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Literature summary for 1.1.3.9 extracted from

  • Whittaker, J.W.
    The radical chemistry of galactose oxidase (2005), Arch. Biochem. Biophys., 433, 227-239.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
high level expression in Pichia pastoris Aspergillus sp.

KM Value [mM]

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

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

Organism UniProt Comment Textmining
Aspergillus sp.
-
-
-

Reaction

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 and Products (Substrate)

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

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, Tyr–Cys Aspergillus sp.