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Literature summary for 1.14.11.7 extracted from
- A role for prolyl 3-hydroxylase 2 in post-translational modification of fibril-forming collagens (2011), J. Biol. Chem., 286, 30662-30669.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| chondrosarcoma cell line | high levels of P3H2 mRNA are expressed | Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | results identify a role for P3H2 in 3-hydroxylation of non-A1 proline residues in clade A collagen chains | Rattus norvegicus | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| P3H2 | - |
Rattus norvegicus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | a knockdown of P3H2 protein using RNA interference reduces 3-hydroxylation at Pro-944, Pro-707, and the GPP repeat at the C-terminus of the triple helix but not at Pro-986 of the clade A pNalpha1(II) collagen chain. When P3H2 expression is turned off, 3-hydroxylation at residue Pro-944 in the alpha2(V) chain is lost, and 3Hyp occupancy at Pro-707 in alpha2(V) and alpha2(I) chains is significantly reduced | Rattus norvegicus |
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Release 2023.1 (January 2023)
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