EC Number   |
Protein Variants |
Reference |
|---|
   3.1.21.2 | E118A |
site-directed mutagenesis |
715906 |
| 3.1.21.2 | G149D |
site-directed mutagenesis, the mutant is deficient in both nucleotide incision repair and exonuclease activities |
-, 716298 |
| 3.1.21.2 | H508A |
catalytically inactive mutant |
-, 716663 |
| 3.1.21.2 | H69A |
site-directed mutagenesis, the mutant is deficient in both nucleotide incision repair and exonuclease activities. The crystal structure of Nfo-H69A mutant reveals the loss of one of the active site zinc atoms and rearrangements of the catalytic site, but no gross changes in the overall enzyme conformation |
-, 716298 |
| 3.1.21.2 | more |
analysis of enzyme activity in naturally occurring mutants of Escherichia coli compared to wild-type strain enzymes, overview |
665452 |
| 3.1.21.2 | S176N |
mutant enzyme retains cleavage activity (17.5% of that of wild-type Endo IV), but loses the polarized and restricted cleavage of a dCs tract. Escherichia coli cells expressing the intact Endo IV mutant enzyme are viable and, in contrast to wild-type Endo IV, the mutant enzyme does not show detrimental effect on the host cells |
682183 |
| 3.1.21.2 | W88R |
mutant enzyme shows no enzymatic activity (less than 0.4% of that of wild-type Endo IV). Escherichia coli cells expressing the intact Endo IV mutant enzyme are viable and, in contrast to wild-type Endo IV, these mutant enzymes do not show detrimental effect on the host cells |
682183 |
