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Literature summary for 1.14.17.3 extracted from
- Striking oxygen sensitivity of the peptidylglycine alpha-amidating monooxygenase (PAM) in neuroendocrine cells (2015), J. Biol. Chem., 290, 24891-24901 .
Application
| Application | Comment | Organism |
|---|---|---|
| analysis | enzyme PAM-dependent amidation has the potential to signal oxygen levels in the same range as the hypoxia-inducible factor (HIF) system | Homo sapiens |
| analysis | enzyme PAM-dependent amidation has the potential to signal oxygen levels in the same range as the hypoxia-inducible factor (HIF) system | Mus musculus |
| analysis | enzyme PAM-dependent amidation has the potential to signal oxygen levels in the same range as the hypoxia-inducible factor (HIF) system | Drosophila melanogaster |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | siRNA knockdown of PAM is accompanied by a loss of 18 kDa JP-NH2 immunoactivity with gamma3-MSH immunoactivity remaining unaffected | Mus musculus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | peptide substrate amidation is strikingly sensitive to the exposure of cells to moderate hypoxia | Drosophila melanogaster | |
| additional information | peptide substrate amidation is strikingly sensitive to the exposure of cells to moderate hypoxia | Homo sapiens | |
| additional information | peptide substrate amidation is strikingly sensitive to the exposure of cells to moderate hypoxia, hypoxia inhibits amidation of constitutively secreted POMC 18-kDa fragment | Mus musculus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| secretory granule | - |
Homo sapiens | 30141 | - |
| secretory granule | - |
Mus musculus | 30141 | - |
| secretory granule | - |
Drosophila melanogaster | 30141 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | dependent on | Homo sapiens |  |
| Cu2+ | dependent on | Mus musculus | |
| Cu2+ | dependent on | Drosophila melanogaster | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | C-terminally amidation of a range of peptides by the copper-dependent enzyme, peptidylglycine alpha-amidating monooxygenase, PAM | ? | - |
? | |
| additional information | Mus musculus | C-terminally amidation of a range of peptides by the copper-dependent enzyme, peptidylglycine alpha-amidating monooxygenase, PAM | ? | - |
? | |
| additional information | Drosophila melanogaster | C-terminally amidation of a range of peptides by the copper-dependent enzyme, peptidylglycine alpha-amidating monooxygenase, PAM. PAM-dependent amidation of POMC peptides in AtT20 cells | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Drosophila melanogaster | O01404 | - |
- |
| Homo sapiens | P19021 | - |
- |
| Mus musculus | P97467 | - |
- |
Oxidation Stability
| Oxidation Stability | Organism |
|---|---|
| oxygen sensitivity of the peptidylglycine alpha-amidating monooxygenase (PAM) in neuroendocrine cells | Homo sapiens |
| oxygen sensitivity of the peptidylglycine alpha-amidating monooxygenase (PAM) in neuroendocrine cells | Mus musculus |
| oxygen sensitivity of the peptidylglycine alpha-amidating monooxygenase (PAM) in neuroendocrine cells | Drosophila melanogaster |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| AtT20 cell | - |
Mus musculus | - |
| H-146 cell | - |
Homo sapiens | - |
| H-69 cell | - |
Homo sapiens | - |
| H727 cell | - |
Homo sapiens | - |
| Kelly cell | - |
Homo sapiens | - |
| neuroendocrine cell | - |
Homo sapiens | - |
| neuroendocrine cell | neuroendocrine Tv cells of larval brains | Drosophila melanogaster | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| chromogranin A + ascorbate + O2 | - |
Homo sapiens | ? + dehydroascorbate + H2O | - |
? | |
| chromogranin A + ascorbate + O2 | - |
Mus musculus | ? + dehydroascorbate + H2O | - |
? | |
| chromogranin A + ascorbate + O2 | - |
Drosophila melanogaster | ? + dehydroascorbate + H2O | - |
? | |
| additional information | C-terminally amidation of a range of peptides by the copper-dependent enzyme, peptidylglycine alpha-amidating monooxygenase, PAM | Homo sapiens | ? | - |
? | |
| additional information | C-terminally amidation of a range of peptides by the copper-dependent enzyme, peptidylglycine alpha-amidating monooxygenase, PAM | Mus musculus | ? | - |
? | |
| additional information | C-terminally amidation of a range of peptides by the copper-dependent enzyme, peptidylglycine alpha-amidating monooxygenase, PAM. PAM-dependent amidation of POMC peptides in AtT20 cells | Drosophila melanogaster | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CG3832 | - |
Drosophila melanogaster |
| PAM | - |
Homo sapiens |
| PAM | - |
Mus musculus |
| PAM | - |
Drosophila melanogaster |
| peptidylglycine alpha-amidating monooxygenase | - |
Homo sapiens |
| peptidylglycine alpha-amidating monooxygenase | - |
Mus musculus |
| peptidylglycine alpha-amidating monooxygenase | - |
Drosophila melanogaster |
| peptidylglycine alpha-hydroxylating monooxygenase | - |
Homo sapiens |
| peptidylglycine alpha-hydroxylating monooxygenase | - |
Mus musculus |
| peptidylglycine alpha-hydroxylating monooxygenase | - |
Drosophila melanogaster |
| PHM | - |
Homo sapiens |
| PHM | - |
Mus musculus |
| PHM | - |
Drosophila melanogaster |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ascorbate | - |
Homo sapiens | |
| ascorbate | - |
Mus musculus | |
| ascorbate | - |
Drosophila melanogaster | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | PAM is a bifunctional enzyme, its copper-dependent peptidylglycine alpha-hydroxylating monooxygenase, PHM, domain converts peptidylglycine substrates to peptidyl-alpha-hydroxyglycine intermediates that are subsequently converted into amidated products plus glyoxylate by the zinc-dependent peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) domain. The reaction catalyzed by PHM results in the stereospecific incorporation of one atom of molecular oxygen into the substrate in a reaction that involves two single electron transfer steps. PAM-mediated C-terminal amidation occurs across a range of biologically active endocrine and nervous system peptides and in many cases has been shown to be required for normal biological activity in vivo. Peptidylglycine alpha-amidating monooxygenase (PAM) is solely responsible for catalysis of amidation, a biologically important posttranslational modification. Peptide substrate amidation is strikingly sensitive to the exposure of cells to moderate hypoxia, physiological effects of hypoxia may be PAM-dependent. Because PAM-dependent amidation is irreversible, bi-directional responses that rapidly upregulate and downregulate levels of amidation can only be observed on rapidly turned-over PAM substrates | Homo sapiens |
| physiological function | PAM is a bifunctional enzyme, its copper-dependent peptidylglycine alpha-hydroxylating monooxygenase, PHM, domain converts peptidylglycine substrates to peptidyl-alpha-hydroxyglycine intermediates that are subsequently converted into amidated products plus glyoxylate by the zinc-dependent peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) domain. The reaction catalyzed by PHM results in the stereospecific incorporation of one atom of molecular oxygen into the substrate in a reaction that involves two single electron transfer steps. PAM-mediated C-terminal amidation occurs across a range of biologically active endocrine and nervous system peptides and in many cases has been shown to be required for normal biological activity in vivo. Peptidylglycine alpha-amidating monooxygenase (PAM) is solely responsible for catalysis of amidation, a biologically important posttranslational modification. Peptide substrate amidation is strikingly sensitive to the exposure of cells to moderate hypoxia, physiological effects of hypoxia may be PAM-dependent. Because PAM-dependent amidation is irreversible, bi-directional responses that rapidly upregulate and downregulate levels of amidation can only be observed on rapidly turned-over PAM substrates | Mus musculus |
| physiological function | peptidylglycine alpha-amidating monooxygenase (PAM) is solely responsible for catalysis of amidation, a biologically important posttranslational modification. Peptide substrate amidation is strikingly sensitive to the exposure of cells to moderate hypoxia, physiological effects of hypoxia may be PAM-dependent. PHM-dependent amidation of POMC peptides is sensitive to oxygen in AtT20 cells. Enzyme PHM is essential for development in Drosophila melanogaster. Peptidylglycine alpha-amidating monooxygenase (PAM) is solely responsible for catalysis of amidation, a biologically important posttranslational modification. Peptide substrate amidation is strikingly sensitive to the exposure of cells to moderate hypoxia, physiological effects of hypoxia may be PAM-dependent. Because PAM-dependent amidation is irreversible, bi-directional responses that rapidly upregulate and downregulate levels of amidation can only be observed on rapidly turned-over PAM substrates | Drosophila melanogaster |
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