EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.17.3 | (E)-(4-dimethylamino)cinnamic acid | - |
Homo sapiens | |
1.14.17.3 | (E)-3,4-methylenedioxycinnamic acid | - |
Homo sapiens | |
1.14.17.3 | (E)-4-aminocinnamic acid | - |
Homo sapiens | |
1.14.17.3 | 2-trifluoromethylcinnamic acid | - |
Homo sapiens | |
1.14.17.3 | 2-trifluoromethylcinnamic acid | - |
Rattus norvegicus | |
1.14.17.3 | 3,4-methylenedioxycinnamic acid | - |
Rattus norvegicus | |
1.14.17.3 | 3-(3-pyridyl)acrylic acid | - |
Homo sapiens | |
1.14.17.3 | 3-(3-pyridyl)acrylic acid | - |
Rattus norvegicus | |
1.14.17.3 | 4-aminocinnamic acid | - |
Rattus norvegicus | |
1.14.17.3 | 4-nitrocinnamic acid | - |
Rattus norvegicus | |
1.14.17.3 | Cinnamic acid | extensive dialysis of bifunctional PAM incubated with cinnamate yielded inactive enzyme unable to catalyze the production of glyoxylate from hippuric acid | Homo sapiens | |
1.14.17.3 | Cinnamic acid | - |
Rattus norvegicus | |
1.14.17.3 | additional information | cinnamic acid and cinnamic acid analogues are inhibitors or inactivators of PHM. The inactivation chemistry of the cinnamates exhibits all the attributes of a suicide-substrate. But no formation of an irreversible linkage between cinnamate and PHM in the inactivated enzyme is detected. Instead reversible formation of a Michael adduct between an active site nucleophile and cinnamate occurs that leads to inactive enzyme. Cinnamates are found in fruits, fruit juices, vegetables and flowers. Protection of PHM against the cinnamate-mediated inactivation by tiopronin. Molecular docking studies, overview | Homo sapiens | |
1.14.17.3 | N,N-dimethyl-4-aminocinnamic acid | - |
Rattus norvegicus | |
1.14.17.3 | N-dansyl-4-aminocinnamate | a fluorescent molecule, an inactivator | Homo sapiens | |
1.14.17.3 | N-dansyl-4-aminocinnamic acid | - |
Rattus norvegicus | |
1.14.17.3 | perdeuterated cinnamic acid | - |
Homo sapiens | |
1.14.17.3 | perdeuterated cinnamic acid | - |
Rattus norvegicus | |
1.14.17.3 | phenylpropionic acid | - |
Rattus norvegicus | |
1.14.17.3 | phenylpropynoic acid | i.e. phenylpropiolic acid | Homo sapiens | |
1.14.17.3 | trans-cinnamic acid | - |
Homo sapiens | |
1.14.17.3 | Urocanic acid | - |
Homo sapiens | |
1.14.17.3 | Urocanic acid | - |
Rattus norvegicus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.17.3 | Cu2+ | dependent on | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.17.3 | peptidylglycine + ascorbate + O2 | Homo sapiens | - |
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? | |
1.14.17.3 | peptidylglycine + ascorbate + O2 | Rattus norvegicus | the enzyme catalyzes the final reaction in the maturation of alpha-amidated peptide hormones | peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.17.3 | Homo sapiens | P19021 | - |
- |
1.14.17.3 | Rattus norvegicus | P14925 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.17.3 | acetyl-glycine + ascorbate + O2 | - |
Rattus norvegicus | ? | - |
? | |
1.14.17.3 | hippuric acid + ascorbate + O2 | - |
Homo sapiens | benzamide + glyoxylate + dehydroascorbate + H2O | - |
? | |
1.14.17.3 | peptidylglycine + ascorbate + O2 | - |
Homo sapiens | peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? | |
1.14.17.3 | peptidylglycine + ascorbate + O2 | - |
Rattus norvegicus | peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? | |
1.14.17.3 | peptidylglycine + ascorbate + O2 | the enzyme catalyzes the final reaction in the maturation of alpha-amidated peptide hormones | Rattus norvegicus | peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.17.3 | PAM | - |
Homo sapiens |
1.14.17.3 | PAM | - |
Rattus norvegicus |
1.14.17.3 | peptidylglycine alpha-amidating monooxygenase | - |
Rattus norvegicus |
1.14.17.3 | peptidylglycine alpha-hydroxylating monooxygenase | - |
Homo sapiens |
1.14.17.3 | PHM | - |
Homo sapiens |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.14.17.3 | 37 | - |
assay at | Homo sapiens |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.14.17.3 | 6 | - |
assay at | Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.17.3 | ascorbate | - |
Homo sapiens |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.17.3 | 0.01 | - |
N-dansyl-4-aminocinnamic acid | 37°C, pH 6.0 | Rattus norvegicus | |
1.14.17.3 | 0.2 | - |
2-trifluoromethylcinnamic acid | 37°C, pH 6.0 | Rattus norvegicus | |
1.14.17.3 | 0.3 | - |
3,4-methylenedioxycinnamic acid | 37°C, pH 6.0 | Rattus norvegicus | |
1.14.17.3 | 0.5 | - |
4-aminocinnamic acid | 37°C, pH 6.0 | Rattus norvegicus | |
1.14.17.3 | 0.6 | - |
4-nitrocinnamic acid | 37°C, pH 6.0 | Rattus norvegicus | |
1.14.17.3 | 2 | - |
phenylpropionic acid | 37°C, pH 6.0 | Rattus norvegicus | |
1.14.17.3 | 3 | - |
N,N-dimethyl-4-aminocinnamic acid | 37°C, pH 6.0 | Rattus norvegicus | |
1.14.17.3 | 4 | - |
Cinnamic acid | 37°C, pH 6.0 | Rattus norvegicus | |
1.14.17.3 | 4 | - |
perdeuterated cinnamic acid | 37°C, pH 6.0 | Rattus norvegicus | |
1.14.17.3 | 6 | - |
3-(3-pyridyl)acrylic acid | 37°C, pH 6.0 | Rattus norvegicus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.17.3 | metabolism | the enzyme catalyzes the final reaction in the maturation of alpha-amidated peptide hormones | Rattus norvegicus |
1.14.17.3 | physiological function | peptidylglycine alpha-amidating monooxygenase (PAM) is a bifunctional enzyme that catalyzes the final reaction in the maturation of alpha-amidated peptide hormones. Peptidylglycine alpha-hydroxylating monooxygenase (PHM) is the PAM domain responsible for the copper-, ascorbate- and O2-dependent hydroxylation of glycine-extended precursor peptides to the active alpha-amidated peptide and glyoxylate. Peptidylamidoglycolate lyase, EC 4.3.2.5, is the PAM domain responsible for the Zn(II)-dependent dealkylation of the alpha-hydroxyglycine-containing precursor to the final alpha-amidated peptide | Homo sapiens |