Any feedback?
Literature summary for 1.14.11.2 extracted from
- Tetramers and monomers of prolyl hydroxylase in isolated chick-embryo tendon cells. The association of inactive monomers to active tetramers and a preliminary characterization of the intracellular monomer-size protein (1977), Eur. J. Biochem., 78, 547-556.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| bovine serum albumin | activation | Gallus gallus | |
| catalase | activation | Gallus gallus | |
| dithiothreitol | activation | Gallus gallus |  |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| dithiothreitol | 95-100% inhibition at 0.45 mM | Gallus gallus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | - |
Gallus gallus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Gallus gallus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| embryo | - |
Gallus gallus | - |
| tendon | embryo | Gallus gallus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
specific activity of the enzyme in the presence and absence of dithiothreitol | 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 | ? | |
| additional information | thermal denaturing of the triple-helical conformation of the substrate before hydroxylation | Gallus gallus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | about 65% of the enzyme is present in the form of active enzyme tetramers, and about 35% in a form corresponding in molecular weight to the enzyme monomers when studied by gel filtration. The monomer-size protein in the cell represents, at least in part, precursors of the enzyme tetramers, and it can be associated to active tetramers after its ribosomal biosynthesis | Gallus gallus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Gallus gallus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ascorbate | - |
Gallus gallus | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
