EC Number   |
Protein Variants |
Reference |
|---|
   3.1.99.B1 | C724A |
site-directed mutagenesis |
751635 |
| 3.1.99.B1 | D181A |
construction of a FEN1 mutant DELTA 336 truncated after residue 336 that bears an additional point mutation at residue 181. FEN1 DELTA336 removes only the flexible, protruding PCNA binding motif and encompasses the entire catalytic domain, and the active site D181A mutation severely retards incision. The DNA contains competing base pairing purine-pyrimidine pairs at the DNA junction, but the C-A mismatch favors 1 nt 3' flap formation |
717471 |
| 3.1.99.B1 | D201I/D204S |
site-directed mutagenesis, the overall reaction catalyzed by mutant D201I/D204S required two Mg2+ ions, in contrast to the wild-type enzyme that requires 3 Mg2+. D201I/D204S T5FENs is biphasic with respect to Ca2+ and ultimately dependent on 1/[Ca2+]2 |
717841 |
| 3.1.99.B1 | F278A |
the substitution of the aromatic residues with alanine leads to a large reduction in kcat value, although the mutants retains Km-value similar to that of the wild-type enzyme |
745273 |
| 3.1.99.B1 | F278A/F279A |
the kcat value of the mutant enzyme with the 5'-recess-end substrate and the the nick substrate is 10-20% of that of wild-type enzyme |
745273 |
| 3.1.99.B1 | F278A/F279A |
the kcat values of the mutant enzyme are decreased about 1020% with the 5'-recess-end substrate and the nick substrate |
719818 |
| 3.1.99.B1 | F278H/F279H |
kcat value decreases 83fold for the 5'-recess-end substrate and 150fold for the nick substrate compared with the wild-type values. 454fold decrease in kcat/Km for the 5'-recess-end substrate, 80fold decrease in kcat/Km for the nick substrate. The Km-value for the endo activity with the double flap substrate is increased 4fold, the kcat/Km-value is decreased 14fold, compared with the wild-type value |
719818 |
| 3.1.99.B1 | F278H/F279H |
the Km value for the 5'-recess-end substrate is elevated 5 times compared with the wild-type value whereas for the nick substrate the Km value of F278H/F279H is 60% the wild-type value |
719818 |
| 3.1.99.B1 | F278H/F279H |
the Km value for the 5'-recess-end substrate is elevated 5times compared with that of wild-type enzyme, for the nick substrate the Km value is 60% that of wild-type enzyme |
745273 |
| 3.1.99.B1 | F278L/F279L |
Km-values are lower than the wild-type values |
719818 |
