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Literature summary extracted from

  • Li, W.; Wang, H.; Chen, Z.; Ye, Q.; Tian, Y.; Xu, X.; Huang, Z.; Li, P.; Tan, X.
    Probing the metal specificity mechanism of superoxide dismutase from human pathogen Clostridium difficile (2014), Chem. Commun. (Camb. ), 50, 584-586.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.1 Co2+ the Co ion can stably substitute the native cofactor Mn ion Clostridioides difficile
1.15.1.1 Fe cognate metal ions Mn, Fe, and Co can effectively occupy the metal site of superoxide dismutase, respectively. MnSOD exhibits the highest SOD activity of 8600 U/mg, while Fe-sub-MnSOD shows only 800 U/mg, and Co-sub-MnSOD does not have any detectable activity. Thermodynamic stability decreases in the order Co-sub-MnSOD, MnSOD, Fe-sub-MnSOD Clostridioides difficile
1.15.1.1 Fe2+ the Fe ion can stably substitute the native cofactor Mn ion Clostridioides difficile
1.15.1.1 Mn cognate metal ions Mn, Fe, and Co can effectively occupy the metal site of superoxide dismutase, respectively. MnSOD exhibits the highest SOD activity of 8600 U/mg, while Fe-sub-MnSOD shows only 800 U/mg, and Co-sub-MnSOD does not have any detectable activity. Thermodynamic stability decreases in the order Co-sub-MnSOD, MnSOD, Fe-sub-MnSOD Clostridioides difficile
1.15.1.1 Mn2+ the enzyme selectively chooses the Mn ion as its native cofactor, although Co and Fe ions can stably substitute the Mn ion Clostridioides difficile
1.15.1.1 additional information Co-sub-MnSOD does not have any detectable activity. Thermodynamic stability decreases in the order Co-sub-MnSOD, MnSOD, Fe-sub-MnSOD Clostridioides difficile
1.15.1.1 additional information the enzyme selectively chooses the Mn ion as its native cofactor, although Co and Fe ions can stably substitute the Mn ion. Molecular mechanism and structural basis of the metal specificity, preparation of Mn-superoxide dismutase, Fe-Mn-superoxide dismutase, and Co-Mn-superoxide dismutase, the cognate metal characters tuned by the metal microenvironment dominate the metal specificity of the enzyme, overview. The H-bond between Gln178 and Tyr64 in Mn-superoxide dismutase is stronger than that in Fe-Mn-superoxide dismutase, while the coupling between Gln178 and the coordinated solvent of Mn-superoxide dismutase is weaker than that of Fe-Mn-superoxide dismutase. In the oxidized Fe-Mn-superoxide dismutase, tight coupling between Gln178 and the coordination hydroxyl may reduce its redox potential and thus impact its catalytic activity Clostridioides difficile

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.15.1.1 2 O2.- + 2 H+ Clostridioides difficile
-
 O2 + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.1 Clostridioides difficile
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.15.1.1 800
-
 isoform FeSOD, pH not specified in the publication, temperature not specified in the publication Clostridioides difficile
1.15.1.1 8600
-
 isoform MnSOD, pH not specified in the publication, temperature not specified in the publication Clostridioides difficile

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.1 2 O2.- + 2 H+
-
 Clostridioides difficile O2 + H2O2
-
 ?

General Information

EC Number General Information Comment Organism
1.15.1.1 additional information molecular metal specificity mechanism of th enzyme, overview Clostridioides difficile