Cloned (Comment) | Organism |
---|---|
- |
Rattus norvegicus |
Protein Variants | Comment | Organism |
---|---|---|
Y318F | site-directed mutagenesis, active site residue mutant, slightly reduced rate constant for C-H bond cleavage compared to the wild-type enzyme | Rattus norvegicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
hippuric acid | - |
Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | competitive and noncompetitive kinetic isotope effects in wild-type enzyme and mutant Y318F, kinetic mechanism | Rattus norvegicus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | required, reductive activation of Cu(II)-OOH to generate a reactive copper-oxo species | Rattus norvegicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O | equilibrium-ordered and steady-state-random or -ordered reaction mechanism for the wild-type and the mutant Y318F enzyme, respectively, active site Y318 is involved, C-H bond activation is dominated by quantum mechanical tunneling, peptide substrate binding structure at the active site | Rattus norvegicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
hippuric acid + ascorbate + O2 | C-H bond cleavage is irreversible, protiated and dideuterated substrate | Rattus norvegicus | ? + dehydroascorbate + H2O | - |
ir | |
peptidylglycine + ascorbate + O2 | C-H bond cleavage is irreversible, activation of molecular O2 and of the C-H bond of the substrate, mechanism, reductive activation of Cu(II)-OOH to generate a reactive copper-oxo species | Rattus norvegicus | peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
ir |
Synonyms | Comment | Organism |
---|---|---|
peptidylglycine alpha-hydroxylating monooxygenase | - |
Rattus norvegicus |
PHM | - |
Rattus norvegicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Rattus norvegicus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | intrinsic rate constants for wild-type and mutant Y318F enzyme | Rattus norvegicus | |
13.6 | - |
hippuric acid | pH 6.0, 37°C, [2H2]-hippuric acid, mutant Y318F | Rattus norvegicus | |
25 | - |
hippuric acid | pH 6.0, 37°C, [2H2]-hippuric acid, wild-type enzyme | Rattus norvegicus | |
27.6 | - |
hippuric acid | pH 6.0, 37°C, [1H2]-hippuric acid, mutant Y318F | Rattus norvegicus | |
39.1 | - |
hippuric acid | pH 6.0, 37°C, [1H2]-hippuric acid, wild-type enzyme | Rattus norvegicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
assay at | Rattus norvegicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ascorbate | - |
Rattus norvegicus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
2.9 | - |
hippuric acid | pH 6.0, 37°C, [1H2]-hippuric acid, wild-type enzyme | Rattus norvegicus | |
4.5 | - |
hippuric acid | pH 6.0, 37°C, [2H2]-hippuric acid, wild-type enzyme | Rattus norvegicus | |
7 | - |
hippuric acid | pH 6.0, 37°C, [2H2]-hippuric acid, mutant Y318F | Rattus norvegicus | |
22 | - |
hippuric acid | pH 6.0, 37°C, [1H2]-hippuric acid, mutant Y318F | Rattus norvegicus |