EC Number   |
Protein Variants |
Reference |
|---|
    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 |
