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

1.14.17.3
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 4.3.2.5. -!- 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.
4.3.2.5
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 1.14.17.3, thus removing a terminal glycine residue and leaving a des-glycine peptide amide.

UniProtKB Entries (1)

P14925
AMD_RAT
Rattus norvegicus
Peptidylglycine alpha-amidating monooxygenase

PDB Structure

PDB 6ALV
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Effects of copper occupancy on the conformational landscape of peptidylglycine alpha-hydroxylating monooxygenase.
Maheshwari, S., Shimokawa, C., Rudzka, K., Kline, C.D., Eipper, B.A., Mains, R.E., Gabelli, S.B., Blackburn, N., Amzel, L.M.
Commun Biol