Information on EC 1.14.99.48 - heme oxygenase (staphylobilin-producing)

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The expected taxonomic range for this enzyme is: Staphylococcus

EC NUMBER
COMMENTARY hide
1.14.99.48
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RECOMMENDED NAME
GeneOntology No.
heme oxygenase (staphylobilin-producing)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
protoheme + 5 reduced acceptor + 4 O2 = 15-oxo-beta-bilirubin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
show the reaction diagram
(2)
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protoheme + 5 reduced acceptor + 4 O2 = 5-oxo-delta-bilirubin + Fe2+ + formaldehyde + 5 acceptor + 4 H2O
show the reaction diagram
(1)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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heme degradation VI
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Porphyrin and chlorophyll metabolism
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform IsdI
UniProt
Manually annotated by BRENDA team
isoform IsdG
UniProt
Manually annotated by BRENDA team
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F8KHM5
UniProt
Manually annotated by BRENDA team
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F8KHM5
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
protoheme + 4 AH2 + 4 O2
15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
show the reaction diagram
protoheme + 4 AH2 + 4 O2
5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
protoheme + 4 AH2 + 4 O2
15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
show the reaction diagram
protoheme + 4 AH2 + 4 O2
5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
show the reaction diagram
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12500
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x * 12500, recombinant His-tagged protein, SDS-PAGE; x * 12500, recombinant His-tagged protein, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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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
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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
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 hide
LITERATURE
F23A
mutation does not significantly affect heme binding or degradation
H77A
mutation abolishes IsdG-mediated heme 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
S70A
mutation does not significantly affect heme binding or degradation
W67A
mutation abolishes IsdG-mediated heme degradation
H77A
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mutation abolishes IsdG-mediated heme degradation
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L17A
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mutation does not significantly affect heme binding or degradation
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N7A
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mutation abolishes IsdG-mediated heme degradation
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S70A
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mutation does not significantly affect heme binding or degradation
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W67A
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mutation abolishes IsdG-mediated heme 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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