Galactose mutarotase (GALM)

Galactose mutarotase (GALM) is an enzyme that catalyzes the interconversion of α-D-galactose and β-D-galactose, the first step in the Leloir pathway, which is responsible for normal galactose metabolism[1][3][4]. Structurally, GALM has been crystallized and extensively studied, showing key catalytic residues, particularly Glu 304 and His 170, required for its function. Its activity is essential for the proper utilization of galactose in cellular metabolism. Genetic defects affecting this enzyme can result in disorders of galactose metabolism, such as galactosemia. GALM belongs to the aldose 1-epimerase family of enzymes and is not a common drug target, nor are there approved drugs specifically interacting with it[1][3][4].

Other names

Galactose mutarotaseAldose 1-epimerasealdose mutarotasegalactomutarotaseBLOCK25GALAC4GLATHEL-S-63pIBD1Galactose enzyme activatorEpididymis secretory sperm binding protein Li 63p

Not applicable (No drugs target GALM directly; mechanism is enzymatic catalysis of galactose epimerization.)