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EC 1.14.17.3 Details
EC number
1.14.17.3
Accepted name
peptidylglycine monooxygenase
Reaction
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
Other name(s)
peptidylglycine 2-hydroxylase, peptidyl α-amidating enzyme, peptide-α-amide synthetase, peptide α-amidating enzyme, peptide α-amide synthase, peptidylglycine α-hydroxylase, peptidylglycine α-amidating monooxygenase, PAM-A, PAM-B, PAM, peptidylglycine,ascorbate:oxygen oxidoreductase (2-hydroxylating)
Systematic name
[peptide]-glycine,ascorbate:oxygen oxidoreductase (2-hydroxylating)
CAS registry number
90597-47-0
Comment
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 α-melanotropin and related biologically active peptides.
History
created 1989, modified 2019
EC Tree
1.14.1.1 created 1961 as EC 1.99.1.1, transferred 1965 to EC 1.14.14.1, deleted 1972
1.14.1.2 created 1965, deleted 1972
1.14.1.3 created 1961 as EC 1.99.1.13, transferred 1965 to EC 1.14.1.3, deleted 1972
1.14.1.4 created 1965, deleted 1972
1.14.1.5 created 1965, deleted 1972
1.14.1.6 created 1961 as EC 1.99.1.7, transferred 1965 to EC 1.14.1.6, deleted 1972
1.14.1.7 created 1965, deleted 1972
1.14.1.8 created 1965, deleted 1972
1.14.1.9 created 1965, deleted 1972
1.14.1.10 created 1965, deleted 1972
1.14.1.11 created 1965, deleted 1972
1.14.17.2 created 1972, deleted 1984