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Literature summary for 1.1.3.9 extracted from

  • Weiner, R.E.; Ettinger, M.J.; Kosman, D.J.
    Fluorescence properties of the copper enzyme galactose oxidase and its tryptophan-modified derivates (1977), Biochemistry, 16, 1602-1606.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
N-bromosuccinimide complete inactivation by oxidation of active center tryptophan Hypomyces rosellus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Hypomyces rosellus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+
-
Hypomyces rosellus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-galactosylpyranoside + O2 Hypomyces rosellus
-
D-galacto-hexodialdose + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Hypomyces rosellus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
mycelium
-
Hypomyces rosellus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-O-methyl-beta-D-galactosylpyranoside + O2 one or more tryptophan residues, the Cu(II) atom and the sugar substrate interact within the native enzyme Hypomyces rosellus 1-O-methyl-beta-D-galacto-hexodialdose + H2O2
-
?
D-galactosylpyranoside + O2
-
Hypomyces rosellus D-galacto-hexodialdose + H2O2
-
?