EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.17.3 | expression in Spodoptera fugiperda cells via baculovirus vector, amino acid sequence analysis | Xenopus laevis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.17.3 | Cu2+ | - |
Xenopus laevis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.17.3 | peptidylglycine + ascorbate + O2 | Xenopus laevis | - |
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.17.3 | Xenopus laevis | - |
peptidylglycine alpha-hydroxylating monooxygenase activity | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.14.17.3 | native wild-type and recombinant from Spodoptera frugiperda cell expression system | Xenopus laevis |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.14.17.3 | [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O | mechanism | Xenopus laevis | |
1.14.17.3 | [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O | ping-pong-mechanism | Xenopus laevis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.17.3 | D-Tyr-Val-Gly + ascorbate + O2 | - |
Xenopus laevis | D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O | - |
? | |
1.14.17.3 | 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 | Xenopus laevis | ? | - |
? | |
1.14.17.3 | peptidylglycine + ascorbate + O2 | - |
Xenopus laevis | peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? | |
1.14.17.3 | peptidylglycine + ascorbate + O2 | COOH-terminal glycine | Xenopus laevis | peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.17.3 | 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) | Xenopus laevis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.17.3 | ascorbate | dependent on | Xenopus laevis |