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Literature summary extracted from

  • Caranto, J.D.; Gebhardt, L.L.; MacGowan, C.E.; Limberger, R.J.; Kurtz, D.M.
    Treponema denticola superoxide reductase: in vivo role, in vitro reactivities, and a novel [Fe(Cys)(4)] site (2012), Biochemistry, 51, 5601-5610.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.15.1.2 overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Treponema denticola

Protein Variants

EC Number Protein Variants Comment Organism
1.15.1.2 additional information construction of inactive 1754M strain containing the insertionally inactivated Td SOR gene Treponema denticola

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.2 Fe2+ non-heme [Fe(His)4Cys] active sites Treponema denticola
1.15.1.2 additional information no other metal-binding domain besides the non-heme [Fe(His)4Cys] sites Treponema denticola

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ Treponema denticola
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ Treponema denticola 35405
-
 rubredoxin + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.2 Treponema denticola
-
-
-
1.15.1.2 Treponema denticola 35405
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.15.1.2 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by anion exchange and metal-chelate affinity chromatography Treponema denticola

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.2 reduced rubredoxin + superoxide + 2 H+
-
 Treponema denticola rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ with NADH Treponema denticola rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+
-
 Treponema denticola 35405 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ with NADH Treponema denticola 35405 rubredoxin + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.15.1.2 More homology structural modeling using the Tp SOR structure, PDB ID 1Y07, as template, overview Treponema denticola

Synonyms

EC Number Synonyms Comment Organism
1.15.1.2 SOR
-
 Treponema denticola

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.15.1.2 25 37 assay at Treponema denticola

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.15.1.2 7.3
-
 assay at Treponema denticola

Cofactor

EC Number Cofactor Comment Organism Structure
1.15.1.2 rubredoxin contains on-heme [Fe(His)4Cys] active sites. Enzymatic reduction of the enzyme iron sites with use of NADH:rubredoxin oxidoreductase and rubredoxin, both from Thermotoga maritima, rates of enzymatic reduction of the ferric center I and enzyme sites are measured Treponema denticola

General Information

EC Number General Information Comment Organism
1.15.1.2 malfunction the enzyme-inactivated 1754M strain is significantly more air-sensitive than the wild-type strain on NOS agarose plates exposed to air Treponema denticola
1.15.1.2 additional information the enzyme contains non-heme [Fe(His)4Cys] active sites, homology structural modeling using the Tp SOR structure, PDB ID 1Y07, as template, overview Treponema denticola
1.15.1.2 physiological function superoxide reductase from the air-sensitive oral spirochete Treponema denticola is a principal enzymatic scavenger of superoxide in this organism, role for the enzyme in oxidative stress protection of O2-exposed Treponema denticola 35405 Treponema denticola