EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.14.17.3 | acetate | form 1, AE-I, activates below pH 6.0 | Xenopus laevis | |
1.14.17.3 | chloride | form 1, AE-I, activates below pH 6.0 | Xenopus laevis | |
1.14.17.3 | Iodide | form 1, AE-I, activates below pH 6.0 | Xenopus laevis |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.17.3 | expression in Spodoptera fugiperda cells via baculovirus vector of soluble form 1, AE-I showing only peptidylglycine alpha-hydroxylating activity | Xenopus laevis |
EC Number | General Stability | Organism |
---|---|---|
1.14.17.3 | stabilized by salts like KI and KCl, recombinant form 1, AE-I | Xenopus laevis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.17.3 | additional information | form 1, AE-I, competitive inhibition by tripeptides with C-terminal glycine, most effective is methione within these peptides | Xenopus laevis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.17.3 | Cu2+ | Cu2+ is absolutely required for optimal activity | 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 | - |
3 genetic forms, 2 protein forms of amidating enzyme: protein form 1, gene AE-I, has only peptidylglycine alpha-hydroxylating activity, protein form 2, genes AE-III and AE-II, show peptidylglycine alpha-hydroxylating activity and peptidylhydroxylglycine N-C lyase activity | - |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.14.17.3 | [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O | ping-pong-mechanism | Xenopus laevis |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.14.17.3 | skin | soluble enzyme with peptidylglycine alpha-hydroxylating activity, AE-I | Xenopus laevis | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.17.3 | dansyl-D-Tyr-Val-Gly + ascorbate + O2 | - |
Xenopus laevis | dansyl-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 | requirement for 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 | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.14.17.3 | 6 | - |
MES buffer, recombinant from 1, AE-I | Xenopus laevis |
1.14.17.3 | 7 | - |
phosphate buffer, recombinant form 1, AE-I | Xenopus laevis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.17.3 | ascorbate | dependent on | Xenopus laevis |