GFPT1

GFPT1 (Glutamine--fructose-6-phosphate transaminase 1) is an enzyme that in humans is encoded by the GFPT1 gene. This enzyme plays a crucial role in the hexosamine biosynthesis pathway, which is important for the post-translational modification of proteins and the production of polysaccharides. GFPT1 catalyzes the conversion of fructose 6-phosphate and glutamine to glucosamine 6-phosphate and glutamate, serving as a rate-limiting step in the production of uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), a critical substrate for glycosylation processes.

The GFPT1 gene is located on chromosome 2q14.3 and consists of multiple exons and introns. Mutations in this gene have been associated with a rare autosomal recessive disorder known as Congenital Myasthenic Syndrome 13 (CMS13), characterized by muscle weakness and fatigue. This condition highlights the importance of GFPT1 in neuromuscular junction function and the broader significance of the hexosamine biosynthesis pathway in human health.

In addition to its role in disease, GFPT1 is also involved in the regulation of glucose metabolism and has been implicated in the development of insulin resistance and diabetes mellitus type 2. The enzyme's activity is influenced by various factors, including nutrient availability and hormone levels, which can affect the flux through the hexosamine biosynthesis pathway and, consequently, the glycosylation of proteins and lipids.

Research into GFPT1 and its associated pathways offers potential therapeutic targets for treating related metabolic and neuromuscular disorders. Inhibitors of GFPT1, for example, are being explored for their potential to modulate the pathway in diseases characterized by aberrant glycosylation patterns.

See also

• Hexosamine biosynthesis pathway
• Congenital Myasthenic Syndromes
• Glucose metabolism
• Insulin resistance