Galactose-1-phosphate uridylyltransferase (GALT)

Galactose-1-phosphate uridylyltransferase (GALT) is a pivotal enzyme in the Leloir pathway of galactose metabolism, responsible for catalyzing the reversible reaction of galactose-1-phosphate and UDP-glucose to glucose-1-phosphate and UDP-galactose[1][2][3]. This conversion is essential for the utilization of galactose from dietary lactose. Loss-of-function mutations in the GALT gene cause classic galactosemia, an autosomal recessive metabolic disorder delineated by the toxic buildup of galactose-1-phosphate, resulting in severe neonatal disease such as jaundice, hepatomegaly, cataracts, and without treatment, can be fatal[2][3][4]. More than 300 mutations have been identified, primarily missense changes, leading to varying degrees of enzymatic deficiency. The only current therapy is life-long dietary elimination of galactose. Recent structural studies have clarified the importance of uridylylation and metal (zinc) binding for enzyme stability and function. Despite dietary management, patients often experience long-term complications including neurological and reproductive issues[2][3][4].

Other names

Galactose-1-phosphate uridylyltransferaseGALTGal-1-P uridylyltransferaseUDP-glucose--hexose-1-phosphate uridylyltransferaseGalactose-1-phosphate uridyl transferaseG1PUTEC 2.7.7.12

Not applicable (therapeutic approach is not direct pharmacological targeting, but dietary modification to prevent substrate accumulation)[2][3][4]