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Literature summary for 1.15.1.1 extracted from

  • Jiang, W.; Han, Y.; Pan, Q.; Shen, T.; Liu, C.
    Roles of exogenous divalent metals in the nucleolytic activity of Cu,Zn superoxide dismutase (2007), J. Inorg. Biochem., 101, 667-677.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions Bos taurus
Mg2+ study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions Bos taurus
Mn2+ study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
commercial preparation
-

Reaction

Reaction Comment Organism Reaction ID
2 superoxide + 2 H+ = O2 + H2O2 presence of a general acid and a general base in catalysis. Catalytic model requires histidine residues, metal-bound water molecules and two hydrated metal ions to operate in concert Bos taurus