2.7.2.8	ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate	-	-	
2.7.2.8	ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate	allosterically regulated mechanism for the enzyme from Maricaulis maris with roles for Lys356, Arg386, Asn391 and Tyr397 in the catalytic mechanism	-, 735596	
2.7.2.8	ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate	enzyme has to interact stoichiometrically with acetylglutamate synthase in order to be active	390290, 486081	
2.7.2.8	ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate	mechanism	642359	
2.7.2.8	ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate	random bi-bi mechanism	642358	
2.7.2.8	ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate	using an elastic network model representation a normal mode analysis shows that the conformational mechanisms for substrate binding by NAGK strongly correlate with the intrinsic dynamics of the enzyme in the unbound form. The conformational change observed between the open and closed forms of EcNAGK are essentially accomplished by movements along a small subset of modes	723511