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Literature summary extracted from
- Expression and characterization of human bifunctional peptidylglycine alpha-amidating monooxygenase (2003), Protein Expr. Purif., 28, 293-302.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.17.3 | subcloning from human heart lambda-gt10 library in Escherichia coli, soluble recombinant enzyme through elimination of the C-terminal membrane-spanning domain, expression of a soluble form in CHO K-1 cells, excretion of the recombinant enzyme to the cell culture medium | Homo sapiens |
| 4.3.2.5 | expression in chinese hamster ovary K-1 cells | Homo sapiens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.3.2.5 | diethyl dicarbonate | - |
Homo sapiens |  |
| 4.3.2.5 | Phenylglyoxal | - |
Homo sapiens | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 4.3.2.5 | membrane | - |
Homo sapiens | 16020 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.17.3 | Ca2+ | 3.26 mol per mol of bifunctional enzyme | Homo sapiens | |
| 1.14.17.3 | Cu2+ | required for peptidylglycine alpha-hydroxylating monooxygenase activity, 1.25 mol per mol of bifunctional enzyme | Homo sapiens | |
| 1.14.17.3 | Fe2+ | 0.37 mol per mol of bifunctional enzyme | Homo sapiens | |
| 1.14.17.3 | Mg2+ | 0.88 mol per mol of bifunctional enzyme | Homo sapiens | |
| 1.14.17.3 | Zn2+ | required for peptidylamidoglycolate lyase activity, 0.62 mol per mol of bifunctional enzyme | Homo sapiens | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.14.17.3 | 91000 | - |
x * 91000, recombinant soluble enzyme, SDS-PAGE | Homo sapiens |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.17.3 | Homo sapiens | P19021 | bifunctional enzyme showing peptidylglycine alpha-hydroxylating monooxygenase, PHM, EC 1.14.17.3, and peptidylamidoglycolate lyase, PAL, EC 4.3.2.5, activities | - |
| 4.3.2.5 | Homo sapiens | - |
EC 1.14.17.3 (PHM) and EC 4.3.2.5 (PAL) are part of a bifunctional protein | - |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 1.14.17.3 | glycoprotein | enzyme contains 2 putative N-glycosylation sites at ASn411 and Asn762, the purified enzyme contains at least 1 sugar chain | Homo sapiens |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.17.3 | recombinant soluble enzyme from culture medium in a 3-step chromatographic procedure, about 40fold to near homogeneity | Homo sapiens |
| 4.3.2.5 | - |
Homo sapiens |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.14.17.3 | [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O | bifunctional enzyme showing peptidylglycine alpha-hydroxylating monooxygenase, EC 1.14.17.3, and peptidylamidoglycolate lyase, PAL, EC 4.3.2.5, activities, the enzyme possesses 2 catalytic domains | Homo sapiens |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.14.17.3 | heart | - |
Homo sapiens | - |
| 4.3.2.5 | heart | - |
Homo sapiens | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.14.17.3 | 0.53 | - |
purified recombinant enzyme, peptidylglycine alpha-hydroxylating monooxygenase activity | Homo sapiens |
| 4.3.2.5 | 0.53 | - |
Sephacryl S-300 purification step | Homo sapiens |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.17.3 | D-iodo-Tyr-Val-Gly + ascorbate + O2 | labeled substrate | Homo sapiens | D-iodo-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O | the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide | ? | |
| 1.14.17.3 | N-trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2 | - |
Homo sapiens | N-trinitrophenyl-D-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O | the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide | ? | |
| 1.14.17.3 | peptidylglycine + ascorbate + O2 | peptidylglycine alpha-hydroxylating monooxygenase reaction | Homo sapiens | 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 | ? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.17.3 | ? | x * 91000, recombinant soluble enzyme, SDS-PAGE | Homo sapiens |
| 1.14.17.3 | More | the enzyme possesses 2 catalytic domains | Homo sapiens |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.17.3 | bifunctional PAM | - |
Homo sapiens |
| 1.14.17.3 | bifunctional peptidylglycine alpha-amidating monooxygenase | - |
Homo sapiens |
| 1.14.17.3 | PHM | - |
Homo sapiens |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.17.3 | 6 | 7 | assay at, dependent on the substrate used | Homo sapiens |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.17.3 | ascorbate | - |
Homo sapiens | |
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