Cloned (Comment) | Organism |
---|---|
expression from HeLa cell lines and from transient HEK293 cells | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
sitting drop vapor diffusion method, crystal structures of full-length human LH3 in complex with cofactors and donor substrates provide a molecular understanding of the biochemical knowledge underlying the multiple functions of this enzyme | Homo sapiens |
structures of full-length human LH3 in complex with cofactors and donor substrates. LH3 has three domains encompassing multiple catalytic sites and forms elongated tail-to-tail dimers showing two distinct catalytic sites at the N- and C-terminal boundaries of each monomer. The glycosyltransferase domain displays distinguishing features compared to other known glycosyltransferases. Known disease-related mutations map in close proximity to the catalytic sites | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | contributes to the overall enzyme stabilization, enzymatic activity peaks at 25 microM Fe2+ | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-alpha-D-galactose + [procollagen]-(5R)-5-hydroxy-L-lysine | Homo sapiens | - |
UDP + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O60568 | - |
- |
Homo sapiens | O60568 | multifunctional, catalyzes reactions of EC 1.14.11.4, EC 2.4.1.50, EC 2.4.1.66 | - |
Purification (Comment) | Organism |
---|---|
- |
Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-alpha-D-galactose + [procollagen]-(5R)-5-hydroxy-L-lysine | - |
Homo sapiens | UDP + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine | - |
? | |
UDP-alpha-D-galactose + [procollagen]-(5R)-5-hydroxy-L-lysine | human lysyl hydroxylase 3 (LH3/PLOD3) is a multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3. Two distinct catalytic sites at the N- and C-terminal boundaries of each monomer are separated by an accessory domain. Collagen glucosyltransferase (EC 2.4.1.66) and procollagen galactosyltransferase (EC 2.4.1.50) activities localize at the N-terminus of the enzyme, whereas the lysyl hydroxylase activity (EC 1.14.11.4) is segregated at the LH3 C-terminus | Homo sapiens | UDP + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | two distinct catalytic sites at the N- and C-terminal boundaries of each monomer are separated by an accessory domain. Dimerization is essential for lysyl hydroxylase activity, whereas disruption of physiological dimers does not significantly perturb the N-terminal glycosyltransferase activities of LH3 | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
LH3 | - |
Homo sapiens |
LH3/PLOD3 | - |
Homo sapiens |
multifunctional procollagen lysine hydroxylase and glycosyltransferase | - |
Homo sapiens |
PLOD3 | - |
Homo sapiens |