EC Number   |
Protein Variants |
Reference |
|---|
   2.4.99.18 | A162R |
no obvious growth defect or staurosporine sensitivity |
659293 |
| 2.4.99.18 | D166A |
lethal phenotype |
659293 |
| 2.4.99.18 | D167A |
lethal phenotype |
659293 |
| 2.4.99.18 | D47E |
mutant does not support glycosylation in vivo |
708611 |
| 2.4.99.18 | D518E |
the four mutant STT3s forms a stable Oligosaccharyl transferase complex that has seriously impaired Oligosaccharyl transferase activity |
686393 |
| 2.4.99.18 | D518E |
the replacement of a key residue, Asp518, located within the WWDYG signature motif (residues 516-520), leads to a distinct tertiary structure, even though both proteins have similar overall secondary structures, as demonstrated by CD, fluorescence and NMR spectroscopies. Asp518 plays a critical structural role, in addition to the catalytic role. The activity of the protein is confirmed by saturation transfer difference and nuclear magnetic resonance titration studies |
707520 |
| 2.4.99.18 | D518E |
within WWDYG signature motif leads to distinct tertiary structure interfering with function (complete loss of N-linked glycosylation activity), lethal |
707520 |
| 2.4.99.18 | D520A |
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant cannot be expressed in Escherichia coli |
-, 718929 |
| 2.4.99.18 | D520N |
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme |
-, 718929 |
| 2.4.99.18 | D526A |
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant cannot be expressed in Escherichia coli |
-, 718929 |
