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Literature summary for 1.14.11.7 extracted from
- Prolyl 3-hydroxylase: partial characterization of the enzyme from rat kidney cortex (1977), Eur. J. Biochem., 73, 485-492.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | required | Rattus norvegicus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Rattus norvegicus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| kidney | cortex | Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| procollagen L-proline + 2-oxoglutarate + O2 | chicken embryo tendon protocollagen and procollagen or cartilage protocollagen. The formation of 3-hydroxyproline is affected by chain length and the conformation of the substrate, in that longer polypeptide chains proved better substrates, while the native triple-helical conformation of protocollagen or procollagen completely prevents the reaction | Rattus norvegicus | procollagen trans-3-hydroxy-L-proline + succinate + CO2 | - |
? | |
| protocollagen containing 4-hydroxyproline + 2-oxoglutarate + O2 | - |
Rattus norvegicus | ? | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | - |
- |
Rattus norvegicus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ascorbate | required | Rattus norvegicus | |
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Release 2023.1 (January 2023)
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