Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
procollagen L-proline + 2-oxoglutarate + O2 | Mus musculus | P3H1 catalyzes the 3-hydroxylation of specific proline residues in procollagen I | procollagen trans-3-hydroxy-L-proline + succinate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
bone | - |
Mus musculus | - |
chondrocyte | - |
Mus musculus | - |
skin | - |
Mus musculus | - |
tendon | - |
Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
procollagen L-proline + 2-oxoglutarate + O2 | P3H1 catalyzes the 3-hydroxylation of specific proline residues in procollagen I | Mus musculus | procollagen trans-3-hydroxy-L-proline + succinate + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
P3H1 | - |
Mus musculus |
prolyl 3-hydroxylase 1 | - |
Mus musculus |
General Information | Comment | Organism |
---|---|---|
additional information | importance of P3H1 to bone structure and development. Mutations in the gene encoding for prolyl 3-hydroxylase 1 can cause a severe, recessive form of osteogenesis imperfecta, a skeletal disorder, minimal 3-hydroxylation of key proline residues in type I collagen as a result of P3H1 deficiency. Prolyl 3-hydroxylase 1 null mice display abnormalities in fibrillar collagen-rich tissues such as tendons, skin, and bones, e.g. abnormalities in collagen fibril ultrastructure in tendons, and alterations in skin architecture, as well as in developing limbs, phenotypes, detailed overview. Collagen secretion rate is decreased in P3H1 null fibroblasts | Mus musculus |