Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (GFPT1)

Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (GFPT1) is an enzyme responsible for the first and rate-limiting step of the hexosamine biosynthetic pathway, catalyzing the conversion of fructose-6-phosphate and glutamine into glucosamine-6-phosphate. This pathway provides substrates for N- and O-glycosylation of proteins, thus regulating post-translational modification and cellular signaling. GFPT1 is expressed in most tissues, with predominance in muscle and limited expression in the brain. Alternative splicing generates isoforms with different activities; the muscle-specific GFPT1-L is important for neuromuscular junction stability and efficient glycolysis, but is less active than the ubiquitous GFPT1-S. Mutations in GFPT1 cause congenital myasthenic syndrome, manifesting as muscle weakness and neuromuscular dysfunction. GFPT1 is crucial for maintaining metabolic and glycoprotein homeostasis.

Other names

Glutamine--fructose-6-phosphate transaminase 1Glutamine:fructose-6-phosphate amidotransferase 1D-fructose-6-phosphate amidotransferase 1GFAT 1GFAT1Hexosephosphate aminotransferase 1GFPTCMSTA1GFAGFATGFPT1LGFAT1mMSLGGlucosamine--fructose-6-phosphate aminotransferase [isomerizing] 1

Drugs or compounds affecting GFPT1 would act by inhibiting or modifying the enzyme’s aminotransferase activity, thereby altering the flux through the hexosamine biosynthetic pathway, impacting protein glycosylation and metabolic regulation