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 A |
Enzyme Information
| 1.14.17.3 |
Peptidylglycine monooxygenase.
based on mapping to UniProt P14925
Peptidylglycine + ascorbate + O(2) = peptidyl(2-hydroxyglycine) + dehydroascorbate + H(2)O.
-!- 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. -!- 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
Peptidylamidoglycolate = peptidyl 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
Peptidyl-glycine alpha-amidating monooxygenase
|
PDB Structure
| PDB | 1OPM |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Cricetulus |
| Primary Citation |
Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase.
Nat.Struct.Biol.
|