Superoxide dismutase (Cu/Zn) / superoxide dismutase copper chaperone (IPR024134)

Short name: SOD_Cu/Zn_/chaperone

Overlapping homologous superfamilies

Family relationships


Superoxide dismutases (SODs) are ubiquitous metalloproteins that prevent damage by oxygen-mediated free radicals by catalysing the dismutation of superoxide into molecular oxygen and hydrogen peroxide [PMID: 2751312]. Superoxide is a normal by-product of aerobic respiration and is produced by a number of reactions, including oxidative phosphorylation and photosynthesis. The dismutase enzymes have a very high catalytic efficiency due to the attraction of superoxide to the ions bound at the active site [PMID: 1463506, PMID: 3891411].

There are three forms of superoxide dismutase, depending on the metal cofactor: Cu/Zn (which binds both copper and zinc), Fe and Mn types. The Fe and Mn forms are similar in their primary, secondary and tertiary structures, but are distinct from the Cu/Zn form [PMID: 2263641]. Prokaryotes and protists contain Mn, Fe or both types, while most eukaryotic organisms utilise the Cu/Zn type.

This entry represents the superoxide dismutase proteins as well as a related family of copper chaperones for superoxide dismutases. These cytosolic proteins deliver copper to Cu/Zn superoxide dismutases and are vital to their function [PMID: 10694572].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.