Information on EC - peptidylglycine monooxygenase

for references in articles please use BRENDA:EC1.14.17.3
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IUBMB Comments
A copper protein. The enzyme binds two copper ions with distinct roles during catalysis. Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme. The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide, a reaction catalysed by EC peptidylamidoglycolate lyase. In mammals, the two activities are part of a bifunctional protein. Involved in the final step of biosynthesis of alpha-melanotropin and related biologically active peptides.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
peptidylglycine alpha-hydroxylating monooxygenase, bifunctional pam, peptidylglycine monooxygenase, peptidyl-glycine alpha-amidating monooxygenase, alpha-ae, phmcc, peptidylglycine alpha-amidating mono-oxygenase, pam-b, peptidylglycine alpha-monooxygenase, peptidylglycine-alpha-amidating monooxygenase, more
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
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