Protein Variants | Comment | Organism |
---|---|---|
D669A | site-directed mutagenesis, inactive mutant | Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
adiponectin-L-lysine + 2-oxoglutarate + O2 | Mus musculus | - |
adiponectin-5-hydroxy-L-lysine + succinate + CO2 | - |
? | |
adiponectin-L-lysine + 2-oxoglutarate + O2 | Mus musculus C57BL/6 | - |
adiponectin-5-hydroxy-L-lysine + succinate + CO2 | - |
? | |
mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2 | Mus musculus | C-terminally FLAG-tagged rat MBL-A | mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2 | - |
? | |
mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2 | Mus musculus C57BL/6 | C-terminally FLAG-tagged rat MBL-A | mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2 | - |
? | |
[procollagen]-L-lysine + 2-oxoglutarate + O2 | Mus musculus | - |
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2 | - |
? | |
[procollagen]-L-lysine + 2-oxoglutarate + O2 | Mus musculus C57BL/6 | - |
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q9R0E1 | - |
- |
Mus musculus C57BL/6 | Q9R0E1 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
adiponectin-L-lysine + 2-oxoglutarate + O2 | - |
Mus musculus | adiponectin-5-hydroxy-L-lysine + succinate + CO2 | - |
? | |
adiponectin-L-lysine + 2-oxoglutarate + O2 | - |
Mus musculus C57BL/6 | adiponectin-5-hydroxy-L-lysine + succinate + CO2 | - |
? | |
mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2 | C-terminally FLAG-tagged rat MBL-A | Mus musculus | mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2 | - |
? | |
mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2 | purified recombinant C-terminally FLAG-tagged MBL-A from Rattus norvegicus | Mus musculus | mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2 | - |
? | |
mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2 | C-terminally FLAG-tagged rat MBL-A | Mus musculus C57BL/6 | mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2 | - |
? | |
mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2 | purified recombinant C-terminally FLAG-tagged MBL-A from Rattus norvegicus | Mus musculus C57BL/6 | mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2 | - |
? | |
[procollagen]-L-lysine + 2-oxoglutarate + O2 | - |
Mus musculus | [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2 | - |
? | |
[procollagen]-L-lysine + 2-oxoglutarate + O2 | - |
Mus musculus C57BL/6 | [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
LH3 | - |
Mus musculus |
lysyl hydroxylase 3 | - |
Mus musculus |
General Information | Comment | Organism |
---|---|---|
malfunction | LH3 knockout studies in mice demonstrate that the loss of LH3 leads to embryonic lethality due to disruption in the formation of basement membranes. The absence of LH3 glycosyltransferase activities are responsible for the lethality. The lack of LH3 leads to loss of all Glc-Gal-Hyl residues in collagens I, IV and VI and prevents the assembly and secretion of type IV and VI collagens. In addition, the mutated LH activity, one out of three activities of LH3, leads to underglycosylation of collagen IV and VI, which is detected as abnormal distribution and aggregation of these collagens in mouse tissues. Oligomerization of recombinant MBL-A is defective in LH3-/- knockout MEF cells | Mus musculus |
physiological function | LH3 is essential for catalyzing formation of the glucosylgalactosylhydroxylysines of mannan-binding lectin-A (MBL-A), the first component of the lectin pathway of complement activation. LH3 catalyzes formation of Glc-Gal-Hyl residues in collagens and in collagenous domain of adiponectin. Similar lysine modifications are also present in MBL-A. LH3 also modifies the lysine residues in the collagenous domain of adiponectin, an insulin-sensitizing hormone, and thus affects the oligomerization and secretion of adiponectin | Mus musculus |