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Enzyme Nomenclature
Information on EC 1.14.99.48 - heme oxygenase (staphylobilin-producing)
Word Map on EC 1.14.99.48
- 1.14.99.48
- ho
- glutathione-s-transferase
-
gonad
- cobalt
-
mussels
-
trophic
-
eastern
-
wastewaters
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The expected taxonomic range for this enzyme is: Staphylococcus
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EC NUMBER 
COMMENTARY 
1.14.99.48
-
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RECOMMENDED NAME
GeneOntology No.
heme oxygenase (staphylobilin-producing)
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protoheme + 5 reduced acceptor + 4 O2 = 15-oxo-beta-bilirubin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
(2)
-
-
-
protoheme + 5 reduced acceptor + 4 O2 = 5-oxo-delta-bilirubin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
(1)
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
protoheme,hydrogen-donor:oxygen oxidoreductase (delta/beta-methene-oxidizing, hydroxylating)
This enzyme, which is found in pathogenic bacteria, is involved in an iron acquisition system that catabolizes the host's hemoglobin. The two enzymes from the bacterium Staphylococcus aureus, encoded by the isdG and isdI genes, produce 67.5 % and 56.2 % 5-oxo-delta-bilirubin, respectively.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
F8KHM5
isoform IsdG-mediated heme catabolism enables the use of heme as a sole source of iron
physiological function
-
isoform IsdI complements the heme utilization deficiency of a Corynebacterium ulcerans heme oxygenase mutant
physiological function
-
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; 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
physiological function
-
isoforms IsdG and IsdI are both important for Staphylococcus aureus growth on haemin as a sole iron source and are necessary for full Staphylococcus aureus pathogenesis. Strains lacking IsdG, IsdI or both exhibit significantly impaired growth on hemin as a sole iron source when compared with wild-type. Inactivation of IsdG and IsdI in combination does not enhance the hemin utilization defect over that of either individual mutant strain. Overexpression of either IsdG or IsdI complements the loss of both enzymes, and expression of IsdG and IsdI is regulated by iron in a Fur-dependent manner and differentially regulated by iron and hemin; isoforms IsdG and IsdI are both important for Staphylococcus aureus growth on haemin as a sole iron source and are necessary for full Staphylococcus aureus pathogenesis. Strains lacking IsdG, IsdI or both exhibit significantly impaired growth on hemin as a sole iron source when compared with wild-type. Inactivation of IsdG and IsdI in combination does not enhance the hemin utilization defect over that of either individual mutant strain. Overexpression of either IsdG or IsdI complements the loss of both enzymes, and expression of IsdG and IsdI is regulated by iron in a Fur-dependent manner and differentially regulated by iron and hemin. Hemin-dependent upregulation of IsdG is occurring post-transcriptionally by enhancing its protein stability
physiological function
-
isoform IsdI complements the heme utilization deficiency of a Corynebacterium ulcerans heme oxygenase mutant; isoforms IsdG and IsdI are both important for Staphylococcus aureus growth on haemin as a sole iron source and are necessary for full Staphylococcus aureus pathogenesis. Strains lacking IsdG, IsdI or both exhibit significantly impaired growth on hemin as a sole iron source when compared with wild-type. Inactivation of IsdG and IsdI in combination does not enhance the hemin utilization defect over that of either individual mutant strain. Overexpression of either IsdG or IsdI complements the loss of both enzymes, and expression of IsdG and IsdI is regulated by iron in a Fur-dependent manner and differentially regulated by iron and hemin; isoforms IsdG and IsdI are both important for Staphylococcus aureus growth on haemin as a sole iron source and are necessary for full Staphylococcus aureus pathogenesis. Strains lacking IsdG, IsdI or both exhibit significantly impaired growth on hemin as a sole iron source when compared with wild-type. Inactivation of IsdG and IsdI in combination does not enhance the hemin utilization defect over that of either individual mutant strain. Overexpression of either IsdG or IsdI complements the loss of both enzymes, and expression of IsdG and IsdI is regulated by iron in a Fur-dependent manner and differentially regulated by iron and hemin. Hemin-dependent upregulation of IsdG is occurring post-transcriptionally by enhancing its protein stability; 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; 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
-
physiological function
-
isoform IsdG-mediated heme catabolism enables the use of heme as a sole source of iron
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 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, 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, 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, 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
F8KHM5
-
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
F8KHM5
-
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
-
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, 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, 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, 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
F8KHM5
-
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
F8KHM5
-
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
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
protoheme + 4 AH2 + 4 O2
15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
Q7A649, Q7A827
-
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, 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
-
-
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
Q7A649, Q7A827
-
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, 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
Q7A649, Q7A827
-
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, 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
-
-
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
Q7A649, Q7A827
-
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, 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
-
?
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Iron
F8KHM5
isoform IsdG is most abundant under iron-depleted conditions. The presence of heme has no effect on the intracellular abundance of IsdG
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12500
-
x * 12500, recombinant His-tagged protein, SDS-PAGE; x * 12500, recombinant His-tagged protein, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 12500, recombinant His-tagged protein, SDS-PAGE; x * 12500, recombinant His-tagged protein, SDS-PAGE
?
-
x * 12500, recombinant His-tagged protein, SDS-PAGE; x * 12500, recombinant His-tagged protein, SDS-PAGE
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
inactive N7A variant of IsdG in complex with Fe3+-protoporphyrin IX, to 1.8 A resolution. The metalloporphyrin is buried into a deep clefts such that the propionic acid forms salt bridges to two Arg residues. His77, a critical residue required for activity, is coordinated to the Fe3+ atom. The bound porphyrin ring forms extensive steric interactions in the binding cleft such that the ring is highly distorted from the plane. This distortion is best described as ruffled and places the beta- and delta-meso carbons proximal to the distal oxygen-binding site. In the IsdG-hemin structure, Fe3+ is pentacoordinate, and the distal side is occluded by the side chain of Ile55; isoform IsdI in complex with cobalt protoporphyrin IX, to 1.8 A resolution. The metalloporphyrin is buried into a deep cleft such that the propionic acid forms salt bridges to two Arg residues. His76, a critical residue required for activity, is coordinated to the Co3+ atom. The bound porphyrin ring forms extensive steric interactions in the binding cleft such that the ring is highly distorted from the plane. This distortion is best described as ruffled and places the beta- and delta-meso carbons proximal to the distal oxygen-binding site. in the structure of IsdI-cobalt protoporphyrin IX, the distal side of the cobalt protoporphyrin IX accommodates a chloride ion in a cavity formed through a conformational change in Ile55. The chloride ion participates in a hydrogen bond to the side chain amide of Asn6
-
isoform IsdI in complex with heme, heme ruffling and constrained binding of oxygen is consistent with cleavage of the porphyrin ring at the beta- or delta-meso carbon atoms
-
to 1.5 A resolution. Structure of the enzyme resembles the ferredoxin-like fold and forms a beta-barrel at the dimer interface. Two large pockets found on the outside of the barrel contain the putative active sites; to 1.5 A resolution. Structure of the enzyme resembles the ferredoxin-like fold and forms a beta-barrel at the dimer interface. Two large pockets found on the outside of the barrel contain the putative active sites
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expresssion in Escherichia coli, cultures overexpressing isoforms IsdG or IsdI exhibit a bright yellow color; expresssion in Escherichia coli, cultures overexpressing isoforms IsdG or IsdI exhibit a bright yellow color
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F23A
mutation does not significantly affect heme binding or degradation
L17A
mutation does not significantly affect heme binding or degradation
M38A
slight reduction of heme degradation, mutation shifts the peak absorbance of the Soret band to 430 nm
N7A
S70A
mutation does not significantly affect heme binding or degradation
L17A
-
mutation does not significantly affect heme binding or degradation
-
S70A
-
mutation does not significantly affect heme binding or degradation
-
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reconstitution of both isoform IsdG and IsdI with heme at pH 8.0 generates optical absorption spectra containing a Soret band at about 412 nm, and alpha/beta bands at about 567 and 532 nm; reconstitution of both isoform IsdG and IsdI with heme at pH 8.0 generates optical absorption spectra containing a Soret band at about 412 nm, and alpha/beta bands at about 567 and 532 nm
-
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.99.48)
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