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Literature summary for 1.14.11.2 extracted from
- Affinity column purification of protocollagen proline hydroxylase from chick embryos and further characterization of the enzyme (1973), J. Biol. Chem., 248, 1175-1182.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| bovine serum albumin | activation | Gallus gallus | |
| catalase | activation | Gallus gallus | |
| dithiothreitol | activation | Gallus gallus |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | - |
Gallus gallus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | - |
Gallus gallus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 230000 | 240000 | sedimentation equilibrium centrifugation | Gallus gallus |
| 350000 | - |
gel filtration | Gallus gallus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Gallus gallus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| using affinity chromatography on a column containing a polypeptide substrate of the enzyme linked to agarose, elution of the enzyme with a second peptide substrate and separation of the enzyme from this peptide by gel filtration | Gallus gallus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| embryo | - |
Gallus gallus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (Pro-Pro-Gly)n + 2-oxoglutarate + O2 | n: 1,5,10 | Gallus gallus | (Pro-4-hydroxy-Pro-Gly)n + succinate + CO2 | n: 1,5,10 | ? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the enzyme is dissociated into both monomers and dimers by either dithiothreitol or mercaptoethanol, indicating that the structural integrity of the enzyme is maintained in part by either intrachain or interchain disulfide bonds | Gallus gallus |
| tetramer | alpha2 beta2, alpha: 64000, beta: 60000, ratio 1 to 1, SDS-PAGE | Gallus gallus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Gallus gallus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| 2-oxoglutarate | - |
Gallus gallus | |
| ascorbate | - |
Gallus gallus | |
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Release 2023.1 (January 2023)
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