EC Number |
Protein Variants |
Reference |
---|
2.4.1.90 | M340H |
the mutant shows about 10% of wild type activity |
758173 |
2.4.1.90 | M344A |
in presence of Mn2+ retains 54.5% of wild-type enzyme activity, in presence of Co2+ retains 6.15% of wild-type enzyme activity |
489556 |
2.4.1.90 | M344A |
site-directed mutagenesis, altered metal ion specificity compared to the wild-type enzyme |
658032 |
2.4.1.90 | M344E |
site-directed mutagenesis, altered metal ion specificity compared to the wild-type enzyme |
658032 |
2.4.1.90 | M344H |
mutant prefers Mg2+ instead of Mn2+ which is preferred by the wild-type enzyme, with Mn2+ the mutant is arrested in the closed inactive conformation |
658502 |
2.4.1.90 | M344H |
site-directed mutagenesis, the mutant shows altered conformational changes upon binding of Mn2+ and substrates or substrate analogues compared to the wild-type enzyme, it forms the closed conformation with bound Mn2+ and UDP-hexanolamine, loss of 98% of Mn2+ binding activity, increased activity with Mg2+ |
658032 |
2.4.1.90 | M344Q |
in presence of Mn2+ retains 15.37% of wild-type enzyme activity, in presence of Co2+ retains 31.08% of wild-type enzyme activity |
489556 |
2.4.1.90 | M344Q |
site-directed mutagenesis, altered metal ion specificity compared to the wild-type enzyme |
658032 |
2.4.1.90 | M344S |
site-directed mutagenesis, altered metal ion specificity compared to the wild-type enzyme |
658032 |
2.4.1.90 | more |
a construct bearing the N-terminal peptides from bovine Cd1 (residues 143175 (P1)) fused with peptide with the Cd7DELTAC protein (last 11 amino acids deleted) shows no impact on the catalytic activity nor the folding efficiency. This construct is used for successful crystallization |
719863 |