase from Comamonas testosteroni 5-MGAM-4D (ATCC 55 744) [22] was recombinantly expressed in Escherichia coli, and the resulting transformant cells immobilized in alginate beads that were subsequently chemically cross-linked with glutaraldehyde and polyethylenimine. This immobilized cell catalyst (at 0.5 % dew per reaction volume) was added to an aqueous reaction mixture containing 32wt% 3-cyanopyridine at 25 °C, and a quantitative conversion to nicotinamide was obtained. The versatility of this catalyst system was further illustrated by a systematic study of substrates, which included... 

Petrillo, K.L., Wu, S., Hann, E.C. et al. (2005) Over-expression in Escherichia coli of a thermally stable and regio-selective nitrile hydratase from Comamonas testosteroni 5-MGAM-4D. Applied Microbiology and Biotechnology, 67 (5), 664-670. 

The poly(HA) depolymerases of the bacteria Alcaligenes faecalis (strains AE122 and Tl), Comamonas acidovorans, Comamonas testosteroni, Comamonas sp., Pseudomonas fluorescens, Pseudomonas lemoignei, Pseudomonas stutzeri, Ralstonia pickettii, Streptomyces exfoliatus, and of the fungi Paecilomyces lilaci-nus, Penicillium funiculosum, and Penicillium pinophilum have been purified and characterized (for details see Table 1). Poly(HA) depolymerases share several characteristics ... 

Schach, S. Schward, G. Fetzner, S., and Lingens, F., Microbial Metabolism of Quinoline and Related Compounds. XVII. Degradation of 3-Methylquinoline by Comamonas Testosteroni 63. Biol. Chem. Hoppe-Seyler, 1993. 374 pp. 175-181. 

A. Oubrie, H.J. Rozeboom, K.H. Kalk, E.G. Huizinga, and B.W. Dijkstra, Crystal structure of qui-nohemoprotein alcohol dehydrogenase from Comamonas testosteroni. J. Biol. Chem. Til, 3727-3732 (2002). 

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