Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes in Escherichia coli strain Origami DE3 | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
D414A | site-directed mutagenesis, the mutation mimics the active site of a halogenase. The substitutions does not convert P4H into a halogenase, but the hydroxylase activity of D414A P4H cannot be rescued with small molecule, the mutant is inactive | Homo sapiens |
D414G | site-directed mutagenesis, the mutation mimics the active site of a halogenase. The substitutions does not convert P4H into a halogenase, but the hydroxylase activity of D414A P4H cannot be rescued with small molecule, the mutant is inactive | Homo sapiens |
D414H | site-directed mutagenesis, the mutation mimics the active site of a cysteine dioxygenase, the mutant is inactive | Homo sapiens |
D414H/H483D | site-directed mutagenesis, the mutant is inactive | Homo sapiens |
H412D/D414H | site-directed mutagenesis, the mutant is inactive | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
potassium bromide | over 80% inhibition at 500 mM | Homo sapiens | |
potassium chloride | over 80% inhibition at 500 mM | Homo sapiens | |
potassium fluoride | over 90% inhibition at 500 mM | Homo sapiens | |
potassium iodide | over 80% inhibition at 500 mM | Homo sapiens | |
sodium bromide | over 80% inhibition at 500 mM | Homo sapiens | |
sodium chloride | over 80% inhibition at 500 mM | Homo sapiens | |
sodium iodide | over 90% inhibition at 500 mM | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | required cofactor, residues His412, Asp414, and His483 form an iron-coordinating 2-His-1-carboxylate motif, high stringency for the iron-binding residues in the P4H active site, mechanism, overview | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
procollagen L-proline + 2-oxoglutarate + O2 | Homo sapiens | P4H catalyzes the post-translational hydroxylation of proline residues in protocollagen strands, stabilizing the ensuing triple helix | procollagen trans-4-hydroxy-L-proline + succinate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes from Escherichia coli strain Origami DE3 | Homo sapiens |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 | reaction mechanism with Fe2+ bound in the active site by a 2-His-1-Asp motif, overview | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
procollagen L-proline + 2-oxoglutarate + O2 | P4H catalyzes the post-translational hydroxylation of proline residues in protocollagen strands, stabilizing the ensuing triple helix | Homo sapiens | procollagen trans-4-hydroxy-L-proline + succinate + CO2 | - |
? | |
procollagen L-proline + 2-oxoglutarate + O2 | high stringency for the iron-binding residues in the P4H active site, structure-function relationship, overview | Homo sapiens | procollagen trans-4-hydroxy-L-proline + succinate + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | alpha2beta2, catalytic alpha subunit | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
More | the enzyme belongs to the alpha-ketoglutarate-dependent iron(II) dioxygenases | Homo sapiens |
P4H | - |
Homo sapiens |
prolyl 4-hydroxylase | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.8 | - |
assay at | Homo sapiens |