GALT Human
Description
GALT is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Galactose-1-Phosphate Uridylyltransferase (GALT) is a crucial enzyme in the Leloir pathway of galactose metabolism. This enzyme catalyzes the conversion of galactose-1-phosphate and UDP-glucose to glucose-1-phosphate and UDP-galactose . The human recombinant form of this enzyme is often used in research to study its structure, function, and role in metabolic disorders such as classic galactosemia.
GALT is a homodimeric enzyme, meaning it consists of two identical subunits. Each subunit contains a covalent uridylylated intermediate and glucose-1-phosphate in the active site, as well as a structural zinc-binding site . The enzyme’s activity is dependent on the presence of zinc, which influences its stability and aggregation tendency .
The primary function of GALT is to facilitate the second step in the Leloir pathway, which is essential for the proper metabolism of galactose . This pathway converts galactose, a sugar found in milk and dairy products, into glucose, which can be used by the body for energy . The Leloir pathway consists of four enzymes: galactose mutarotase (GALM), galactokinase 1 (GALK1), GALT, and UDP-galactose 4’-epimerase (GALE) .
Mutations in the GALT gene can lead to classic galactosemia, a potentially lethal metabolic disorder . Over 300 disease-associated GALT mutations have been reported, with the majority being missense changes . These mutations can impair the enzyme’s ability to bind zinc or form the uridylylated intermediate, leading to protein misfolding and aggregation . Classic galactosemia is characterized by the inability to properly metabolize galactose, resulting in the accumulation of galactose-1-phosphate in the blood .
Human recombinant GALT is used in various research applications to better understand the enzyme’s structure and function. It serves as a model for studying the molecular consequences of disease mutations and for developing potential therapies . For example, the crystal structure of human GALT has been used to design pharmacological chaperone therapies that aim to stabilize the enzyme and prevent aggregation .
