peptidylglycine monooxygenase EC#: 1.14.17.3; ChemWhat Code: 1375743
Product Name | peptidylglycine monooxygenase |
Example Structure | |
Synonyms | alpha-AE, bifunctional PAM, bifunctional peptidylglycine alpha-amidating monooxygenase, CG3832, hPHMcc, More, PAM, PAM-1, PAM-2, PAM-A, PAM-B, PAM/PHM, peptide alpha-amidating enzyme, peptide alpha-amide synthase, peptide-alpha-amide synthetase, peptidyl alpha-amidating enzyme, peptidyl alpha-hydroxylating monooxygenase, peptidyl-glycine alpha-amidating monooxygenase, peptidylglycine 2-hydroxylase, peptidylglycine alpha-amidating mono-oxygenase, peptidylglycine alpha-amidating monooxygenase, peptidylglycine alpha-hydroxylase, peptidylglycine alpha-hydroxylating monooxygenase, peptidylglycine alpha-hydroxylating-monooxygenase, peptidylglycine alpha-monooxygenase, peptidylglycine monooxygenase, peptidylglycine-alpha-amidating monooxygenase, PHM, PHMcc, synthase, peptide alpha-amide, type A PAM |
EC Number | 1.14.17.3 |
CAS Registry Number | 90597-47-0 |
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 4.3.2.5 peptidylamidoglycolate lyase. In mammals, the two activities are part of a bifunctional protein. Involved in the final step of biosynthesis of ¦Á-melanotropin and related biologically active peptides. |
Cofactor | Cu cation |
History | |
Reactions | Peptidylglycine + ascorbate + O(2) = peptidyl(2-hydroxyglycine) + dehydroascorbate + H(2)O. |
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