BRENDA - Enzyme Database show
show all sequences of 1.14.99.48

IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus

Skaar, E.P.; Gaspar, A.H.; Schneewind, O.; J. Biol. Chem. 279, 436-443 (2004)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
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
Staphylococcus aureus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
;
Staphylococcus aureus
5737
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
12500
-
x * 12500, recombinant His-tagged protein, SDS-PAGE; x * 12500, recombinant His-tagged protein, SDS-PAGE
Staphylococcus aureus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
protoheme + 4 AH2 + 4 O2
Staphylococcus aureus
-
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
Staphylococcus aureus
-
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
Staphylococcus aureus N315
-
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
Staphylococcus aureus N315
-
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
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Staphylococcus aureus
Q7A649
isoform IsdG
-
Staphylococcus aureus
Q7A827
isoform IsdI
-
Staphylococcus aureus N315
Q7A649
isoform IsdG
-
Staphylococcus aureus N315
Q7A827
isoform IsdI
-
Renatured (Commentary)
Commentary
Organism
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
Staphylococcus aureus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
protoheme + 4 AH2 + 4 O2
-
725362
Staphylococcus aureus
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
-
725362
Staphylococcus aureus N315
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
-
725362
Staphylococcus aureus
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
-
725362
Staphylococcus aureus N315
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
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 12500, recombinant His-tagged protein, SDS-PAGE; x * 12500, recombinant His-tagged protein, SDS-PAGE
Staphylococcus aureus
Cloned(Commentary) (protein specific)
Commentary
Organism
expresssion in Escherichia coli, cultures overexpressing isoforms IsdG or IsdI exhibit a bright yellow color
Staphylococcus aureus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Staphylococcus aureus
5737
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
12500
-
x * 12500, recombinant His-tagged protein, SDS-PAGE
Staphylococcus aureus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
protoheme + 4 AH2 + 4 O2
Staphylococcus aureus
-
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
Staphylococcus aureus
-
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
Staphylococcus aureus N315
-
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
Staphylococcus aureus N315
-
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
-
?
Renatured (Commentary) (protein specific)
Commentary
Organism
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
Staphylococcus aureus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
protoheme + 4 AH2 + 4 O2
-
725362
Staphylococcus aureus
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
-
725362
Staphylococcus aureus N315
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
-
725362
Staphylococcus aureus
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
-
725362
Staphylococcus aureus N315
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
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 12500, recombinant His-tagged protein, SDS-PAGE
Staphylococcus aureus
General Information
General Information
Commentary
Organism
physiological function
isoform IsdI complements the heme utilization deficiency of a Corynebacterium ulcerans heme oxygenase mutant
Staphylococcus aureus
General Information (protein specific)
General Information
Commentary
Organism
physiological function
isoform IsdI complements the heme utilization deficiency of a Corynebacterium ulcerans heme oxygenase mutant
Staphylococcus aureus
Other publictions for EC 1.14.99.48
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
740954
Conger
Tight binding of heme to Staph ...
Staphylococcus aureus
Metallomics
9
556-563
2017
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3
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740760
Streit
Time-resolved studies of IsdG ...
Staphylococcus aureus, Staphylococcus aureus N315
J. Biol. Chem.
291
862-871
2016
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6
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6
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740768
Lockhart
Hydrogen bond donation to the ...
Staphylococcus aureus, Staphylococcus aureus MW2
J. Biol. Inorg. Chem.
20
757-770
2015
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1
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725532
Loutet
IruO is a reductase for heme d ...
Staphylococcus aureus, Staphylococcus aureus N315
J. Biol. Chem.
288
25749-25759
2013
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8
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12
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16
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8
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16
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1
2
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740058
Matsui
Heme degradation by Staphyloco ...
Staphylococcus aureus
Biochemistry
52
3025-3027
2013
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3
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740703
Ukpabi
Inactivation of the heme degra ...
Staphylococcus aureus, Staphylococcus aureus N315
J. Biol. Chem.
287
34179-34188
2012
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1
4
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6
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725264
Haley
Staphylococcus lugdunensis Isd ...
Staphylococcus lugdunensis, Staphylococcus lugdunensis N920143
J. Bacteriol.
193
4749-4757
2011
1
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2
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4
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1
1
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740051
Reniere
The flexible loop of Staphyloc ...
Staphylococcus aureus, Staphylococcus aureus Newman
Biochemistry
50
6730-6737
2011
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1
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2
2
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725997
Reniere
The IsdG-family of haem oxygen ...
Staphylococcus aureus, Staphylococcus aureus N315
Mol. Microbiol.
75
1529-1538
2010
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1
1
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12
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1
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1
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8
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725384
Lee
Ruffling of metalloporphyrins ...
Staphylococcus aureus
J. Biol. Chem.
283
30957-30963
2008
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1
1
1
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725994
Reniere
Staphylococcus aureus haem oxy ...
Staphylococcus aureus, Staphylococcus aureus N315
Mol. Microbiol.
69
1304-1315
2008
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12
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1
2
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725367
Wu
Staphylococcus aureus IsdG and ...
Staphylococcus aureus, Staphylococcus aureus ATCC 700699, Staphylococcus aureus MW2
J. Biol. Chem.
280
2840-2846
2005
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1
7
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725362
Skaar
IsdG and IsdI, heme-degrading ...
Staphylococcus aureus, Staphylococcus aureus N315
J. Biol. Chem.
279
436-443
2004
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1
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