EC Number |
Reaction |
Reference |
---|
1.15.1.1 | 2 superoxide + 2 H+ = O2 + H2O2 |
A metalloprotein. Enzymes from most eukaryotes contain both copper and zinc, those from mitochondria and most prokaryotes contain manganese or iron. ligand binding site and structure |
-, 438186, 438189, 438190 |
1.15.1.1 | 2 superoxide + 2 H+ = O2 + H2O2 |
active site is not conserved, differing from others of Mn-SOD and Fe-SOD |
438096 |
1.15.1.1 | 2 superoxide + 2 H+ = O2 + H2O2 |
active site, manganese-binding site and contact site between monomers |
-, 438096 |
1.15.1.1 | 2 superoxide + 2 H+ = O2 + H2O2 |
amino acid composition, comparison |
-, 438113, 438116, 438128, 438129, 438134, 438142, 438145, 438147, 438153, 438157, 438162, 438166, 438167, 438177, 438182, 438184 |
1.15.1.1 | 2 superoxide + 2 H+ = O2 + H2O2 |
amino acid sequence alignment and comparison |
-, 438096, 438141, 438171, 438173, 438179, 438187, 438188, 438189, 438190 |
1.15.1.1 | 2 superoxide + 2 H+ = O2 + H2O2 |
Cu2+-binding |
438123 |
1.15.1.1 | 2 superoxide + 2 H+ = O2 + H2O2 |
electrostatic guidance of anionic substrate to the active site, detailed overview. Generation of a model for electrostatic-mediated diffusion, and efficient binding of superoxide for catalysis |
745653 |
1.15.1.1 | 2 superoxide + 2 H+ = O2 + H2O2 |
mechanism |
-, 438096, 438097, 438122, 438125, 438126 |
1.15.1.1 | 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 |
675243 |
1.15.1.1 | 2 superoxide + 2 H+ = O2 + H2O2 |
the amino acid residues His46, His48, His63, His71, His80, and His120, and Asp83 in the active site are conserved as in other Cu/ZnSODs |
-, 690078 |