EC Number   |
General Information |
Reference |
|---|
   1.1.3.9 | evolution |
galactose oxidase is a member of the radical copper oxidase family and is classified as a member of the carbohydrate active-enzyme family AA5, subfamiliy 2 |
-, 743642 |
| 1.1.3.9 | evolution |
galactose oxidases (GAOs) are classified as members of the auxiliary activity (AA) family AA5. This family includes copper radical oxidases and two subfamilies, AA5 1 and AA5 2, containing presently glyoxal oxidases and GAOs, respectively, which share similar tertiary structures and virtually identical active sites despite different catalytic specificities and low sequence similarity |
-, 743101 |
| 1.1.3.9 | evolution |
the enzyme belongs to the the galactose 6-oxidase/glyoxal oxidase family of mononuclear copper-radical oxidases, auxiliary activity family 5, AA5, subfamily 2, AA5_2. Structure-function analysis and comparison to other structurally related but catalytically inactive members of the family, from Colletotrichum graminicola and Colletotrichum gloeosporioides, CgrAlcOx and CglAlcOx, reveals catalytic diversity in the galactose oxidase and glyoxal oxidase family, overview. All AA5 sequences known to date contain the key active site residues of FgrGalOx, namely, C228 and Y272 |
743337 |
| 1.1.3.9 | malfunction |
deletion of domain 1 completely abolishes the enzyme activity and is thus speculated to be important also for the correct folding of domain 2 |
743101 |
| 1.1.3.9 | metabolism |
copper-containing complexes, namely (benzoato-kappa2O,O')[(E)-2-({[2-(diethylamino)ethyl]imino}methyl)phenolato-kappa3N,N',O]copper(II) dihydrate, [Cu(C7H5O2)(C13H19N2O)] 2H2O, [(E)-2-({[2-(diethylamino)-ethyl]imino}methyl)phenolato-kappa3N,N',O](2-phenylacetato-kappa2O,O')copper(II), [Cu-(C8H7O2)(C13H19N2O)], and bis[my-(E)-2-({[3-(diethylamino)propyl]imino}-methyl)phenolato]-kappa4N,N',O:O;kappa4O:N,N',O-(my-2-methylbenzoato-kappa2O:O')copper(II) perchlorate, [Cu2(C8H7O2)(C12H17N2O)2]ClO4, have been tested for their activity in the oxidation of D-galactose. The results suggest that, unlike the enzyme galactose oxidase, due to the precipitation of Cu2O, this reaction is not catalytic |
762565 |
| 1.1.3.9 | metabolism |
the indole ring, as an electron donor, stabilizes the phenoxyl radical by the pi-pi stacking interaction. A CuII complex of a methoxy-substituted salen-type ligand, containing a pendent indole ring on the dinitrogen chelate backbone exhibits the pi-pi stacking interaction of the indole ring mainly with one of the two phenolate moieties. The phenolate moiety in close contact with the indole moiety shows the characteristic phenoxyl radical structural features, indicating that the indole ring favors the pi-pi stacking interaction with the phenoxyl radical |
762926 |
| 1.1.3.9 | more |
active site structure, analysis of crystal structure PDB ID 1GOF, overview. Molecular modeling of the pre-processed Cu(I)-galactose oxidase active site and biogenesis reaction coordinate |
742748 |
| 1.1.3.9 | more |
enzyme active site structure analysis of immobilzed enzyme, overview. In the active site region, the Cu ion is coordinated to two tyrosines (Tyr272 and Tyr495), two histidines (H496 and H581), and a solvent ligand (water), forming the inner coordination sphere (a type 2 centre). Importantly, Tyr272 is covalently bonded to Cys228 via a thioether bond and its radical form (Tyrc272) serves as a catalytic cofactor (i.e. the second redox site). Trp290 stacks over the Cys228 side chain and plays an essential role in generating Tyrc272 radicals for maintaining the enzyme catalytic cycles. Three-dimensional structure analysis |
743780 |
| 1.1.3.9 | more |
GalOx is unusual among metalloenzymes in catalyzing a two-electron redox chemistry at a mononuclear metal ion active site |
-, 743642 |
| 1.1.3.9 | more |
influence of a family 29 carbohydrate binding module on the activity of galactose oxidase from Fusarium graminearum |
741991 |
