Open AccessPyrimidine base and ribonucleoside catabolic enzyme activities of the Pseudomonas diminuta group
Author(s) -
West Thomas P.
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05586.x
Subject(s) - dihydropyrimidine dehydrogenase , ribonucleoside , pyrimidine , hydrolase , dehydrogenase , biochemistry , enzyme , biology , adenosine deaminase , enzyme assay , nucleoside , pyrimidine metabolism , nucleotide salvage , chemistry , purine , nucleotide , thymidylate synthase , rna , fluorouracil , genetics , chemotherapy , gene
Pyrimidine base and ribonucleoside catabolic enzyme activities of the two type strains of the Pseudomonas diminuta group were investigated for taxonomic classification purposes. The presence of the pyrimidine salvage enzyme nucleoside hydrolase was indicated in both type strains following thin‐layer chromatographic analysis. The presence of the hydrolase was also confirmed by enzyme assay. In addition, the activities of the pyrimidine salvage enzymes dihydropyrimidine dehydrogenase and dihydropyrimidinase were measurable in cell‐free extracts of both P. diminuta and P. vesicularis . An absence of cytosine deaminase activity was found when assaying extracts of the two type strains. Nucleoside hydrolase and dihydropyrimidine dehydrogenase levels in P. vesicularis were influenced by carbon source while dihydropyrimidinase activity was observed to increase after P. diminuta growth on dihydrothymine as a nitrogen source.