Function and Biology Details
Reactions catalysed:
[Peptide]-glycine + 2 ascorbate + O(2) = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H(2)O
[Peptide]-(2S)-2-hydroxyglycine = [peptide]-amide + glyoxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Peptidylglycine alpha-hydroxylating monooxygenase/peptidyl-hydroxyglycine alpha-amidating lyase
- PHM/PNGase F domain superfamily
- Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-2 conserved site
- Copper type II, ascorbate-dependent monooxygenase-like, C-terminal
- Copper type II ascorbate-dependent monooxygenase, C-terminal
- Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-1 conserved site
- Copper type II, ascorbate-dependent monooxygenase, N-terminal
- Copper type II, ascorbate-dependent monooxygenase, N-terminal domain superfamily
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Peptidylglycine alpha-amidating monooxygenase (preferred)
PDBe Complex ID:
PDB-CPX-147156 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidylglycine alpha-amidating monooxygenase
Molecule details ›
Chain: A
Length: 312 amino acids
Theoretical weight: 34.71 KDa
Source organism: Rattus norvegicus
Expression system: Cricetulus griseus
UniProt:
Sequence domains:
Length: 312 amino acids
Theoretical weight: 34.71 KDa
Source organism: Rattus norvegicus
Expression system: Cricetulus griseus
UniProt:
- Canonical:
P14925 (Residues: 45-356; Coverage: 33%)
Sequence domains:
- Copper type II ascorbate-dependent monooxygenase, N-terminal domain
- Copper type II ascorbate-dependent monooxygenase, C-terminal domain
