2.7.4.6	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate	isozyme NDPKB shows a ping-pong phospho-transfer mechanism, salt and nucleotide dependent NDPKB assembly is dynamic and requires its catalytic activity	691099	
2.7.4.6	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate	many nucleoside diphosphates can act as acceptors, while many ribo- and deoxyribonucleoside triphosphates can act as donors	-	
2.7.4.6	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate	mechanism	642637, 642662, 642665, 642669, 642673	
2.7.4.6	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate	mechanism, role of 3’-OH moiety of nucleotide	642672	
2.7.4.6	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate	overview on mechanism	642682	
2.7.4.6	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate	phosphoenzyme intermediate with 2-4 mol phosphate per mol of enzyme	642661	
2.7.4.6	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate	ping pong mechanism with formation of an enzyme intermediate phosphorylated at His118	694346	
2.7.4.6	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate	the catalytic mechanism involves a phosphoenzyme intermediate	642644, 642646, 642655, 642656	
2.7.4.6	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate	the reaction catalyzed by NDK starts with the transfer of a phosphate from ATP to His117. ADP is then released and the acceptor nucleoside diphosphate is bound and phosphorylated. Nucleotide phosphates are coordinated by a network of basic Arg and His residues, and a polar Thr. All NDKs follow a ping-pong enzymatic mechanism involving a phosphorylated histidine residue in the active site	737374	
2.7.4.6	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate	two-step ping-pong mechanism	-, 660576