6.3.4.15	A43G	catalytic efficiency is 2fold lower than catalytic efficiency of wild-type enzyme	-, 671759	
6.3.4.15	D571N	naturally occuring mutation, important in positioning K579 in the AMP binding site	691104	
6.3.4.15	D615Y	naturally occuring mutation in the loop between alpha3 and beta6 that cover AMP, may coordinate oxygens of the AMP phosphate	691104	
6.3.4.15	D634Y	naturally occuring mutation of a solvent exposed residue, distal to active site on alpha4 and alpha5, respectively	691104	
6.3.4.15	D715G	naturally occuring mutation on beta9, may be involved in capping and stabilising the catalytic domain structure	691104	
6.3.4.15	DELTA1-81	elimination of N-terminal domain plus part of the central domain, complete loss of ligase activity	-, 745788	
6.3.4.15	DELTA1-81	elimination of N-terminal domain plus part of the central domain, loss of ligase activity	-, 746268	
6.3.4.15	DELTA2-63	elimination of N-terminal domain, mutant shows normal ligase activity	-, 746268	
6.3.4.15	DELTA2-65	elimination of N-terminal domain, complete loss of ligase activity	-, 745788	
6.3.4.15	DELTA2-65	elimination of N-terminal domain, mutant shows normal ligase activity	-, 746268