CATH Classification

Domain Context

CATH Clusters

Superfamily Copper type II, ascorbate-dependent monooxygenase, N-terminal domain
Functional Family peptidyl-glycine alpha-amidating monooxygenase isoform X1

Enzyme Information
Peptidylglycine monooxygenase.
based on mapping to UniProt P14925
[Peptide]-glycine + 2 ascorbate + O(2) = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H(2)O.
-!- 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 catalyzed by EC -!- 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.
Peptidylamidoglycolate lyase.
based on mapping to UniProt P14925
[Peptide]-(2S)-2-hydroxyglycine = [peptide]-amide + glyoxylate.
-!- Acts on the product of the reaction catalyzed by EC, thus removing a terminal glycine residue and leaving a des-glycine peptide amide.

UniProtKB Entries (1)

Rattus norvegicus
Peptidylglycine alpha-amidating monooxygenase

PDB Structure

External Links
Organism Cricetulus
Primary Citation
Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase.
Prigge, S.T., Kolhekar, A.S., Eipper, B.A., Mains, R.E., Amzel, L.M.