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Literature summary for 1.14.18.1 extracted from
- Role of the tertiary structure in the diphenol oxidase activity of Octopus vulgaris hemocyanin (2008), Arch. Biochem. Biophys., 471, 159-167.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | an increase, up to three orders of magnitude, of tyrosinase-like activity is observed when the cleaved Odd-like (cleavage site between the alpha and beta domains of the functional unit homologous to Odd, in the Octopus dofleini sequence) is incubated with L-DOPA in the presence of trifluoroethanol or hexafluoroisopropanol | Octopus vulgaris |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | hemocyanin is stabilized by the presence of Ca2+ ions in solution | Octopus vulgaris |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Octopus vulgaris | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-tyrosine + L-dopa + O2 | - |
Octopus vulgaris | L-dopa + dopaquinone + H2O | - |
? | |
| o-diphenol + O2 | low activity | Octopus vulgaris | o-quinone + H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| tyrosinase | - |
Octopus vulgaris |
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