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  • 1
    Digitale Medien
    Digitale Medien
    Pyrimidine ribonucleoside catabolism in Pseudomonas fluorescens biotype A (1990)
    Springer
    Antonie van Leeuwenhoek 57 (1990), S. 253-257 
    Details
    ISSN: 1572-9699
    Schlagwort(e): Pseudomonas ; pyrimidines ; nucleoside hydrolase ; cytosine deaminase
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The pyrimidine ribonucleosides uridine or cytidine were shown to serve as a source of nitrogen or carbon for the growth of Pseudomonas fluorescens strain A126. After incubation of either pyrimidine ribonucleoside with extracts of this strain, the resultant catabolic products were detected by thin-layer chromatography. It was found that pyrimidine ribonucleoside catabolism in this pseudomonad involved the enzymes nucleoside hydrolase and cytosine deaminase. The specific activities of both these enzymes could be influenced by the nitrogen or carbon source present in the medium.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00400157
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Pyrimidine base and ribonucleoside utilization by thePseudomonas alcaligenes group (1991)
    Springer
    Antonie van Leeuwenhoek 59 (1991), S. 263-268 
    Details
    ISSN: 1572-9699
    Schlagwort(e): cytosine deaminase ; dihydropyrimidinase ; dihydropyrimidine dehydrogenase ; nucleoside hydrolase ; Pseudomonas ; pyrimidines
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Pyrimidine base and ribonucleoside utilization was investigated in the two type strains of thePseudomonas alcaligenes group. As sole sources of nitrogen, the pyrimidine bases uracil, thymine and cytosine as well as the dihydropyrimidine bases dihydrouracil and dihydrothymine supported the growth ofPseudomonas pseudoalcaligenes ATCC 17440 but neither these bases nor pyrimidine nucleosides supportedPseudomonas alcaligenes ATCC 14909 growth. Ribose, deoxyribose, pyrimidine and dihydropyrimidine bases as well as pyrimidine nucleosides failed to be utilized by eitherP. pseudoalcaligenes orP. alcaligenes as sole carbon sources. The activities of the pyrimidine salvage enzymes nucleoside hydrolase, cytosine deaminase, dihydropyrimidine dehydrogenase and dihydropyrimidinase were detected in cell-free extracts ofP. pseudoalcaligenes andP. alcaligenes. InP. pseudoalcaligenes, the levels of cytosine deaminase, dihydropyrimidine dehydrogenase and dihydropyrimidinase could be affected by the nitrogen source present in the culture medium.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00583679
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Pyrimidine ribonucleoside catabolic enzyme activities ofPseudomonas pickettii (1994)
    Springer
    Antonie van Leeuwenhoek 66 (1994), S. 307-312 
    Details
    ISSN: 1572-9699
    Schlagwort(e): pyrimidine ; nucleoside hydrolase ; cytosine deaminase ; dihydropyrimidine dehydrogenase ; dihydropyrimidinase ; phosphatase ; Pseudomonas
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Pyrimidine ribonucleoside catabolic enzyme activities of the opportunistic pathogenPseudomonas pickettii were examined. Of the pyrimidine and related compounds tested, only dihydrouracil (nitrogen source) and ribose (carbon source) supported growth. Thin-layer chromatographic separation of the uridine and cytidine catabolities produced byP. pickettii extracts indicated that this pseudomonad contained nucleoside hydrolase activity. Its presence was confirmed by enzyme assay. Hydrolase activity was elevated in both glucose- and ribose-grown cells relative to succinate-grown cells. Nucleoside hydrolase activity was depressed when dihydrouracil served as a nitrogen source. Cytosine deaminase activity was present in extracts prepared from succinate-, glucose- or ribose-grown cells when (NH4)2SO4 served as the nitrogen source although cells grown on glucose or ribose exhibited a higher enzyme activity. Cytosine deaminase activity was not detected in extracts prepared from cells grown on dihydrouracil as a nitrogen source. Both dihydropyrimidine dehydrogenase and dihydropyrimidinase activities were measurable inP. pickettii. The dehydrogenase activity was higher with NADH than with NADPH as its nicotinamide cofactor when uracil served as its substrate. Carbon source did not affect dehydrogenase or dihydropyrimidinase activity greatly but both activities were diminished in cells grown on the nitrogen source dihydrouracil.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00882765
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    Degradation of pyrimidine ribonucleosides by Pseudomonas aeruginosa (1996)
    Springer
    Antonie van Leeuwenhoek 69 (1996), S. 331-335 
    Details
    ISSN: 1572-9699
    Schlagwort(e): pyrimidine ; nucleoside hydrolase ; cytosine deaminase ; Pseudomonas aeruginosa ; 5-methylcytosine
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Pyrimidine ribonucleoside degradation in the human pathogen Pseudomonas aeruginosa ATCC 15692 was investigated. Either uracil, cytosine, 5-methylcytosine, thymine, uridine or cytidine supported P. aeruginosa growth as a nitrogen source when glucose served as the carbon source. Using thin-layer chromatographic analysis, the enzymes nucleoside hydrolase and cytosine deaninase were shown to be active in ATCC 15692. Compared to (NH4)2SO4-grown cells, nucleoside hydrolase activity in ATCC 15692 approximately doubled after growth on 5-methylcytosine as a nitrogen source while its cytosine deaminase activity increased several-fold after growth on the pyrimidine bases and ribonucleosides examined as nitrogen sources. Regulation at the level of protein synthesis by 5-methylcytosine was indicated for nucleoside hydrolase and cytosine deaminase in P. aeruginosa.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00399622
    Standort Signatur Erwartet Verfügbarkeit
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    Artikel (Nationallizenzen)
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