ENZYME entry: EC 1.14.17.3
| Accepted Name |
| Peptidylglycine monooxygenase.
|
| Alternative Name(s) |
| PAM. |
| Peptidyl alpha-amidating enzyme. |
| Peptidylglycine 2-hydroxylase. |
| Peptidylglycine alpha-amidating monooxygenase. |
| Reaction catalysed |
| Peptidylglycine + ascorbate + O(2) <=> peptidyl(2-hydroxyglycine) + dehydroascorbate + H(2)O |
| Cofactor(s) |
| Copper.
|
| Comment(s) |
- 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.
|
| Cross-references |
| PROSITE | PDOC00080 |
| BRENDA | 1.14.17.3 |
| EC2PDB | 1.14.17.3 |
| ExplorEnz | 1.14.17.3 |
| PRIAM enzyme-specific profiles | 1.14.17.3 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.14.17.3 |
| IUBMB Enzyme Nomenclature | 1.14.17.3 |
| IntEnz | 1.14.17.3 |
| MEDLINE | Find literature relating to 1.14.17.3 |
| MetaCyc | 1.14.17.3 |
| UniProtKB/Swiss-Prot |
|
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