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Literature summary for 1.14.17.3 extracted from
- Adaptor protein-1 complex affects the endocytic trafficking and function of peptidylglycine alpha-amidating monooxygenase, a luminal cuproenzyme (2015), J. Biol. Chem., 290, 21264-21279 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene PAM-1, recombinant stable expression in murine AtT-20 cells | Homo sapiens |
| gene PAM-1, recombinant stable expression in murine AtT-20 cells. Atp7a, AP-1, and PAM co-localize in the Golgi region of recombinant AtT-20 cells | Rattus norvegicus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| endoplasmic reticulum membrane | integral membrane enzyme | Homo sapiens | 5789 | - |
| endoplasmic reticulum membrane | integral membrane enzyme | Rattus norvegicus | 5789 | - |
| Golgi apparatus | quantification of PAM endocytic trafficking to the trans-Golgi network | Homo sapiens | 5794 | - |
| Golgi apparatus | quantification of PAM endocytic trafficking to the trans-Golgi network | Rattus norvegicus | 5794 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | the cuproenzyme PAM requires copper to catalyze peptide amidation | Homo sapiens |  |
| Cu2+ | the cuproenzyme PAM requires copper to catalyze peptide amidation | Rattus norvegicus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | constitutive-like secretion of POMC products in recombinant enzyme-expressing cells | ? | - |
? | |
| additional information | Rattus norvegicus | constitutive-like secretion of POMC products in recombinant enzyme-expressing cells | ? | - |
? | |
| proopiomelanocortin peptide + ascorbate + O2 | Homo sapiens | a POMC 18-kDa fragment | proopiomelanocortin peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? | |
| proopiomelanocortin peptide + ascorbate + O2 | Rattus norvegicus | a POMC 18-kDa fragment | proopiomelanocortin peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P19021 | - |
- |
| Rattus norvegicus | P14925 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| cell culture | - |
Homo sapiens | - |
| cell culture | primary anterior pituitary cells | Rattus norvegicus | - |
| additional information | Atp7a, AP-1, and PAM co-localize in the Golgi region of primary pituitary cells | Rattus norvegicus | - |
| neuroendocrine cell | - |
Homo sapiens | - |
| pituitary gland | primary anterior pituitary cells | Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | constitutive-like secretion of POMC products in recombinant enzyme-expressing cells | Homo sapiens | ? | - |
? | |
| additional information | constitutive-like secretion of POMC products in recombinant enzyme-expressing cells | Rattus norvegicus | ? | - |
? | |
| proopiomelanocortin peptide + ascorbate + O2 | a POMC 18-kDa fragment | Homo sapiens | proopiomelanocortin peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? | |
| proopiomelanocortin peptide + ascorbate + O2 | a POMC 18-kDa fragment | Rattus norvegicus | proopiomelanocortin peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? | |
| proopiomelanocortin peptide + ascorbate + O2 | a POMC 18-kDa fragment, establishment of an assay method | Homo sapiens | proopiomelanocortin peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? | |
| proopiomelanocortin peptide + ascorbate + O2 | a POMC 18-kDa fragment, establishment of an assay method | Rattus norvegicus | proopiomelanocortin peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PAM | - |
Homo sapiens |
| PAM | - |
Rattus norvegicus |
| PAM-1 | - |
Homo sapiens |
| PAM-1 | - |
Rattus norvegicus |
| peptidylglycine alpha-amidating monooxygenase | - |
Homo sapiens |
| peptidylglycine alpha-amidating monooxygenase | - |
Rattus norvegicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
in vivo assay at | Homo sapiens |
| 37 | - |
in vivo assay at | Rattus norvegicus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
in vivo assay at | Homo sapiens |
| 7.4 | - |
in vivo assay at | Rattus norvegicus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ascorbate | - |
Homo sapiens | |
| ascorbate | - |
Rattus norvegicus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | disruption of AP-1-dependent late endosomal trafficking diminishes the ability of PAM to retain copper and produce amidated peptides. Impaired AP-1 function alters luminal copper delivery to PAM. Altered luminal cuproenzyme function may contribute to diseases associated with diminished AP-1 function. Reduced AP-1 function makes 18-kDa fragment amidation more sensitive to inhibition by bathocuproine disulfonate, a cell-impermeant Cu(I) chelator. The endocytic trafficking of PAM is altered, and PAM-1 accumulates on the cell surface when AP-1 levels are reduced | Homo sapiens |
| malfunction | disruption of AP-1-dependent late endosomal trafficking diminishes the ability of PAM to retain copper and produce amidated peptides. Impaired AP-1 function alters luminal copper delivery to PAM. Altered luminal cuproenzyme function may contribute to diseases associated with diminished AP-1 function. Reduced AP-1 function makes 18-kDa fragment amidation more sensitive to inhibition by bathocuproine disulfonate, a cell-impermeant Cu(I) chelator. The endocytic trafficking of PAM is altered, and PAM-1 accumulates on the cell surface when AP-1 levels are reduced | Rattus norvegicus |
| physiological function | in neuroendocrine cells, ATP7A provides copper to peptidylglycine alpha-amidating monooxygenase (PAM), an essential enzyme that requires copper to catalyze peptide amidation, one of the final steps in the production of bioactive peptides. Trafficking of Atp7a, a copper pump, and the cuproenzyme PAM-1 depend on adaptor protein-1 complex (AP-1). The enzyme is involved in the prohormone POMC processing pathway and constitutive-like secretion, overview. Production of the amidated products of POMC (18-kDa fragment-NH2, JP-NH2, and ACTH(1-13)NH2) requires both PAM and Atp7a | Homo sapiens |
| physiological function | in neuroendocrine cells, ATP7A provides copper to peptidylglycine alpha-amidating monooxygenase (PAM), an essential enzyme that requires copper to catalyze peptide amidation, one of the final steps in the production of bioactive peptides. Trafficking of Atp7a, a copper pump, and the cuproenzyme PAM-1 depend on adaptor protein-1 complex (AP-1). The enzyme is involved in the prohormone POMC processing pathway and constitutive-like secretion, overview. Production of the amidated products of POMC (18-kDa fragment-NH2, JP-NH2, and ACTH(1-13)NH2) requires both PAM and Atp7a, Atp7a concentrates in the Golgi region in pituitary cells | Rattus norvegicus |
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