Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | in both active and inactive forms, protein monomer integrity is lost with a single radiation interaction anywhere in the polypeptide, but enzymatic activity is more resistant, yielding target sizes considerably smaller than that of the monomer | Hypomyces rosellus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | essentially required, copper enzyme, removal of copper and free radicals inactivates the enzyme | Hypomyces rosellus | |
additional information | the monomeric enzyme containing a mononuclear copper ionis coordinated with an unusually stable cysteinyl-tyrosine protein free radical, removal of copper and free radicals inactivates the enzyme | Hypomyces rosellus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
68000 | - |
1 * 68000, SDS-PAGE | Hypomyces rosellus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-galactose + O2 | Hypomyces rosellus | - |
D-galacto-hexodialdose + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Hypomyces rosellus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
the enzyme from commercial preparation is further purified by gel filtration | Hypomyces rosellus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Hypomyces rosellus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-galactose + O2 | - |
Hypomyces rosellus | D-galacto-hexodialdose + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 68000, SDS-PAGE | Hypomyces rosellus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
assay at | Hypomyces rosellus |
General Information | Comment | Organism |
---|---|---|
additional information | the structure of galactose oxidase must make its catalytic activity unusually robust, permitting the enzymatic properties to survive in molecules following cleavage of the polymer chain | Hypomyces rosellus |