EC Number   |
Protein Variants |
Reference  |
|---|
   2.7.7.8 | A552T |
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 | A552T |
ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.7, as compared with 1.0 in wild-type |
672449 |
| 2.7.7.8 | DELTA549-709 |
complementation of growth defect at 15°C of host strain |
672449 |
| 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 | more |
deletion of KHS1 domain, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.6, as compared with 1.0 in wild-type. Deletion mutant lacking amino acids 549-709, no growth at 15°C. Both first and second core domains are involved in the catalysis of the phosphorolytic reaction, and both phosphorolytic activity and RNA binding are required for autogenous regulation and growth in the cold |
672449 |
