EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.11.4 | transient transfection of HA-tagged LH1 in 714 mouse embryonic fibroblasts | Mus musculus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.11.4 | additional information | the endoplasmic reticulum complex including SC65 and prolyl 3-hydroxylase 3affects the activity of lysyl-hydroxylase 1 potentially through interactions with the enzyme and/or cyclophilin B. Loss of Sc65 in the mouse results in instability of this complex, altered collagen lysine hydroxylation and cross-linking leading to connective tissue defects that include low bone mass and skin fragility, while it has no effect on prolyl 3-hydroxylation. CRTAP, a non-enzymic member of the Leprecan family of proteins which includes Synaptonemal Complex 65 (SC65) and the prolyl 3-hydroxylases (P3H1, P3H2 and P3H3), is an essential third subunit of a complex with prolyl 3-hydroxylase 1 (aka LEPRECAN) and cyclophilin B (CYPB) in the endoplasmic reticulum, forming the so-called collagen prolyl 3-hydroxylation complex | Mus musculus | |
1.14.11.4 | SC65 | directly interacts with lysyl-hydroxylase 1, LH1 | Mus musculus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.14.11.4 | endoplasmic reticulum | - |
Mus musculus | 5783 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.11.4 | [procollagen]-L-lysine + 2-oxoglutarate + O2 | Mus musculus | - |
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2 | - |
? | |
1.14.11.4 | [procollagen]-L-lysine + 2-oxoglutarate + O2 | Mus musculus 714 | - |
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.11.4 | Mus musculus | Q9R0E2 | - |
- |
1.14.11.4 | Mus musculus 714 | Q9R0E2 | - |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.14.11.4 | bone | - |
Mus musculus | - |
1.14.11.4 | fibroblast | skin and embryonic | Mus musculus | - |
1.14.11.4 | osteoblast | primary calvarial | Mus musculus | - |
1.14.11.4 | skin | - |
Mus musculus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.11.4 | [procollagen]-L-lysine + 2-oxoglutarate + O2 | - |
Mus musculus | [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2 | - |
? | |
1.14.11.4 | [procollagen]-L-lysine + 2-oxoglutarate + O2 | - |
Mus musculus 714 | [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.11.4 | LH1 | - |
Mus musculus |
1.14.11.4 | lysyl-hydroxylase 1 | - |
Mus musculus |
1.14.11.4 | Plod1 | - |
Mus musculus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.11.4 | malfunction | mice with loss of function of Leprel2 (encoding P3H3) have the same loss of tissue type I collagen lysine-hydroxylation as that observed in the Sc65 knockout mice. Loss of Sc65 in the mouse results in instability of this complex, altered collagen lysine hydroxylation and cross-linking leading to connective tissue defects that include low bone mass and skin fragility, while it has no effect on prolyl 3-hydroxylation. Sc65KO mouse generation and confirmation of bone loss phenotype, overview | Mus musculus |
1.14.11.4 | metabolism | the endoplasmic reticulum complex including SC65 and prolyl 3-hydroxylase 3 affects the activity of lysyl-hydroxylase 1 potentially through interactions with the enzyme and/or cyclophilin B. The prolyl-hydroxylase complex in the endoplasmic reticulum controls lysyl-hydroxylase activity during collagen synthesis. SC65/LH1/P3H3 are interlinked within a protein complex in the endoplasmic reticulum | Mus musculus |
1.14.11.4 | physiological function | in the endoplasmic reticulum, specific proline and lysine residues of newly translated procollagen chains are modified by prolyl- and lysyl-hydroxylases, respectively. These enzymes share a highly conserved catalytic 2-oxoglutarate, ascorbate- and Fe(II)-dependent dioxygenase domain | Mus musculus |