2.7.4.8	C3S/C5S	PSD-95aC3S/C5S mutant	700475	
2.7.4.8	D103N	active	642706	
2.7.4.8	D74A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	700079	
2.7.4.8	E101D	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	700079	
2.7.4.8	E72Q	no guanylate or adenylate kinase activity	642706	
2.7.4.8	E72Q/D103D	no active	642706	
2.7.4.8	G3A	decrease in Tm-value by 1.4°C as compared to wild-type enzyme. Decrease in catalytic efficiency (kcat/Km) by 14%	761496	
2.7.4.8	additional information	construction of mutant PSD-95 SH3-GK which contains a deleterious point mutation in the C-terminal SH3 domain	676138	
2.7.4.8	additional information	RNAi knockdown of the cytosolic enzyme, a v2 mutant is temperature-sensitive and develops chlorotic leaves at restrictive temperatures, the v2 mutation causes inhibition of chloroplast differentiation; in particular, it disrupts the chloroplast translation machinery during early leaf development	700744	
2.7.4.8	N103D	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	700079	
2.7.4.8	P564S/S631D	PSD-95 construct	662176	
2.7.4.8	R116Q	decrease in Tm-value by 1.8°C as compared to wild-type enzyme. Decrease in catalytic efficiency (kcat/Km) by 18%	761496	
2.7.4.8	R96H	decrease in Tm-value by 4°C as compared to wild-type enzyme. Increase in catalytic efficiency (kcat/Km) by 22%	761496	
2.7.4.8	S121F	decrease in Tm-value by 3.6°C as compared to wild-type enzyme. Decrease in catalytic efficiency (kcat/Km) by 25%	761496	
2.7.4.8	S186Y	decrease in Tm-value by 2.8°C as compared to wild-type enzyme. Decrease in catalytic efficiency (kcat/Km) by 7%	761496	
2.7.4.8	S2L	decrease in Tm-value by 1.9°C as compared to wild-type enzyme. Decrease in catalytic efficiency (kcat/Km) by 11%	761496	
2.7.4.8	S35N/V168F	the mutations significantly suppress enzyme catalytic activity	721551	
2.7.4.8	S35P	reduced activity	662176	
2.7.4.8	S35P	the conversed proline residue at this position among all GK domains, drastically impairs the GMP binding affinity and significantly reduces the guanylate kinase activity, functional transition of the enzyme guanylate kinase is induced by a single mutation leading to the functional transition of the enzyme from a phosphoryl transfer kinase into a phosphorprotein interaction domain, molecular dynamic and metadynamics simulations, overview. The serine to proline mutation can also lead to the misrecognition of GMP, explaining the catalytic inactivity of the mutant. The GK domain is in an open state in the S35P mutant	739667	
2.7.4.8	S35P/D101S	reduced activity	662176	
2.7.4.8	S80A	sluggish enzyme	642701	
2.7.4.8	V91M	decrease in Tm-value by 3°C as compared to wild-type enzyme. Decrease in catalytic efficiency (kcat/Km) by 14%	761496	
2.7.4.8	Y76F	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	700079	
2.7.4.8	Y78F	affinity for MgATP2- similar to wild type but affinity for GMP decreases by a factor of 12	642702