The PGM2 protein shares about 20% identity with mammalian PGM1. Sequence analysis suggested that PGM2 is a cytosolic protein. Quantitative RT-PCR of mouse tissues detected the highest expression levels of PGM2 in lung, spleen, and thymus. PGM2 acted more than 10-fold better as a phosphopentomutasethan as a phosphoglucomutase. PGM2 may play a role in congenital immunodeficiencies. phosphopentomutase uses ribose 1-phosphate and deoxyribose 1-phosphate, which are formed by purine nucleoside phosphorylase and uridine phosphorylase, and that the absence of phosphopentomutase should result in the accumulation of ribose 1-phosphate and deoxyribose 1-phosphate and therefore in a functional block of purine nucleoside phosphorylase.
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