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Abstract Background The purine salvage enzyme inosine 5'-monophosphate (IMP)-specific 5'-nucleotidase catalyzes degradation of IMP to inosine. Although this enzymatic activity has been purified and characterized in <it>Saccharomyces cerevisiae</it>, the gene encoding IMP 5'-nucleotidase had not been identified. Results Mass spectrometry analysis of several peptides of this enzyme purified from yeast allowed identification of the corresponding gene as <it>YOR155c</it>, an open reading frame of unknown function, renamed <it>ISN1</it>. The deduced Isn1p sequence was clearly not homologous to 5'-nucleotidases from other species. However, significant similarities to Isn1p were found in proteins of unknown function from <it>Neurospora crassa</it>, <it>Plasmodium falciparum </it>and several yeast species. Knock-out of <it>ISN1 </it>resulted in the total loss of IMP-specific 5'-nucleotidase activity, thus confirming that the <it>ISN1 </it>gene indeed encodes the enzymatic activity purified from yeast. <it>In vivo </it>studies revealed that, when IMP is overproduced through constitutive activation of the IMP <it>de novo </it>synthesis pathway, <it>ISN1 </it>is required for excretion of inosine and hypoxanthine in the medium. Conclusion We have identified a new yeast gene, <it>ISN1 </it>(<it>YOR155c</it>), as encoding IMP-specific 5'-nucleotidase activity. The <it>ISN1 </it>gene defines a new type of 5'-nucleotidase which was demonstrated to be functional <it>in vivo</it>.</p

The yeast ISN1 (YOR155c) gene encodes a new type of IMP-specific 5'-nucleotidase.