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Literature summary for 1.3.3.6 extracted from
- Three-dimensional structure of rat-liver acyl-CoA oxidase in complex with a fatty acid: insights into substrate-recognition and reactivity toward molecular oxygen (2006), J. Biochem., 139, 789-795.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli | Rattus norvegicus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| cocrystallization of ACO-II with lauroyl-CoA by the hanging-drop vapor-diffusion method under oil, to 2.07 A resolution | Rattus norvegicus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | P07872 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Rattus norvegicus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| lauroyl-CoA + O2 | binding mode of C12-fatty acid suggests that the active site does not close upon substrate binding, but remains spacious during the entire catalytic process, the oxygen accessibility in the oxidative half-reaction thereby being maintained | Rattus norvegicus | trans-2-dodecenoyl-CoA + H2O2 | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ACO-II | - |
Rattus norvegicus |
| acyl-CoA oxidase-II | - |
Rattus norvegicus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Rattus norvegicus | |
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Release 2023.1 (January 2023)
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