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 | 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 | 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P19021 | - |
- |
Rattus norvegicus | P14925 | - |
- |
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 | 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 | 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 Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
in vivo assay at | Homo sapiens |
37 | - |
in vivo assay at | Rattus norvegicus |
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 | Comment | Organism | Structure |
---|---|---|---|
ascorbate | - |
Homo sapiens | |
ascorbate | - |
Rattus norvegicus |
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 |