Glucosamine-6-phosphate deaminase

Glucosamine-6-phosphate deaminase is an enzyme (EC 3.5.99.6) that catalyzes the reversible conversion of D-glucosamine 6-phosphate and water to D-fructose 6-phosphate and ammonia, acting as a hydrolase and isomerase in the metabolism of amino sugars. Mechanistically, this enzyme opens the pyranose ring of glucosamine-6-phosphate and mediates both isomerization and deamination steps, which are essential for the hexosamine biosynthetic pathway and cellular aminosugar metabolism. It is structurally a hexameric enzyme (at least in E. coli) and is regulated allosterically—for example, by N-acetylglucosamine-6-phosphate. Although disruptions in this enzyme's function could theoretically contribute to human disease, there is little direct evidence of congenital disorders or common pathologies directly tied to glucosamine-6-phosphate deaminase deficiency in humans.

Other names

glucosamine-6-phosphate isomeraseglucosaminephosphate isomerasephosphoglucosaminisomeraseglucosamine phosphate deaminaseaminodeoxyglucosephosphate isomerasephosphoglucosamine isomerase

Catalyzes ring opening of glucosamine-6-phosphate, followed by base-catalyzed deamination and isomerization to fructose-6-phosphate; mechanism features Asp72 as a key proton exchanger residue