EC Number |
Protein Variants |
Reference |
---|
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 | 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/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 | H26A/K34A/K132A |
inactive |
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 | F117Y |
no change in regioselectivity |
661923 |
1.14.99.58 | N19K |
no change in regioselectivity |
661923 |
1.14.99.58 | G125V |
single-phase kinetics of transfer of heme from heme-binding protein PhuS |
678146 |