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 | C1310T |
mutation invovled in sRNA regulation defects |
-, 723757 |
2.7.7.8 | C277T |
mutation invovled in sRNA regulation defects |
-, 723757 |
2.7.7.8 | C943T |
mutation invovled in sRNA regulation defects |
-, 723757 |
2.7.7.8 | D135G |
unlike trimeric wild-type, mutant is monomeric. Almost complete inhibition of degradation and polyadenylation activities |
695109 |
2.7.7.8 | D323A |
weakening of interaction with RNase Y. Asp-323 sits near the C-terminal end of the RNase Y peptide sequence |
-, 738702 |
2.7.7.8 | D526A |
mutation of the full-length and S1-domain deletion PNPases does not affect manganese- or magnesisum-dependent binding to RNA |
737684 |
2.7.7.8 | D526A/D532A |
mutation of the full-length and S1-domain deletion PNPases does not affect manganese-or magnesium-dependent binding to RNA |
737684 |
2.7.7.8 | D544G |
decrease in degradation activity, increase in polymerization |
695109 |