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Pseudomonas testosteroni

The isomerase (EC 5.3.3.1) from Pseudomonas testosteroni has been studied in detail. This enzyme transfers a hydrogen from position 4 to the 6fl-position. Although several isomerases have been detected, their presence is often seen as presenting problems as they frequently lead to product diversification. [Pg.321]

Harpel MR, JD Lipscomb (1990) Gentisate 1,2-dioxygenase fiomPseudontonas. Purification, characterization, and comparison of the enzymers from Pseudomonas testosteroni and Pseudomonas acidovorans. J Biol Chem 265 6301-6311. [Pg.139]

Sondossi M, M Sylvestre, D Ahmad (1992) Effects of chlorobenzoate transformation on the Pseudomonas testosteroni biphenyl and chlorobiphenyl degradation pathway. Appl Environ Microbiol 58 485-495. [Pg.239]

FIGURE 8.30 Biodegradation of 3,4-dihydroxybenzoate mediated by (a) 4,5-dioxygenase in Pseudomonas testosteroni and (b) 2,3-dioxygenase in Bacillus macerans. [Pg.429]

Wheelis M, NJ Palleroni, RY Stanier (1967) The metabolism of aromatic acids by Pseudomonas testosteroni and P. acidovorans. Arch Mikrobiol 59 302-314. [Pg.446]

Ahmad D, M Sylvestre, M Sondossi (1991) Subcloning of bph genes from Pseudomonas testosteroni B-356 in Pseudomonas putida and Escherichia colt evidence for dehalogenation during initial attack on chloro-biphenyls. Appl Environ Microbiol 57 2880-2887. [Pg.476]

Ahmad D, R Masse, M Sylvestre (1990) Cloning, physical mapping and expression in Pseudomonas putida of 4-chlorobiphenyl transformation genes from Pseudomonas testosteroni strain B-356 and their homology to the genomic DNA from other PCB-degrading bacteria. Gene 86 53-61. [Pg.476]

Experiments nsing Pseudomonas testosteroni strain B-356 in microcosm systems revealed the necessity of adding biphenyl to promote degradation of the tetrachlorinated congeners of Arochlor 1242, and the effectiveness of repeated inoculation (Barriault and Sylvestre 1993). [Pg.665]

Pseudomonas fluorescens, 1 732 11 4 Pseudomonas putida, 11 4 Pseudomonas testosteroni alcohol dehydrogenase, 3 672 Pseudopelletierine, 2 81-82 Pseudoplastic flow, 7 280t Pseudoplastic fluids, 11 768 Pseudoplasticity, 10 679 Pseudoplastic with yield stress flow, 7 280t Pseudopolymorphism, 8 69... [Pg.771]

D5-3-ketosteroid Pseudomonas testosteroni AOT/isooctane Kinetics and stability studies [93]... [Pg.132]

In the study of Pettigrew et al. (1990) a bacterial consortium was shown to mineralize 4-CB and dehalogenate 4,4 -CB. It included three isolates a Pseudomonas testosteroni which catalyzed the breakdown of the chlorinated biphenyls to 4-chlorobenzoic acid (the so-called upper pathway ) an Arthrobacter species that mediated 4-chlorobenzoic acid mineralization (the so-called lower pathway ) and a third strain from the consortium with a role that has not been determined. This pattern of co-culture degradation for upper and lower pathway degradation has been observed generally in the field of PCB biodegradation. Few strains have been shown with the capability to catalyze both upper and lower pathway degradation. [Pg.214]

Sylvestre and co-workers cloned the genes from their Pseudomonas testosteroni strain B-356, which had been demonstrated to biodegrade 4-CB into 4-chlorobenzoic acid. In these studies, they demonstrated the homology between many different PCB-degrading bacteria isolated from different geographic locations (Ahmad etal.,... [Pg.223]

Sondossi, M., Sylvestre, M., Ahmad, D. Masse, R. (1991). Metabolismof hydroxybiphenyl and chloro-hydroxybiphenyl by biphenyl/chlorobiphenyl degrad i ng Pseudomonas testosteroni, strain B-356- Journal of Industrial Microbiology, 7, 77-88. [Pg.251]

Ahmad, D., Masse, R. Sylvestre, M. (1990). Cloning and expression of genes involved in 4-chlorobiphenyl transformation by Pseudomonas testosteroni homology to poly-chlorobiphenyl-degrading genes in other bacteria. Gene, 86, 53-61. [Pg.376]

Cultures of Pseudomonas testosteroni, of an unidentified bacterium isolated from soil from Seveso, Italy, and of a mixture of 6 unidentified bacterial strains isolated from Seveso soil were incubated aerobically with 14C-2,3,7,8-TCDD for 35, 54, and 12 weeks, respectively (Philippi et al. 1982). Results showed the occurrence of a metabolite of 14C-2,3,7,8-TCDD in all three cultures. The polar metabolite amounted to approximately 1% of the input material and was found to be a hydroxylated derivative of 14C-2,3,7,8-TCDD (Philippi et al. 1982). [Pg.453]

Benzoic acid Alcaligenes eutophus Aspergillus niger Azotobacter sp. Bacillus sp. Pseudomonas sp. Pseudomonas acidovorans Pseudomonas testosteroni Pseudomonas sp. strain HI Pseudomonas PN-1... [Pg.247]

K. S. Kim, W. Lee, K. Y. Choi, and B.-H. Oh, Crystal structure of delta A -3-ketosteroid isomerase from pseudomonas testosteroni in complex with equilenin settles the correct hydrogen bonding scheme for transition state stabilization, J. Biol. Chem. 274, 32863-32868 (1999). (e) T. K. Manojkumar, C. Cui, and K. S. Kim, Theoretical insights into the mechanism of acetylcholinesterase-catalyzed acylation of acetylcholine, J. Comput. Chem. 26, 606-611... [Pg.191]

The enzyme 3a-hydroxysteroid dehydrogenase (EC 1.1.1.50), which is isolated from Pseudomonas testosteroni, catalyzes the conversion of all 3a-hydroxycholanic acids to 3-ketochoIanic acids, with the concomitant reduction of NAD to NADH. The NADH formed in the reaction is then determined spectrophotometrically at 340 nm. To ensure complete reaction, hydrazine is usually added to bind the 3-keto products (P2). The optimum conditions for enzymatic assay include a pH of 9.0 to 9.5 and reaction temperature in the range 20 to 40 C (T13). Reaction rates for individual bile acids may not be identical, but the assay is normally carried out as an endpoint determination. Alternatively, the addition of bovine serum albumin appears to overcome the problem of variable aflinity of 3a-hy-droxysteroid dehydrogenase for different bile acids if reaction rates are to be measured (S13). [Pg.197]


See other pages where Pseudomonas testosteroni is mentioned: [Pg.730]    [Pg.777]    [Pg.125]    [Pg.223]    [Pg.428]    [Pg.430]    [Pg.460]    [Pg.461]    [Pg.658]    [Pg.163]    [Pg.138]    [Pg.696]    [Pg.28]    [Pg.160]    [Pg.86]    [Pg.291]    [Pg.203]    [Pg.696]    [Pg.210]    [Pg.328]    [Pg.199]    [Pg.550]   
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Pseudomonas testosteroni hydroxysteroid dehydrogenases

Pseudomonas testosteroni ketosteroid isomerase

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