Abstract
Formylglycine-generating enzyme (FGE) is an O(2) -utilizing oxidase that converts specific cysteine residues of client proteins to formylglycine. We show that Cu(I) is an integral cofactor of this enzyme and binds with high affinity (K(D) =of 10(-17) m) to a pair of active-site cysteines. These findings establish FGE as a novel type of copper enzyme.