| Description | This entry represents a β-propeller domain found in galactose oxidase and in Kelch repeat-containing proteins.The known functions of kelch-containing proteins are diverse: scruin is an actin cross-linking protein; galactose oxidase catalyses the oxidation of the hydroxyl group at the C6 position in D-galactose; neuraminidase hydrolyses sialic acid residues from glycoproteins; and kelch may have a cytoskeletal function, as it is localised to the actin-rich ring canals that connect the 15 nurse cells to the developing oocyte in Drosophila [ ]. Nevertheless, based on the location of the kelch pattern in the catalytic unit in galactose oxidase, functionally important residues have been predicted in glyoxal oxidase [].Galactose oxidase ( ) is a monomeric enzyme that contains a single copper ion and catalyses the stereospecific oxidation of primary alcohols to their corresponding aldehyde [ ]. The protein contains an unusual covalent thioether bond between a tyrosine and a cysteine that forms during its maturation []. Galactose oxidase is a three-domain protein: the N-terminal domain forms a jelly-roll sandwich, the central domain forms a seven 4-bladed β-propeller, and the C-terminal domain has an immunoglobulin-like fold. | Name | Galactose oxidase/kelch, beta-propeller |
| Short Name | Gal_Oxase/kelch_b-propeller | Type | Homologous_superfamily |
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