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Literature summary for 1.14.99.48 extracted from

  • Skaar, E.P.; Gaspar, A.H.; Schneewind, O.
    IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus (2004), J. Biol. Chem., 279, 436-443.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expresssion in Escherichia coli, cultures overexpressing isoforms IsdG or IsdI exhibit a bright yellow color Staphylococcus aureus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Staphylococcus aureus 5737
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
12500
-
x * 12500, recombinant His-tagged protein, SDS-PAGE Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment 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)

Renatured (Comment) 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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 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 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 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 Comment Organism
? x * 12500, recombinant His-tagged protein, SDS-PAGE Staphylococcus aureus

General Information

General Information Comment Organism
physiological function isoform IsdI complements the heme utilization deficiency of a Corynebacterium ulcerans heme oxygenase mutant Staphylococcus aureus