EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.14.11.2 | cysteine | activation | Gallus gallus | |
1.14.11.2 | cysteine | activation | Homo sapiens | |
1.14.11.2 | dithiothreitol | activation | Gallus gallus | |
1.14.11.2 | dithiothreitol | activation | Homo sapiens |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.11.2 | preparation of cDNA clones for the two subunits, expression in Escherichia coli | Homo sapiens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.11.2 | 2,3-Dihydroxybenzoate | - |
Gallus gallus | |
1.14.11.2 | 2,3-Dihydroxybenzoate | - |
Homo sapiens | |
1.14.11.2 | 3,4-dihydroxybenzoate | - |
Gallus gallus | |
1.14.11.2 | 3,4-dihydroxybenzoate | - |
Homo sapiens | |
1.14.11.2 | 3,4-Dihydroxyphenylacetate | - |
Gallus gallus | |
1.14.11.2 | 3,4-Dihydroxyphenylacetate | - |
Homo sapiens | |
1.14.11.2 | 4-hydroxybenzoate | - |
Gallus gallus | |
1.14.11.2 | 4-hydroxybenzoate | - |
Homo sapiens | |
1.14.11.2 | Cu2+ | - |
Gallus gallus | |
1.14.11.2 | Cu2+ | - |
Homo sapiens | |
1.14.11.2 | glutamyl-3,4-dehydroprolyl-bradykinin | - |
Gallus gallus | |
1.14.11.2 | glutamyl-3,4-dehydroprolyl-bradykinin | - |
Homo sapiens | |
1.14.11.2 | hydroxybenzene | - |
Gallus gallus | |
1.14.11.2 | poly(L-proline) | - |
Gallus gallus | |
1.14.11.2 | poly(L-proline) | - |
Homo sapiens | |
1.14.11.2 | poly(L-proline) | - |
Mus musculus | |
1.14.11.2 | Pyridine 2,4-dicarboxylate | - |
Gallus gallus | |
1.14.11.2 | Pyridine 2,4-dicarboxylate | - |
Homo sapiens | |
1.14.11.2 | Pyridine 2,4-dicarboxylate | - |
Mus musculus | |
1.14.11.2 | Pyridine 2,5-dicarboxylate | - |
Gallus gallus | |
1.14.11.2 | Pyridine 2,5-dicarboxylate | - |
Homo sapiens | |
1.14.11.2 | pyridine 2-carboxylate | - |
Gallus gallus | |
1.14.11.2 | Zn2+ | - |
Gallus gallus | |
1.14.11.2 | Zn2+ | - |
Homo sapiens |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.11.2 | Fe2+ | - |
Gallus gallus | |
1.14.11.2 | Fe2+ | - |
Mus musculus | |
1.14.11.2 | Fe2+ | - |
Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.3.4.1 | Proteins | Homo sapiens | native, reduced or with wrong disulfide bonds | ? | - |
? | |
5.3.4.1 | Proteins | Gallus gallus | may play a role in retaining prolyl 4-hydroxylase in its native conformation | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.11.2 | Gallus gallus | - |
- |
- |
1.14.11.2 | Homo sapiens | - |
- |
- |
1.14.11.2 | Mus musculus | - |
- |
- |
5.3.4.1 | Gallus gallus | - |
- |
- |
5.3.4.1 | Homo sapiens | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
1.14.11.2 | glycoprotein | carbohydrate composition | Gallus gallus |
1.14.11.2 | glycoprotein | carbohydrate composition | Homo sapiens |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.14.11.2 | isolation of subunits | Gallus gallus |
1.14.11.2 | using affinity chromatography, ion-exchange chromatography and gel filtration | Gallus gallus |
1.14.11.2 | using affinity chromatography, ion-exchange chromatography and gel filtration | Homo sapiens |
5.3.4.1 | - |
Gallus gallus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.14.11.2 | embryo | - |
Gallus gallus | - |
1.14.11.2 | liver | - |
Gallus gallus | - |
1.14.11.2 | liver | - |
Mus musculus | - |
1.14.11.2 | liver | - |
Homo sapiens | - |
1.14.11.2 | placenta | - |
Homo sapiens | - |
5.3.4.1 | cartilage | embryonal | Gallus gallus | - |
5.3.4.1 | embryo | - |
Gallus gallus | - |
5.3.4.1 | fibroblast | cultured, confluent | Homo sapiens | - |
5.3.4.1 | fibroblast | lung | Homo sapiens | - |
5.3.4.1 | skin fibroblast | cultured, confluent | Homo sapiens | - |
5.3.4.1 | tendon | embryonal | Gallus gallus | - |
5.3.4.1 | WI-38 cell | SV40 transformed, cultured, confluent, weak activity | Homo sapiens | - |
EC Number | Storage Stability | Organism |
---|---|---|
5.3.4.1 | -20°C, stable for several months | Gallus gallus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.11.2 | proline containing peptide + 2-oxoglutarate + O2 | the presence of 2-oxoglutarate is an absolute and highly specific requirement, the formation of 4-hydroxyproline is accompanied by a stoichiometric decarboxylation of 2-oxoglutarate, the oxygen of the hydroxyl group is derived from molecular oxygen, the other atom of the O2 molecule being incorporated into the succinate, the activated form of oxygen is probably superoxide | Gallus gallus | 4-hydroxyproline containing peptide + succinate + CO2 | - |
? | |
1.14.11.2 | proline containing peptide + 2-oxoglutarate + O2 | the presence of 2-oxoglutarate is an absolute and highly specific requirement, the formation of 4-hydroxyproline is accompanied by a stoichiometric decarboxylation of 2-oxoglutarate, the oxygen of the hydroxyl group is derived from molecular oxygen, the other atom of the O2 molecule being incorporated into the succinate, the activated form of oxygen is probably superoxide | Homo sapiens | 4-hydroxyproline containing peptide + succinate + CO2 | - |
? | |
5.3.4.1 | Proteins | native, reduced or with wrong disulfide bonds | Gallus gallus | Proteins | with correct disulfide bonds | ? | |
5.3.4.1 | Proteins | native, reduced or with wrong disulfide bonds | Homo sapiens | Proteins | with correct disulfide bonds | ? | |
5.3.4.1 | Proteins | incorrectly disulfide-linked bovine pancreatic ribonuclease | Gallus gallus | Proteins | with correct disulfide bonds | ? | |
5.3.4.1 | Proteins | native, reduced or with wrong disulfide bonds | Homo sapiens | ? | - |
? | |
5.3.4.1 | Proteins | may play a role in retaining prolyl 4-hydroxylase in its native conformation | Gallus gallus | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.14.11.2 | tetramer | fibroblasts, SDS-PAGE, due to a larger carbohydrate content the alpha-subunit also exists in larger forms | Gallus gallus |
1.14.11.2 | tetramer | newborn, SDS-PAGE, due to a larger carbohydrate content the alpha-subunit also exists in larger forms | Mus musculus |
1.14.11.2 | tetramer | liver, SDS-PAGE, due to a larger carbohydrate content the alpha-subunit also exists in larger forms | Homo sapiens |
1.14.11.2 | tetramer | alpha2 beta2, alpha: 64000, beta: 60000, ratio 1 to 1, SDS-PAGE | Gallus gallus |
1.14.11.2 | tetramer | alpha2 beta2, alpha: 64000, beta: 60000, ratio 1 to 1, SDS-PAGE | Homo sapiens |
1.14.11.2 | tetramer | there are two forms of the alpha subunit | Gallus gallus |
1.14.11.2 | tetramer | there are two forms of the alpha subunit | Mus musculus |
1.14.11.2 | tetramer | there are two forms of the alpha subunit | Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.11.2 | ascorbate | - |
Mus musculus | |
1.14.11.2 | ascorbate | highly specific for | Gallus gallus | |
1.14.11.2 | ascorbate | highly specific for | Homo sapiens | |
1.14.11.2 | ascorbate | oxygen acceptor in the decarboxylation of 2-oxoglutarate without subsequent hydroxylation of peptide substrate | Gallus gallus | |
1.14.11.2 | ascorbate | oxygen acceptor in the decarboxylation of 2-oxoglutarate without subsequent hydroxylation of peptide substrate | Homo sapiens |