6.3.4.2	A20R	mutation disrupts cytoophidium assembly	744847	
6.3.4.2	C379A	mutant enzyme is fully active with ammonia but has no glutamine-dependent activity, no inhibition by glutamate gamma-semialdehyde	648963	
6.3.4.2	C404G	inactive	-, 745736	
6.3.4.2	D107A	enzyme exhibits wild-type NH3-dependent activity and affinity for glutamine, but impaired glutamine-dependent CTP formation, affinity of the mutant enzyme for GTP is reduced 2-4fold	648962	
6.3.4.2	D149E	the single point mutation in the resistant strain L2/CPEC results in loss of CTP feedback inhibition, cells are resistant to the cytotoxic effects of cyclopentenyl cytosine	-, 648995	
6.3.4.2	D70A	mutation in the ATP binding site, mutant exhibits approximately twofold increase in the number of cells containing filaments	-, 745736	
6.3.4.2	DELTA20	deletion of the N-terminal 20 amino acids alone is sufficient to disrupt cytoophidium assembly, mutant protein forms distinct cytoplasmic structures which appear as large clusters	744847	
6.3.4.2	E103A	mutant enzyme exhibits no glutamine-dependent activity and is only partially active with NH3	648962	
6.3.4.2	E146A	mutation in the ATP binding site, mutant exhibits approximately twofold increase in the number of cells containing filaments	-, 745736	
6.3.4.2	E161K	mutation in CTP binding site, filament formation is completely disrupted and the enzyme can only form foci. Mutation decreases the affinity of the enzyme for CTP	-, 745736