Reactome | SOD1 catalyzes 2H+ + 2O2.- => O2 + H2O2 (cytosol)

SOD1 catalyzes 2H+ + 2O2.- => O2 + H2O2 (cytosol)

Stable Identifier

R-HSA-3299691

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

SOD1 catalyzes 2H+ + 2O2.- => O2 + H2O2 (cytosol)

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Cu-Zn superoxide dismutase (SOD1), originally known as erythrocuprein, catalyzes the reaction of two molecules of superoxide (O2.-) to yield one molecule of hydrogen peroxide (H2O2) and one molecule of oxygen (O2) (McCord and Fridovich 1969 assayed both bovine and human Cu-Zn superoxide dismutase, the human sample provided by Carrico and Deutsch). Diffusion of hydrogen peroxide, the product of SOD1, across the cytosol is limited (Mishina et al. 2011)

Literature References

PubMed ID	Title	Journal	Year
20690882	Does cellular hydrogen peroxide diffuse or act locally? Markvicheva, KN, Lukyanov, S, Tyurin-Kuzmin, PA, Vorotnikov, AV, Schultz, C, Tkachuk, VA, Belousov, VV, Laketa, V, Mishina, NM	Antioxid. Redox Signal.	2011
5389100	Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein) Fridovich, I, McCord, JM	J. Biol. Chem.	1969
7021796	Purification of superoxide dismutases from human placenta using immunoadsorbent columns Hirano, K, Inoue, H, Ito, Y, Adachi, T, Sugiura, M	J. Pharmacobio-dyn.	1981
3532102	High-level expression of enzymatically active human Cu/Zn superoxide dismutase in Escherichia coli Yavin, Z, Gorecki, M, Bartfeld, D, Aviv, H, Kanner, D, Hartman, JR, Geller, T	Proc. Natl. Acad. Sci. U.S.A.	1986