Pyrimidine 5'-nucleosidase in Neisseria meningitidis. An enzyme specific for uridine 5'-monophosphate.
A previously unknown pyrimidine 5'-nucleosidase (pyrimidine 5'-nucleotide phosphoribohydrolase) specific for uridine 5'-monophosphate (5'-UMP) was present in crude extract from Neisseria meningitidis. Of seven strains, six were found to degrade the N-glycosidic linkage of 5'-UMP. One strain showed negligible activity. The substrate was quantitatively converted to uracil and ribose 5'-phosphate (R5P). Cytidine 5'-monophosphate (5'-CMP) or the 2-deoxy 5'-monophosphates of the pyrimidine nucleosides (5'-dUMP, 5'-dCMP, 5'-dTMP) were found not to be degraded. Neither was uridine 3'-monophosphate (3'-UMP) degraded by extracts from the three strains selected for this test.
Jyssum
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Kaptein W. Wilhelmsen og Frues Bakteriologiske Institutt, University of Oslo, Rikshospitalet, Norway.
D009699:N-Glycosyl Hydrolases / Q000302:isolation & purification*; D009345:Neisseria meningitidis / Q000201:enzymology*; D012267:Ribosemonophosphates / Q000096:biosynthesis; D013302:Streptomyces / Q000201:enzymology; D014498:Uracil / Q000096:biosynthesis; D014542:Uridine Monophosphate / Q000378:metabolism
D012267:Ribosemonophosphates; C031626:ribose-5-phosphate; D014498:Uracil; D014542:Uridine Monophosphate; D009699:N-Glycosyl Hydrolases; C019599:adenosine nucleosidase