show all | hide all No of entries

Information on EC - peptidylglycine monooxygenase

for references in articles please use BRENDA:EC1.14.17.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Select one or more organisms in this record: ?
Word Map
The enzyme appears in viruses and cellular organisms
peptidylglycine alpha-hydroxylating monooxygenase, bifunctional pam, peptidylglycine monooxygenase, peptidyl-glycine alpha-amidating monooxygenase, alpha-ae, peptidylglycine alpha-amidating mono-oxygenase, phmcc, pam-b, peptidylglycine alpha-monooxygenase, peptidylglycine-alpha-amidating monooxygenase, more
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
show the reaction diagram