Any feedback?
Literature summary for 1.8.3.1 extracted from
- Sulfite oxidase activity of cytochrome c role of hydrogen peroxide (2016), Biochem. Biophys. Rep., 5, 96-104 .
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrial intermembrane space | - |
Homo sapiens | 5758 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe3+ | ferric cytochrome c, Fe3+ cyt c | Homo sapiens |  |
| Molybdenum | - |
Homo sapiens | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| sulfite + O2 + H2O | Homo sapiens | under normal physiological conditions, SO catalyzes the oxidation of sulfite to sulfate with cytochrome c (cyt c) as oxidizing substrate | sulfate + H2O2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P51687 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Homo sapiens | - |
| lung | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | mechanism of oxidation of sulfite and radical generation by ferric cytochrome c (Fe3+ cyt c) in the absence and presence of H2O2, oxidation of sulfite by the Fe3+ cyt c increased with sulfite concentration, overview | Homo sapiens | ? | - |
? | |
| sulfite + O2 + H2O | under normal physiological conditions, SO catalyzes the oxidation of sulfite to sulfate with cytochrome c (cyt c) as oxidizing substrate | Homo sapiens | sulfate + H2O2 | - |
? | |
| sulfite + O2 + H2O | usage of Fe3+ oxidized cytochrome c from horse heart | Homo sapiens | sulfate + H2O2 | - |
? | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| cytochrome c | ferric cytochrome c, Fe3+ cyt c, cytochrome c is known to participate in mitochondrial respiration and has antioxidant and peroxidase activities. Fe3+ cyt c might have a role in the deleterious effects of sulfite in biological systems due to increased production of sulfite radical. Mammalian cytochrome c (cyt c) is a small, globular protein that exists in high concentrations in the inner membrane of mitochondria | Homo sapiens | |
| molybdenum cofactor | - |
Homo sapiens | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | in humans, sulfite oxidase deficiency is one of the most accepted causes of sulfite hypersensitivity and toxicity. A congenital deficiency of sulfite oxidase can cause an excessive accumulation of sulfite and lead to early death in infancy (usually between 2 and 6 years of age), or in neonatal cases, neurological abnormalities, mental retardation, intractable seizures, and ocular lens dislocation. Molybdenum cofactor deficiency, which compromises sulfite oxidase activity, results in profound mental retardation, brain damage, microcephaly, and spasticity. It has also been suggested that hypoxic-ischemic encephalopathy is due to molybdenum cofactor deficiency | Homo sapiens |
| physiological function | sulfite is detoxified in the liver and lung to sulfate by sulfite oxidase (SO), a molybdenum dependent mitochondrial enzyme. The enzyme ensures that intracellular levels of the sulfite ion remain at acceptably low levels. Sulfite oxidation is the final step in the metabolism of sulfur derived from sulfur containing amino acids. SO catalyzes the oxidation of endogenous or exogenous sulfite to sulfate, which is excreted in to the urine | Homo sapiens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
