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Literature summary extracted from

  • Risteli, M.; Ruotsalainen, H.; Bergmann, U.; Venkatraman Girija, U.; Wallis, R.; Myllylae, R.
    Lysyl hydroxylase 3 modifies lysine residues to facilitate oligomerization of mannan-binding lectin (2014), PLoS ONE, 9, e113498 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.14.11.4 D669A site-directed mutagenesis, inactive mutant Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.11.4 adiponectin-L-lysine + 2-oxoglutarate + O2 Mus musculus
-
adiponectin-5-hydroxy-L-lysine + succinate + CO2
-
?
1.14.11.4 adiponectin-L-lysine + 2-oxoglutarate + O2 Mus musculus C57BL/6
-
adiponectin-5-hydroxy-L-lysine + succinate + CO2
-
?
1.14.11.4 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
-
?
1.14.11.4 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
-
?
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 C57BL/6
-
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.4 Mus musculus Q9R0E1
-
-
1.14.11.4 Mus musculus C57BL/6 Q9R0E1
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.4 adiponectin-L-lysine + 2-oxoglutarate + O2
-
Mus musculus adiponectin-5-hydroxy-L-lysine + succinate + CO2
-
?
1.14.11.4 adiponectin-L-lysine + 2-oxoglutarate + O2
-
Mus musculus C57BL/6 adiponectin-5-hydroxy-L-lysine + succinate + CO2
-
?
1.14.11.4 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
-
?
1.14.11.4 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
-
?
1.14.11.4 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
-
?
1.14.11.4 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
-
?
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 C57BL/6 [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
?

Synonyms

EC Number Synonyms Comment Organism
1.14.11.4 LH3
-
Mus musculus
1.14.11.4 lysyl hydroxylase 3
-
Mus musculus

General Information

EC Number General Information Comment Organism
1.14.11.4 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
1.14.11.4 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