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Literature summary extracted from
- Expression and characterization of frog peptidylglycine alpha-hydroxylating monooxygenase (2003), Protein Expr. Purif., 27, 35-41.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.17.3 | stable and functional expression in CHO cells, method establishment, induction of enzyme expression by addition of sodium propionate, N,N'-hexamethylene-bis-acetamide, or best by sodium butyrate, recombinant enzyme is mostly excreted to the medium | Xenopus laevis |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.17.3 | 0.0011 | - |
N-trinitrophenyl-D-Tyr-Val-Gly | pH 6.0, 37°C, recombinant enzyme | Xenopus laevis |  |
| 1.14.17.3 | 0.057 | - |
D-Tyr-Val-Gly | pH 7.5, 37°C, recombinant enzyme | Xenopus laevis | |
| 1.14.17.3 | 0.61 | - |
hippuric acid | pH 5.0, 37°C, recombinant enzyme | Xenopus laevis | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.14.17.3 | 40000 | - |
x * 40000, recombinant enzyme, SDS-PAGE | Xenopus laevis |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.17.3 | additional information | Xenopus laevis | peptide alpha-amidation, enzyme is responsible for formation of peptide C-terminal amide | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.17.3 | Xenopus laevis | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.17.3 | recombinant enzyme from CHO cell culture medium by copper-chelating affinity chromatography | Xenopus laevis |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|
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 | additional information | - |
- |
Xenopus laevis |
| 1.14.17.3 | 0.85 | - |
purified recombinant enzyme, substrate N-trinitrophenyl-D-Tyr-Val-Gly | Xenopus laevis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.17.3 | D-Tyr-Val-Gly + ascorbate + O2 | synthetic substrate | Xenopus laevis | D-Tyr-Val-NH2 + glyoxylate + dehydroascorbate + H2O | - |
? | |
| 1.14.17.3 | hippuric acid + ascorbate + O2 | synthetic substrate | Xenopus laevis | ? + dehydroascorbate + H2O | - |
ir | |
| 1.14.17.3 | additional information | peptide alpha-amidation, enzyme is responsible for formation of peptide C-terminal amide | Xenopus laevis | ? | - |
? | |
| 1.14.17.3 | additional information | peptide alpha-amidation, the N-terminal substrate structure affects the interaction with the active site of the enzyme | Xenopus laevis | ? | - |
? | |
| 1.14.17.3 | N-trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2 | synthetic substrate | Xenopus laevis | N-trinitrophenyl-D-Tyr-Val-NH2 + glyoxylate + dehydroascorbate + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.17.3 | ? | x * 40000, recombinant enzyme, SDS-PAGE | Xenopus laevis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.17.3 | peptidylglycine alpha-hydroxylating monooxygenase | - |
Xenopus laevis |
| 1.14.17.3 | PHM | - |
Xenopus laevis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.17.3 | 37 | - |
assay at | Xenopus laevis |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.17.3 | 0.02 | - |
hippuric acid | pH 5.0, 37°C, recombinant enzyme | Xenopus laevis | |
| 1.14.17.3 | 0.13 | - |
D-Tyr-Val-Gly | pH 7.5, 37°C, recombinant enzyme | Xenopus laevis | |
| 1.14.17.3 | 1.4 | - |
N-trinitrophenyl-D-Tyr-Val-Gly | pH 6.0, 37°C, recombinant enzyme | Xenopus laevis | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.17.3 | 5 | - |
with substrate hippuric acid | Xenopus laevis |
| 1.14.17.3 | 6 | - |
with substrate N-trinitrophenyl-D-Tyr-Val-Gly | Xenopus laevis |
| 1.14.17.3 | 7.5 | - |
with substrate D-Tyr-Val-Gly | Xenopus laevis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.17.3 | ascorbate | - |
Xenopus laevis | |
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