2.7.1.162	ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate	-	-	
2.7.1.162	ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate	enzyme acts by a sequential bi bi (two substrates-two products) mechanism, with the reaction occurring after the binding of both ATP and N-acetylhexosamine	-, 677700	
2.7.1.162	ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate	open–close conformational change at the active site, structure overview	-, 737770	
2.7.1.162	ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate	regio- and stereoselectivity, catalytic mechanism, structure-function analysis, overview. Nucleophilic attack on the gamma-phosphate atom in a bond-breaking/bond formation manner of transfer (an SN2-like reaction). The carboxyl group of residue Asp208 within hydrogen-bond distance of C1 OH of GlcNAc/GalNAc is likely to serve as the active-site general base	-, 737343	
2.7.1.162	ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-alpha-D-hexosamine 1-phosphate	the N-acetylhexosamine 1-kinase shows a concerted mechanism of two-magnesium-ion-assisted GlcNAc phosphorylation, flexibility behavior of lid motif upon substrate recognition, and water-assisted GlcNAc-1-P release	-, 760251