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Literature summary for 1.3.3.6 extracted from
- Purification of the peroxisomal fatty acyl-CoA oxidase from rat liver (1980), Biochem. Biophys. Res. Commun., 95, 7-12.
General Stability
| General Stability | Organism |
|---|---|
| stabilization with benzoate necessary for purification of the holoenzyme | Rattus norvegicus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| peroxisome | - |
Rattus norvegicus | 5777 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 22000 | - |
2 * 45000 + 2 * 22000, SDS-PAGE | Rattus norvegicus |
| 45000 | - |
2 * 45000 + 2 * 22000, SDS-PAGE | Rattus norvegicus |
| 136000 | - |
gel filtration | Rattus norvegicus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acyl-CoA + O2 | Rattus norvegicus | CoA derivatives of fatty acids with chain length from 8 to 18, first reaction of peroxisomal beta-oxidation, rate limiting for this process | trans-2,3-dehydroacyl-CoA + H2O2 | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| holo- and apoenzyme | Rattus norvegicus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Rattus norvegicus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 27.2 | - |
purified enzyme | Rattus norvegicus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acyl-CoA + O2 | - |
Rattus norvegicus | trans-2,3-dehydroacyl-CoA + H2O2 | - |
? | |
| acyl-CoA + O2 | CoA derivatives of fatty acids with chain length from 8 to 18, first reaction of peroxisomal beta-oxidation, rate limiting for this process | Rattus norvegicus | trans-2,3-dehydroacyl-CoA + H2O2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | 2 * 45000 + 2 * 22000, SDS-PAGE | Rattus norvegicus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | flavoprotein with noncovalently bound FAD | Rattus norvegicus | |
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Release 2023.1 (January 2023)
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