Cloned (Comment) | Organism |
---|---|
expression in Spodoptera fugiperda cells via baculovirus vector of membrane-associated, bifunctional enzyme form 2, AE-III | Xenopus laevis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | peptidylglycine alpha-hydroxylating activity and peptidylhydroxylglycine N-C lyase activity | Xenopus laevis | 5737 | - |
membrane | recombinant bifunctional enzyme form 2, uncleaved in insect cells | Xenopus laevis | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | - |
Xenopus laevis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
peptidylglycine + ascorbate + O2 | Xenopus laevis | - |
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
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 | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | predominantly membrane-associated, bifunctional enzyme | Xenopus laevis | - |
heart | predominantly membrane-associated, bifunctional enzyme | Xenopus laevis | - |
heart | atrium | Xenopus laevis | - |
heart | ventricle | Xenopus laevis | - |
additional information | tissue distribution, overview | Xenopus laevis | - |
skin | soluble enzyme with peptidylglycine alpha-hydroxylating activity or peptidylhydroxylglycine N-C lyase activity | Xenopus laevis | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.0124 | - |
skin, peptidylhydroxylglycine N-C lyase, highest activity of all tissues | Xenopus laevis |
0.0206 | - |
skin, peptidylglycine alpha-hydroxylating activity, highest activity of all tissues | Xenopus laevis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dansyl-D-Tyr-Val-Gly + ascorbate + O2 | - |
Xenopus laevis | dansyl-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O | - |
? | |
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 | ? | - |
? | |
peptidylglycine + ascorbate + O2 | - |
Xenopus laevis | peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? | |
peptidylglycine + ascorbate + O2 | COOH-terminal glycine | Xenopus laevis | peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
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 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Xenopus laevis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ascorbate | dependent on | Xenopus laevis |