Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
copper | the oxidative activity of ascorbate oxidase is dominated by the highly selective substrate-binding affinity based on electrostatic interaction beyond the one-electron redox potential difference between type 1 copper site of ascorbate oxidase and substrate | Acremonium sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acremonium sp. | - |
HI-25 | - |
Acremonium sp. HI-25 | - |
HI-25 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the oxidative activity of ascorbate oxidase is dominated by the highly selective substrate-binding affinity based on electrostatic interaction beyond the one-electron redox potential difference between type 1 copper site of ascorbate oxidase and substrate | Acremonium sp. | ? | - |
? | |
additional information | the oxidative activity of ascorbate oxidase is dominated by the highly selective substrate-binding affinity based on electrostatic interaction beyond the one-electron redox potential difference between type 1 copper site of ascorbate oxidase and substrate | Acremonium sp. HI-25 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ASOM | - |
Acremonium sp. |