Glucosamine-6-phosphate deaminase

In enzymology, a glucosamine-6-phosphate deaminase is an enzyme that catalyzes the chemical reaction


 * D-glucosamine 6-phosphate + H2O $$\rightleftharpoons$$ D-fructose 6-phosphate + NH3

Thus, the two substrates of this enzyme are glucosamine 6-phosphate and H2O, whereas its two products are fructose 6-phosphate and NH3.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol isomerizing). Other names in common use include glucosaminephosphate isomerase, glucosamine-6-phosphate isomerase, phosphoglucosaminisomerase, glucosamine phosphate deaminase, aminodeoxyglucosephosphate isomerase, and phosphoglucosamine isomerase. This enzyme participates in aminosugars metabolism. This enzyme has at least one effector, N-Acetyl-D-glucosamine 6-phosphate.

Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes, , , , and.