Galactose Oxidase has structural similarity to neuraminidase but its function and active site are very different. This preprint shows how a compact tetrahedral structure can be assembled from the X-ray crystal structure. This is the first protein reconstruction that confronts earlier physical measurements that suggest the native form is a monomer. The preprint therefore addresses the limitations of the earlier physical measurements.
Galactose oxidase is a copper enzyme with an aromatic electron-relay system connecting copper ions in adjacent subunits, thus allowing two-electron reduction of molecular oxygen. Apart from this novel feature the enzyme is similar to neuraminidases in having a channel from the active site to the enzyme exterior in order that substrate moieties can be oxidised while still part of a polysaccharide or glycoprotein.
Link here to the preprint.
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