General Stability | Organism |
---|---|
partially unfolding of the enzyme by 1.4 M guanidinium hydrochloride or 2.8 M urea | Cucurbita pepo |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | essential for activity, a tri-nuclear copper center structure, a partial loss of tertiary structure has strong effects on copper | Cucurbita pepo |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 L-ascorbic acid + O2 | Cucurbita pepo | - |
2 L-dehydroascorbic acid + 2 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cucurbita pepo | P37064 | green zucchini | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
4 L-ascorbate + O2 = 4 monodehydroascorbate + 2 H2O | the transition from native dimer to the dimeric intermediate is characterized by the release of copper ions forming the tri-nuclear copper center located at the interface between domain 2 and 3 of each subunit | Cucurbita pepo |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 L-ascorbic acid + O2 | - |
Cucurbita pepo | 2 L-dehydroascorbic acid + 2 H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | unfolding studies, pressure-induced and denaturing agents-induced dissociation and unfolding, and the role of dimerization in the folding strategy of a large protein, crystal structure analysis, physico-chemical properties of a molten dimer enzyme, three distinct domains per subunit, sharing a common beta-barrel topology, overview | Cucurbita pepo |
Synonyms | Comment | Organism |
---|---|---|
ascorbate oxidase | - |
Cucurbita pepo |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | - |
assay at | Cucurbita pepo |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
assay at | Cucurbita pepo |