Protein Variants | Comment | Organism |
---|---|---|
C228G | the oxidized C228G mutant shows a higher reduction potential than the wild-type enzyme | Hypomyces rosellus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-galactose + O2 | Hypomyces rosellus | - |
D-galacto-hexodialdose + H2O2 | - |
? | |
additional information | Hypomyces rosellus | the oxidized form of the enzyme catalyzes the two-electron oxidation of a broad range of primary alcohols to corresponding aldehydes with the concomitant reduction of O2 to H2O2 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Hypomyces rosellus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-galactose + O2 | - |
Hypomyces rosellus | D-galacto-hexodialdose + H2O2 | - |
? | |
additional information | the oxidized form of the enzyme catalyzes the two-electron oxidation of a broad range of primary alcohols to corresponding aldehydes with the concomitant reduction of O2 to H2O2 | Hypomyces rosellus | ? | - |
? |
General Information | Comment | Organism |
---|---|---|
additional information | the catalytically relevant, oxidized state of the active site of galactose oxidase is composed of antiferromagnetically coupled Cu(II) and a posttranslationally generated Tyr-Cys radical cofactor. The thioether bond of the Tyr-Cys cross-link affects the stability, the reduction potential, and the catalytic efficiency of the enzyme active site. Electronic and geometric structures of the metal center and the coordinated [Yยท-C] cofactor, computational modeling, overview. Significant difference in the spin density distribution of an isolated Tyr-Cys unit relative to its protein embedded form | Hypomyces rosellus |