GNPNAT1 Human

GNPNAT1 belongs to the family of transferases, specifically acyltransferases, which transfer an acetyl group from acetyl-CoA to the primary amine in glucosamine-6-phosphate. This reaction generates a free CoA and N-acetyl-D-glucosamine-6-phosphate . The systematic name of this enzyme class is acetyl-CoA:D-glucosamine-6-phosphate N-acetyltransferase .

The hexosamine biosynthesis pathway (HBP) is one of the glucose processing pathways in general metabolism. It shares the initial two steps with glycolysis and diverges only a small portion of glucose flux from this more traditional glycolytic pathway . The end product of this pathway is UDP-N-Acetylglucosamine, which is involved in the modification of complex molecules such as glycolipids, proteoglycans, and glycoproteins .

GNPNAT1 is a small dimeric protein located in the Golgi matrix and endomembrane . It serves as the rate-limiting enzyme in the second step of the HBP . The enzyme’s activity is crucial for the biosynthesis of UDP-N-acetylglucosamine, which acts as a carrier of N-acetylglucosamine, a monomeric unit of chitin, a structural polymer found in the shells of crustaceans and insects, as well as the cell wall of fungi .

The GNPNAT1 gene is a protein-coding gene associated with several pathways, including the synthesis of substrates in N-glycan biosynthesis and metabolism of proteins . Diseases associated with GNPNAT1 include Rhizomelic Dysplasia, Ain-Naz Type, and Hyperinsulinemic Hypoglycemia, Familial, 2 . The gene is predicted to be involved in the UDP-N-acetylglucosamine biosynthetic process and is located in the late endosome, Golgi apparatus, and endoplasmic reticulum .

Human recombinant GNPNAT1 is used in various research applications to study its role in metabolic pathways and its implications in diseases. Understanding the enzyme’s function and regulation can provide insights into metabolic disorders and potential therapeutic targets.