Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Almeida, R.M.; Turano, P.; Moura, I.; Moura, J.J.; Pauleta, S.R.
    Superoxide reductase: different interaction modes with its two redox partners (2013), ChemBioChem, 14, 1858-1866.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.15.1.2 expression in Escherichia coli strain BL21(DE3) Megalodesulfovibrio gigas

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.15.1.2 Zn-substituted rubredoxin generation of Zn-substituted rubredoxin, which is diamagnetic and redox inactive, titration of Zn-rubredoxin with superoxide reductase, overview Megalodesulfovibrio gigas

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.15.1.2 additional information
-
 additional information steady-state kinetics, overview Megalodesulfovibrio gigas

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.15.1.2 cytoplasm
-
 Megalodesulfovibrio gigas 5737
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.2 Fe2+ the class II enzyme has a single redox catalytic center consisting of an Fe atom bound to four nitrogen atoms from histidine side chains in the equatorial plane and to one cysteine sulfur in the axial plane Megalodesulfovibrio gigas
1.15.1.2 additional information ionic strength dependence of superoxide-mediated rubredoxin oxidation Megalodesulfovibrio gigas

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.15.1.2 29000
-
-
 Megalodesulfovibrio gigas

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.15.1.2 reduced desulforedoxin + superoxide + 2 H+ Megalodesulfovibrio gigas
-
 desulforedoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ Megalodesulfovibrio gigas
-
 rubredoxin + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.2 Megalodesulfovibrio gigas
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.15.1.2 recombinant enzyme from Escherichia coli strain BL21(DE3) by ultracentrifugation, anion exchange chromatography, and gel filtration Megalodesulfovibrio gigas

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.2 reduced desulforedoxin + superoxide + 2 H+
-
 Megalodesulfovibrio gigas desulforedoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+
-
 Megalodesulfovibrio gigas rubredoxin + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.15.1.2 homodimer
-
 Megalodesulfovibrio gigas

Synonyms

EC Number Synonyms Comment Organism
1.15.1.2 SOR
-
 Megalodesulfovibrio gigas

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.15.1.2 additional information
-
 ionic strength dependence of superoxide-mediated rubredoxin oxidation Megalodesulfovibrio gigas
1.15.1.2 7.6
-
 assay at Megalodesulfovibrio gigas

Cofactor

EC Number Cofactor Comment Organism Structure
1.15.1.2 desulforedoxin endogenous, contains Zn2+, the protein is able to transfer electrons to superoxide reductase with a maximum kapp of 31/min at an ionic strength of 57 mM, the enzyme complex with superoxide reductase is not detected by chemical shift perturbation Megalodesulfovibrio gigas
1.15.1.2 additional information titration of Zn-rubredoxin with superoxide reductase, overview. NMR competition assay between desulforedoxin and rubredoxin for binding to SOR, overview Megalodesulfovibrio gigas
1.15.1.2 rubredoxin endogenous. A monomeric, non-heme iron protein that contains a tetrahedral FeS4 metal center. The rubredoxin surface involved in the electron transfer complex with superoxide reductase comprises the solvent-exposed hydrophobic residues in the vicinity of its metal center, Cys9, Gly10, Cys42, Gly43, and Ala44. Kd of 0.003 mM at 59 mM ionic strength by NMR. Model structure of superoxide reductase-rubredoxin complex, overview Megalodesulfovibrio gigas

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.15.1.2 0.0004
-
 pH 7.6, temperature not specified in the publication Megalodesulfovibrio gigas Zn-substituted rubredoxin

General Information

EC Number General Information Comment Organism
1.15.1.2 evolution the enzyme belongs to the class II superoxide reductase family Megalodesulfovibrio gigas
1.15.1.2 additional information model structure of SOR-rubredoxin complex, docking simulations, overview Megalodesulfovibrio gigas