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Literature summary for 1.14.17.3 extracted from
- A new proposal for the mechanism of glycine hydroxylation as catalyzed by peptidylglycine alpha-hydroxylating monooxygenase (PHM) (2004), Med. Hypotheses, 62, 392-400.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | enzyme expression is induced by androgen-deprivation therapy | Rattus norvegicus |
Application
| Application | Comment | Organism |
|---|---|---|
| pharmacology | enzyme is an attractive target for development of anti-tumor compounds | Rattus norvegicus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| copper | metalloenzyme, required for catalysis, bound at the active site | Rattus norvegicus |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Rattus norvegicus | enzyme is required for amidation of autocrine growth factors causing proliferation in tumor cells | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O | detailed analysis of the reaction mechanism, reaction scheme, strictly ordered ping-pong kinetic mechanism in which ascorbate first reduces Cu(II) to Cu(I), semidehydroascorbate being released, after which the peptide binds and finally oxygen, active site structure | Rattus norvegicus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | substrate specificity | Rattus norvegicus | ? | - |
? | |
| additional information | enzyme is required for amidation of autocrine growth factors causing proliferation in tumor cells | Rattus norvegicus | ? | - |
? | |
| peptidylglycine + ascorbate + O2 | peptidylglycine alpha-hydroxylating monooxygenase reaction | Rattus norvegicus | peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide | ? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| bifunctional peptidylglycine alpha-amidating monooxygenase | - |
Rattus norvegicus |
| PAM | - |
Rattus norvegicus |
| PAM/PHM | - |
Rattus norvegicus |
| peptidylglycine alpha-hydroxylating monooxygenase | - |
Rattus norvegicus |
| PHM | - |
Rattus norvegicus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ascorbate | - |
Rattus norvegicus | |
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Release 2023.1 (January 2023)
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