1.14.99.58: heme oxygenase (biliverdin-IX-beta and delta-forming)
This is an abbreviated version!
For detailed information about heme oxygenase (biliverdin-IX-beta and delta-forming), go to the full flat file.
Reaction
Synonyms
biliverdin IXbeta/delta-selective heme oxygenase, BphO, heme-PigA heme oxygenase, heme-PigA(HO), HemO, PigA
ECTree
1.14.99.58 heme oxygenase (biliverdin-IX-beta and delta-forming)Advanced search results
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results (Engineering
Engineering on EC 1.14.99.58 - heme oxygenase (biliverdin-IX-beta and delta-forming)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F189A
-
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
F189G
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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
F189L
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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
F189T
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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
G125V
-
single-phase kinetics of transfer of heme from heme-binding protein PhuS
K132A
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the heme degradation activity of the mutant is similar to that of the wild-type enzyme, but the mutant produces 12% of alpha-biliverdin in addition to the formation of normal beta- (26%) and delta- (62%) biliverdins
K34A
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the heme degradation activity of the mutant is similar to that of the wild-type enzyme, but the mutant produces 11% of alpha-biliverdin in addition to the formation of normal beta- (34%) and delta- (55%) biliverdins
K34A/K132A
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the heme degradation activity of the mutant is similar to that of the wild-type enzyme, but the mutant produces 18% of alpha-biliverdin in addition to the formation of normal beta- (27%) and delta- (56%) biliverdins
N19K/F117Y
N19K/F117Y/K132A
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destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics
N19K/F117Y/K34N
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destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics
R80L
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mutant exhibits allmost global conformational disorder related to significantly lower efficiency to hydroxylate heme in the presence of H2O2
T189W
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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
additional information
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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
N19K/F117Y
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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
N19K/F117Y
-
destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics
