GFPT2

GFPT2, also known as glutamine-fructose-6-phosphate transamidase 2, is an enzyme encoded by the GFPT2 gene. This gene is found in humans and other mammals. The GFPT2 enzyme plays a crucial role in the biosynthesis of glucosamine, a precursor molecule for a variety of important cellular compounds. Specifically, GFPT2 catalyzes the conversion of fructose-6-phosphate and glutamine into glucosamine-6-phosphate and glutamate. This reaction is considered the rate-limiting step in the hexosamine biosynthetic pathway, a metabolic route that significantly impacts glucose metabolism, insulin signaling, and protein glycosylation.

The hexosamine biosynthetic pathway is involved in the production of UDP-N-acetylglucosamine (UDP-GlcNAc), which serves as a substrate for O-GlcNAcylation. O-GlcNAcylation is a post-translational modification that occurs on serine and threonine residues of proteins and is dynamically regulated, similar to phosphorylation. This modification is implicated in a wide range of cellular processes, including gene expression, signal transduction, and protein stability. Consequently, GFPT2 activity is indirectly linked to these diverse cellular functions. Dysregulation of GFPT2 has been associated with various metabolic disorders, including type 2 diabetes and obesity, suggesting its potential involvement in the pathogenesis of these conditions. Further research continues to explore the precise roles of GFPT2 and the hexosamine biosynthetic pathway in health and disease.