CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.60 | Sandwich |
|
2.60.120 | Jelly Rolls |
|
2.60.120.230 |
Domain Context
CATH Clusters
| Superfamily | 2.60.120.230 |
| Functional Family | Peptidyl-glycine alpha-amidating monooxygenase B |
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 | 6AY0 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Effects of copper occupancy on the conformational landscape of peptidylglycine alpha-hydroxylating monooxygenase.
Commun Biol
|