Crystallographic Trapping of a Precatalytic Enzyme Complex Provides New Insight Into Dioxygen Activation at a Mononuclear Copper Center

摘要

To characterize the ternary complex of the enzyme peptidylglycine alpha-hydroxylating monooxygenase with oxygen and substrate by X-ray crystallography.Peptidylglycine alpha-hydroxylating monooxygenase (PHM) is one component of the bifunctional enzyme peptidylglycine alpha-amidating monooxygenase (PAM),which amidates the C-terminus of peptide hormones,neuro-peptides,and antimicrobials.In the first step of the PAM reaction,PHM hydroxylates the Calpha atom of a terminal glycine residue (Scheme 1).