EC Number   |
Protein Variants |
Reference |
|---|
    2.7.4.6 | A117D |
complete loss of nucleoside diphosphate kinase activity, but no loss of nuclease activity |
673695 |
| 2.7.4.6 | A134E |
site-directed mutagenesis, the mutant forms a dimer in analogy to the wild-type enzyme of Halomonas sp., which possesses an E134 residue, overview |
692339 |
| 2.7.4.6 | A134E/A135E |
site-directed mutagenesis, the mutant shows decreased oligomerization compared to the wild-type enzyme |
695007 |
| 2.7.4.6 | A77T |
site-directed mutagenesis, the mutant shows an altered import behaviour into chloroplasts compared to the wild-type enzyme, overview |
675668 |
| 2.7.4.6 | C139S |
site-directed mutagenesis, the mutation in the dimeric nucleoside diphosphate kinase generates a catalytically competent enzyme monomer |
738396 |
| 2.7.4.6 | C139S |
site-directed mutagenesis, the mutation in the dimeric nucleoside diphosphate kinase generates a catalytically competent enzyme monomer. Substitution of Cys139 for Ser causes dissociation of dimeric CsNDK into monomer in Tris buffer, and the mutant CsNDK becomes more susceptible to endproteinase GluC cleavage, which is suppressed by an NDK substrate, ATP |
-, 738396 |
| 2.7.4.6 | C139S |
the mutant forms a dimer |
-, 722131 |
| 2.7.4.6 | D112S |
the mutant shows reduced specific activity compared to the wild type enzyme |
722401 |
| 2.7.4.6 | D135A/E136T |
site-directed mutagenesis |
-, 739593 |
| 2.7.4.6 | D148C |
the mutation enhances stability and folding in low salt solution by S-S bond. The mutant shows increased thermal stability by about 10°C in 0.2 M NaCl over the wild type enzyme |
721435 |
