1.14.99.48: heme oxygenase (staphylobilin-producing)
This is an abbreviated version!
For detailed information about heme oxygenase (staphylobilin-producing), go to the full flat file.
Word Map on EC 1.14.99.48
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1.14.99.48
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glutathione-s-transferase
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trophic
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eastern
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wastewaters
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mussels
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gonad
- 1.14.99.48
- glutathione-s-transferase
-
trophic
-
eastern
-
wastewaters
-
mussels
-
gonad
Reaction
+ 5 reduced acceptor + 4 O2 = + + + 5 acceptor + 4 H2O
Synonyms
haem oxidase, haem oxygenase, heme oxidase, heme oxygenase, heme oxygenase (decyclizing), heme oxygenase (staphylobilin-producing) 1, heme oxygenase (staphylobilin-producing) 2, isdG, isdI
ECTree
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Substrates Products
Substrates Products on EC 1.14.99.48 - heme oxygenase (staphylobilin-producing)
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REACTION DIAGRAM
protoheme + 5 reduced acceptor + 4 O2
15-oxo-beta-bilirubin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
protoheme + 5 reduced acceptor + 4 O2
5-oxo-delta-bilirubin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
enzyme cleaves the tetrapyrrol ring structure of heme in the presence of NADPH cytochrome P450 reductase, thereby releasing iron
-
?
protoheme + 4 AH2 + 4 O2
15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
oxidoreductase IruO, gene name NWMN2274, is the likely in vivo reductant required for heme degradation by Staphylococcus aureus. In the presence of NADPH and IruO, either IsdI or IsdG degrade bound heme 10fold more rapidly than with the chemical reductant ascorbic acid. The major heme degradation products are 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin, i.e. staphylobilins
-
?
protoheme + 4 AH2 + 4 O2
15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
oxidoreductase IruO, gene name thatNWMN2274, is the likely in vivo reductant required for heme degradation by Staphylococcus aureus. In the presence of NADPH and IruO, either IsdI or IsdG degrade bound heme 10fold more rapidly than with the chemical reductant ascorbic acid. The major heme degradation products are 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin, i.e. staphylobilins
-
?
protoheme + 4 AH2 + 4 O2
15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
product is a red-orange solid that becomes yellow when dissolved in dimethyl sulfoxide or water/acetonitrile. It is more polar than biliverdin and bilirubin
-
?
protoheme + 4 AH2 + 4 O2
15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
in the presence of NADPH and IruO, either IsdI or IsdG degrade bound heme 10fold more rapidly than with the chemical reductant ascorbic acid. The major heme degradation products are 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin, i.e. staphylobilins
-
?
protoheme + 4 AH2 + 4 O2
15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
product is a red-orange solid that becomes yellow when dissolved in dimethyl sulfoxide or water/acetonitrile. It is more polar than biliverdin and bilirubin
-
?
protoheme + 4 AH2 + 4 O2
15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
enzyme cleaves the tetrapyrrol ring structure of heme in the presence of NADPH cytochrome P450 reductase, thereby releasing iron
-
?
protoheme + 4 AH2 + 4 O2
15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
oxidoreductase IruO, gene name thatNWMN2274, is the likely in vivo reductant required for heme degradation by Staphylococcus aureus. In the presence of NADPH and IruO, either IsdI or IsdG degrade bound heme 10fold more rapidly than with the chemical reductant ascorbic acid. The major heme degradation products are 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin, i.e. staphylobilins
-
?
protoheme + 4 AH2 + 4 O2
15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
in the presence of NADPH and IruO, either IsdI or IsdG degrade bound heme 10fold more rapidly than with the chemical reductant ascorbic acid. The major heme degradation products are 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin, i.e. staphylobilins
-
?
protoheme + 4 AH2 + 4 O2
15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
oxidoreductase IruO, gene name NWMN2274, is the likely in vivo reductant required for heme degradation by Staphylococcus aureus. In the presence of NADPH and IruO, either IsdI or IsdG degrade bound heme 10fold more rapidly than with the chemical reductant ascorbic acid. The major heme degradation products are 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin, i.e. staphylobilins
-
?
protoheme + 4 AH2 + 4 O2
15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
heme degradation by IsdG results in the release of free iron and the production of the chromophore staphylobilin, i.e. 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin
-
?
protoheme + 4 AH2 + 4 O2
15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
heme degradation by IsdG results in the release of free iron and the production of the chromophore staphylobilin, i.e. 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin
-
?
5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
enzyme cleaves the tetrapyrrol ring structure of heme in the presence of NADPH cytochrome P450 reductase, thereby releasing iron
-
?
protoheme + 4 AH2 + 4 O2
5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
oxidoreductase IruO, gene name NWMN2274, is the likely in vivo reductant required for heme degradation by Staphylococcus aureus. In the presence of NADPH and IruO, either IsdI or IsdG degrade bound heme 10fold more rapidly than with the chemical reductant ascorbic acid. The major heme degradation products are 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin, i.e. staphylobilins
-
?
protoheme + 4 AH2 + 4 O2
5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
oxidoreductase IruO, gene name thatNWMN2274, is the likely in vivo reductant required for heme degradation by Staphylococcus aureus. In the presence of NADPH and IruO, either IsdI or IsdG degrade bound heme 10fold more rapidly than with the chemical reductant ascorbic acid. The major heme degradation products are 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin, i.e. staphylobilins
-
?
protoheme + 4 AH2 + 4 O2
5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
product is a red-orange solid that becomes yellow when dissolved in dimethyl sulfoxide or water/acetonitrile. It is more polar than biliverdin and bilirubin
-
?
protoheme + 4 AH2 + 4 O2
5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
in the presence of NADPH and IruO, either IsdI or IsdG degrade bound heme 10fold more rapidly than with the chemical reductant ascorbic acid. The major heme degradation products are 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin, i.e. staphylobilins
-
?
protoheme + 4 AH2 + 4 O2
5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
product is a red-orange solid that becomes yellow when dissolved in dimethyl sulfoxide or water/acetonitrile. It is more polar than biliverdin and bilirubin
-
?
protoheme + 4 AH2 + 4 O2
5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
enzyme cleaves the tetrapyrrol ring structure of heme in the presence of NADPH cytochrome P450 reductase, thereby releasing iron
-
?
protoheme + 4 AH2 + 4 O2
5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
oxidoreductase IruO, gene name thatNWMN2274, is the likely in vivo reductant required for heme degradation by Staphylococcus aureus. In the presence of NADPH and IruO, either IsdI or IsdG degrade bound heme 10fold more rapidly than with the chemical reductant ascorbic acid. The major heme degradation products are 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin, i.e. staphylobilins
-
?
protoheme + 4 AH2 + 4 O2
5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
in the presence of NADPH and IruO, either IsdI or IsdG degrade bound heme 10fold more rapidly than with the chemical reductant ascorbic acid. The major heme degradation products are 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin, i.e. staphylobilins
-
?
protoheme + 4 AH2 + 4 O2
5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
oxidoreductase IruO, gene name NWMN2274, is the likely in vivo reductant required for heme degradation by Staphylococcus aureus. In the presence of NADPH and IruO, either IsdI or IsdG degrade bound heme 10fold more rapidly than with the chemical reductant ascorbic acid. The major heme degradation products are 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin, i.e. staphylobilins
-
?
protoheme + 4 AH2 + 4 O2
5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
heme degradation by IsdG results in the release of free iron and the production of the chromophore staphylobilin, i.e. 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin
-
?
protoheme + 4 AH2 + 4 O2
5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
-
heme degradation by IsdG results in the release of free iron and the production of the chromophore staphylobilin, i.e. 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin
-
?
15-oxo-beta-bilirubin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
-
-
-
-
?
protoheme + 5 reduced acceptor + 4 O2
15-oxo-beta-bilirubin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
-
-
-
?
protoheme + 5 reduced acceptor + 4 O2
15-oxo-beta-bilirubin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
-
-
-
?
5-oxo-delta-bilirubin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
-
-
-
-
?
protoheme + 5 reduced acceptor + 4 O2
5-oxo-delta-bilirubin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
-
-
-
?
protoheme + 5 reduced acceptor + 4 O2
5-oxo-delta-bilirubin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
-
-
-
?
?
-
an apparent meso-hydroxyheme is a likely common intermediate with the canonical heme oxygenases. Unlike heme oxygenases, this intermediate does not form with added H2O2 nor does it convert to verdoheme and CO. Rather, the next intermediates are a set of formyloxobilin isomers. These convert in separate fast and slow phases to beta-/delta-staphylobilin isomers and formaldehyde
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-
?
additional information
?
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dissociation equilibrium constants of heme are 1.4 nM and 12.9 nM for isoforms IsdG and IsdI, respectively. Heme dissociation rate constants are 0.022 per s for IsdG and 0.092 per s for IsdI. It is proposed that only IsdG is a member of the heme iron acquisition pathway and IsdI regulates heme homeostasis
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?
additional information
?
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the primary C1 product of the both isoform IsdG and IsdH is formaldehyde. In the mechanism, one meso carbon atom of the porphyrin ring is liberated primarily as formaldehyde
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-
?
additional information
?
-
an apparent meso-hydroxyheme is a likely common intermediate with the canonical heme oxygenases. Unlike heme oxygenases, this intermediate does not form with added H2O2 nor does it convert to verdoheme and CO. Rather, the next intermediates are a set of formyloxobilin isomers. These convert in separate fast and slow phases to beta-/delta-staphylobilin isomers and formaldehyde
-
-
?