EC Number   |
Protein Variants |
Reference |
|---|
   2.7.7.8 | D625N |
naturally occuring mutation in the catalytic site, inactive mutant |
-, 723424 |
| 2.7.7.8 | DELTA549-709 |
complementation of growth defect at 15°C of host strain |
672449 |
| 2.7.7.8 | E331A |
loss of interaction with RNase Y. The Glu-331 side faces the helical domain of the RNase Y peptide |
-, 738702 |
| 2.7.7.8 | E371K |
complementation of growth defect at 15°C of host strain. Modest effect of mutation on phosphorolytic activity and protein abundance |
672449 |
| 2.7.7.8 | E371K |
ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.6, as compared with 1.0 in wild-type |
672449 |
| 2.7.7.8 | E81D |
complementation of growth defect at 15°C of host strain. Increase in PNPase abundance without significantly impairing phosphorolytic activity |
672449 |
| 2.7.7.8 | E81D |
impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 1.6, as compared with 1.0 in wild-type |
672449 |
| 2.7.7.8 | E81K |
complementation of growth defect at 15°C of host strain. Increase in PNPase abundance without significantly impairing phosphorolytic activity |
672449 |
| 2.7.7.8 | E81K |
impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.4, as compared with 1.0 in wild-type |
672449 |
| 2.7.7.8 | F635A |
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme |
722555 |
