EC Number |
Protein Variants |
Reference |
---|
2.4.1.90 | E317A |
when partially activated by Mn2+ binding to the primary site, can be further activated by Co2+ or inhibited by Ca2+, an effect that is the opposite of what is observed with the wild-type enzyme |
489556 |
2.4.1.90 | E317D |
when partially activated by Mn2+ binding to the primary site, can be further activated by Co2+ or inhibited by Ca2+, an effect that is the opposite of what is observed with the wild-type enzyme |
489556 |
2.4.1.90 | E317Q |
when partially activated by Mn2+ binding to the primary site, can be further activated by Co2+ or inhibited by Ca2+, an effect that is the opposite of what is observed with the wild-type enzyme |
489556 |
2.4.1.90 | H343A |
the mutant shows about 3% of wild type activity |
758173 |
2.4.1.90 | H347D |
in presence of Mn2+ retains 0.02% of wild-type enzyme activity, in presence of Co2+ retains 0.085% of wild-type enzyme activity |
489556 |
2.4.1.90 | H347E |
in presence of Mn2+ retains 0.1% of wild-type enzyme activity, in presence of Co2+ retains 0.4% of wild-type enzyme activity |
489556 |
2.4.1.90 | H347N |
in presence of Mn2+ retains 0.07% of wild-type enzyme activity, in presence of Co2+ retains 0.36% of wild-type enzyme activity |
489556 |
2.4.1.90 | H347Q |
in presence of Mn2+ retains 0.28% of wild-type enzyme activity, in presence of Co2+ retains 1.21% of wild-type enzyme activity |
489556 |
2.4.1.90 | I285Y |
site-directed mutagenesis, the mutation converts the betaGALNAcT1 enzyme into an efficient beta4Gal-T1, the N-acetylgalactosaminyltransferase activity is reduced by nearly 1000fold, while the galactosyltransferase activity is enhanced by 80fold |
675421 |
2.4.1.90 | M340E |
the mutant shows about 85% of wild type activity |
758173 |