Pyrimidine nucleoside catabolism in Sphingomonas paucimobilis: role of cytidine deaminase and uridine phosphorylase.
Pyrimidine nucleoside catabolism in the human pathogen Sphingomonas paucimobilis was studied. It was observed that S. paucimobilis was only capable of utilizing cytidine or deoxycytidine as a sole nitrogen source when glucose served as the carbon source. Thinlayer chromatographic analyses of cytidine and uridine catabolic products revealed that the enzymes cytidine deaminase and uridine phosphorylase were active in the extracts prepared from S. paucimobilis cells. The levels of cytidine deaminase and cytosine deaminase activities were lowered after growth on cytidine or deoxycytidine as a nitrogen source instead of ammonium sulfate. Uridine phosphorylase activity increased more than 4-fold after growth on deoxycytidine as a nitrogen source while growth on the nitrogen source cytidine caused a depression in phosphorylase activity.
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Olson Biochemistry Laboratories, Department of Chemistry, South Dakota State University, Brookings 57007, USA.
D003564:Cytidine Deaminase / Q000502:physiology*; D011549:Pseudomonas / Q000378:metabolism*; D011741:Pyrimidine Nucleosides / Q000378:metabolism*; D014543:Uridine Phosphorylase / Q000502:physiology*
D011741:Pyrimidine Nucleosides; D014543:Uridine Phosphorylase; D003564:Cytidine Deaminase