Cloned (Comment) | Organism |
---|---|
high level expression in Pichia pastoris | Aspergillus sp. |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics, isotope kinetics, kinetic analysis | Aspergillus sp. | |
3 | - |
O2 | - |
Aspergillus sp. | |
175 | - |
D-galactose | - |
Aspergillus sp. |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | metalloradical complex structure, overview, comprised of a protein radical coordinated to a copper ion in the active site, the coordination environment of the metal center is altered during redox and ligation changes in the active site | Aspergillus sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus sp. | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
D-galactose + O2 = D-galacto-hexodialdose + H2O2 | detailed reaction mechanism, the active site of galactose oxidase bears a Cu2+ with an inner coordination sphere involving Tyr272, Tyr495, His496, His581, and a coordinated solvent molecule, and Trp290 in the outer sphere of the complex, overview | Aspergillus sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
benzylalcohol + O2 | substrate reaction profiling | Aspergillus sp. | benzaldehyde + H2O2 | - |
? | |
D-galactose + O2 | - |
Aspergillus sp. | D-galacto-hexodialdose + H2O2 | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | mechanism of cofactor biogenesis, overview, metalloradical complex, comprised of a protein radical coordinated to a copper ion in the active site, the unusually stable protein radical is formed from the redox-active side chain of a cross-linked tyrosine residue, TyrCys | Aspergillus sp. |