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Literature summary for 1.15.1.1 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
Search for more literature for 1.15.1.1

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ the Co ion can stably substitute the native cofactor Mn ion Clostridioides difficile
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
Fe2+ the Fe ion can stably substitute the native cofactor Mn ion Clostridioides difficile
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
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
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
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)

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

Organism

Organism UniProt Comment Textmining
Clostridioides difficile
-
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

General Information

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