Phosphoglucomutase 2 (PGM2)

Phosphoglucomutase 2 (PGM2) is an enzyme of the α-D-phosphohexomutase superfamily, distinct from the classical phosphoglucomutase 1 (PGM1). It is most active on pentose phosphosugars, including ribose 1-phosphate and deoxyribose 1-phosphate, and shows a tissue-dependent expression pattern with highest levels in lung, spleen, and thymus. PGM2 catalyzes the reversible transfer of a phosphate group within sugars, which is essential for processes such as glycogen synthesis, glycogen breakdown, and nucleotide sugar metabolism. Like other phosphoglucomutases, it requires a phosphorylated serine residue for activity, and a divalent metal ion such as Mg²⁺ for optimal function. Structurally, PGM2 shares the four-domain “heart-shaped” fold typical for the superfamily and contains conserved motifs for substrate and metal binding. Though not yet a direct drug target, enzymes of this family are important for metabolic regulation, and dysfunction of related enzymes is linked to congenital metabolic disorders. PGM2's role is being actively studied, particularly concerning its unique substrate preferences and expression patterns.

Other names

PGM2phosphopentomutase