EC Number   |
Protein Variants |
Reference |
|---|
  1.14.99.58 | more |
chromosomal knock-out gene bphO mutants shows identical growth behavior as the wild type under various conditions, the bphO mutant and the double mutant strain DELTAbphO show increased levels of pyocyanin, as well as decreased heat tolerance in the stationary phase, phenotypes, overview |
692400 |
| 1.14.99.58 | N19K |
no change in regioselectivity |
661923 |
| 1.14.99.58 | N19K/F117Y |
change in regioselectivity, producing alpha-biliverdin and less beta- and delta-biliverdin, enzyme exists as a mixture of molecules exhibiting 2 distinct heme seatings, one seating is identical to wild-type, the other is similar to that typical of alpha-hydroxylating heme oxigenases |
661923 |
| 1.14.99.58 | N19K/F117Y |
destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics |
678146 |
| 1.14.99.58 | N19K/F117Y/K132A |
destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics |
678146 |
| 1.14.99.58 | N19K/F117Y/K34N |
destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics |
678146 |
| 1.14.99.58 | N19K/K34A/F117Y/K132A |
the mutant produces biliverdin-IX-alpha |
742894 |
| 1.14.99.58 | R80L |
mutant exhibits allmost global conformational disorder related to significantly lower efficiency to hydroxylate heme in the presence of H2O2 |
680357 |
| 1.14.99.58 | T189W |
the heme degradation activity of the mutant is similar to that of the wild-type enzyme. The mutant produces only beta- and delta-biliverdins, but no alpha-biliverdin |
742737 |
