InterPro domain: IPR037293

This entry represents a beta-propeller domain found in galactose oxidase.

Galactose oxidase ( 1.1.3.9 ) is a monomeric enzyme that contains a single copper ion and catalyses the stereospecific oxidation of primary alcohols to their corresponding aldehyde [ 1 ]. The protein contains an unusual covalent thioether bond between a tyrosine and a cysteine that forms during its maturation [ 2 ]. Galactose oxidase is a three-domain protein: the N-terminal domain forms a jelly-roll sandwich, the central domain forms a seven 4-bladed beta-propeller, and the C-terminal domain has an immunoglobulin-like fold.

1. Crystal structure of the precursor of galactose oxidase: an unusual self-processing enzyme. Proc. Natl. Acad. Sci. U.S.A. 98, 12932-7
2. Galactose oxidase. Adv. Protein Chem. 60, 1-49