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Literature summary for 1.1.3.9 extracted from

  • Rokhsana, D.; Howells, A.E.; Dooley, D.M.; Szilagyi, R.K.
    Role of the Tyr-Cys cross-link to the active site properties of galactose oxidase (2012), Inorg. Chem., 51, 3513-3524.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C228G the oxidized C228G mutant shows a higher reduction potential than the wild-type enzyme Hypomyces rosellus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Hypomyces rosellus
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-
-

Substrates and Products (Substrate)

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

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