Peptidylglycine monooxygenase

In enzymology, a peptidylglycine monooxygenase is an enzyme that catalyzes the chemical reaction


 * peptidylglycine + ascorbate + O2 $$\rightleftharpoons$$ peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O

The 3 substrates of this enzyme are peptidylglycine, ascorbate, and O2, whereas its 3 products are peptidyl(2-hydroxyglycine), dehydroascorbate, and H2O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced ascorbate as one donor, and incorporation of one ato of oxygen into the other donor. The systematic name of this enzyme class is peptidylglycine,ascorbate:oxygen oxidoreductase (2-hydroxylating). Other names in common use include peptidylglycine 2-hydroxylase, peptidyl alpha-amidating enzyme, peptide-alpha-amide synthetase, synthase, peptide alpha-amide, peptide alpha-amidating enzyme, peptide alpha-amide synthase, peptidylglycine alpha-hydroxylase, peptidylglycine alpha-amidating monooxygenase, PAM-A, PAM-B, and PAM. It employs one cofactor, copper.

Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , and.