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Pseudomonas catalase

Figure 2. Aerobic catabolism of methylated sulfides (adapted from Kelly, 1988). 1) DMSO reductase (Hyphomicrobium sp.) 2) DMDS reductase (Thiobacillus sp. 3) trimethylsulfonium-tetrahydrofolate methyltransferase (Pseudomonas sp.) 4) DMS monooxygenase 5) methanethiol oxidase 6) sulfide oxidizing enzymes 7) catalase 8) formaldehyde dehydrogenase 9) formate dehydrogenase 10) Calvin cycle for CO2 assimilation (Thiobacillus sp.) 11) serine pathway for carbon assimilation (Hyphomicrobium sp.). Figure 2. Aerobic catabolism of methylated sulfides (adapted from Kelly, 1988). 1) DMSO reductase (Hyphomicrobium sp.) 2) DMDS reductase (Thiobacillus sp. 3) trimethylsulfonium-tetrahydrofolate methyltransferase (Pseudomonas sp.) 4) DMS monooxygenase 5) methanethiol oxidase 6) sulfide oxidizing enzymes 7) catalase 8) formaldehyde dehydrogenase 9) formate dehydrogenase 10) Calvin cycle for CO2 assimilation (Thiobacillus sp.) 11) serine pathway for carbon assimilation (Hyphomicrobium sp.).
MCD spectra perhaps provide the best fingerprint for the existence of an FeIV=0 structure. Fig. 8 shows that there is a great similarity between the spectra of horseradish peroxidase compound II, horseradish peroxidase compound X, cytochrome c peroxidase compound I, Pseudomonas aeruginosa peroxidase compound I and ferryl myoglobin at acid pH. Similar features are seen in the spectra of catalase [170] and myoglobin [171] compound II. [Pg.94]

Protons, transhydrogenase and, 77-78 Protoporphyrin IX, catalase and, 366 Pseudomonas transhydrogenase function, 80... [Pg.453]

Bromoperoxidase has been isolated from Pseudomonas aureofaciens ATCC 15926, also displays peroxidase and catalase activities, and contains ferriprotoporphyrin IX (van Pee and Lingens 1985). Four different bromoperoxidases have been isolated from Streptomyces griseus (Zeiner et al. 1988). Only one of them, however, contains ferriprotoporphyrin IX and displays peroxidase and catalase activities. This illustrates that there are two different groups of enzymes, one of which lacks heme prosthetic groups. [Pg.311]

The isolate 9B, purified from the mixed culture enriched in the presence of di-n-tridecyl sulfosuccinate, was identified as Pseudomonas sp. on the basis of the following results. Morphology on nutrient agar plates circular, entire, smooth, shiny umbonate colonies 2-4 mm in diameter. Positive tests catalase, acid from glucose growth at 37°C,... [Pg.197]

Brown, S. M., Howell, M L., Vasil, M. B., Anderson, A. J., and Hassett, D. J. (1995). Cloning and characterization of the katB gene of Pseudomonas aeruginosa encoding a hydrogen peroxide-indudble catalase Purification of KatB, cellular localization, and demonstration that it is essential for optimal resistance to hydrogen peroxide. /. Bacteriol. 177,6536-6544. [Pg.414]

Elkins, J. G., Hassett, D. J., Stewart, P. S., Schweizer, H. P., and McDermott, T. R. (1999). Pseudomonas aeruginosa biofilm resistance to hydrogen peroxide Protective role of catalase. Appl. Environ. Microbiol. 65, 4594-4600. [Pg.414]

Tests for Pseudomonas aeruginosa are not used in the standard tests for the examination of water. Tests for this organism are frequently used by manufacturers of food, drinks, and pharmaceuticals. Pseudomonas is a Gram-negative rod, giving positive catalase and oxidase tests and producing pigmentation. [Pg.120]

L-Lactate L-Lactate can be determined with two different enzyme systems the lactate-2-mono-oxyge-nase (EC 1.13.12.4) from Mycobacterium smegmatis providing a linear range of 0.005-2 mmol 1 in 0.2 mol 1 sodium phosphate buffer, pH 7.0, or the lactate oxidase from Pediococcus pseudomonas (EC 1.1.3.2) together with catalase giving a linear range of 0.002-1 mmol 1 in 0.1 mol 1 phosphate buffer, pH 7.0. [Pg.4372]

Klinke S, de Roo G, Witholt B, Kessler B (2000) Role of phaD in accumulation of medium-chain-length poly(3-hydroxyalkanoates) in Pseudomonas oleovorans. Appl Environ Microbiol 66 3705-3710 Knauf HJ, Vogel RE, Hammes WP (1992) Cloning, sequence, and phenotypic expression of KatA which encodes the catalase of Lactobacillus sake LTH677. Appl Environ Microbiol 58 832-839... [Pg.71]

L-Lysine is converted by an enzyme from a strain of Pseudomonas into y-aminovalerianic acid, NH3, and COg. The rate of incorporation of in dry matter is fairly important. These results point to the frequent occurrence of reactions such as (91) and many others similar and unknown. In the L-lysine oxidase experiments oxygen consumption cannot be affected by crystalline catalase. Methylene blue, triphenyltetrazolium chloride, and 2,6-dichlorophenolindolephenol cannot replace oxygen. [Pg.399]


See other pages where Pseudomonas catalase is mentioned: [Pg.249]    [Pg.866]    [Pg.134]    [Pg.236]    [Pg.271]    [Pg.249]    [Pg.116]    [Pg.866]    [Pg.191]    [Pg.76]    [Pg.473]    [Pg.4]    [Pg.498]    [Pg.697]    [Pg.525]    [Pg.527]    [Pg.162]    [Pg.6]    [Pg.407]    [Pg.110]    [Pg.161]    [Pg.41]    [Pg.17]    [Pg.212]   
See also in sourсe #XX -- [ Pg.136 ]




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