EC Number   |
Protein Variants |
Reference |
|---|
   2.7.12.2 | C147S |
90% of wild-type activity |
760483 |
| 2.7.12.2 | C218S |
84% of wild-type activity, mutation drastically augments the protein production and crystallographic resolution. C218S crystals grown under microgravity in a space environment yield a 1.3 A resolution structure |
760483 |
| 2.7.12.2 | C218S/C276S |
40% of wild-type activity |
760483 |
| 2.7.12.2 | C218S/C276S/C147S |
40% of wild-type activity |
760483 |
| 2.7.12.2 | C218S/C276S/C147S/C296S |
20% of wild-type activity |
760483 |
| 2.7.12.2 | C276S |
98% of wild-type activity, mutation maintains the specific activity and increases the protein yield |
760483 |
| 2.7.12.2 | C296S |
79% of wild-type activity, mutation maintains the specific activity and increases the protein yield |
760483 |
| 2.7.12.2 | D208N |
mutation abolishes MAPKK activity |
491924 |
| 2.7.12.2 | K102R |
site-directed mutagenesis, kinase inactive mutant, but slight autophosphorylation activity, the mutant strain shows a phenotype with a proliferation defect after infection of human macrophages and no or delayed lesion development in mice |
666395 |
| 2.7.12.2 | K120R |
generation of kinase-negative mutants of both protein kinases SymRK and SIP2 by replacing the essential Lys residue with Arg at the ATP binding site. This Lys-to-Arg substitution (SymRK-PK-KR and SIP2-KR) abolishes the kinase activity completely, but does not affect the interaction between SymRK and SIP2 |
741156 |
