Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | Cu2+ is absolutely required for optimal activity | Equus caballus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
peptidylglycine + ascorbate + O2 | Equus caballus | - |
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Equus caballus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Equus caballus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O | structure analysis | Equus caballus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
serum | - |
Equus caballus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | at alkaline pH spontaneous conversion | Equus caballus | ? | - |
? | |
additional information | EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase | Equus caballus | ? | - |
? | |
peptidylglycine + ascorbate + O2 | - |
Equus caballus | peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? | |
peptidylglycine + ascorbate + O2 | requirement for O2 | Equus caballus | peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? | |
peptidylglycine + ascorbate + O2 | COOH-terminal glycine | Equus caballus | peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? | |
Phe-Gly-Phe-Gly + ascorbate + O2 | - |
Equus caballus | Phe-Gly-Phe-2-hydroxyglycine + dehydroascorbate + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
More | at alkaline pH spontaneous conversion | Equus caballus |
More | EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PHM), 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PHL) | Equus caballus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ascorbate | dependent on | Equus caballus |