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Literature summary extracted from
- Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3: The 30-kDa N-terminal fragment is not required for lysyl hydroxylase activity (2002), J. Biol. Chem., 277, 23084-23091.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.11.4 | expression in insect cells using a baculovirus vector | Homo sapiens |
| 2.4.1.66 | full-length LH3 and the N-terminal 30 kDa fragment A with GGT activity is cloned, sequenced and expressed in High Five insect cells | Homo sapiens |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.11.4 | 0.1 | - |
2-oxoglutarate | lysyl hydroxylase 3 | Homo sapiens |  |
| 1.14.11.4 | 0.12 | - |
2-oxoglutarate | lysyl hydroxylase 1 | Homo sapiens | |
| 1.14.11.4 | 0.35 | - |
ascorbate | lysyl hydroxylases 1 and 3 | Homo sapiens | |
| 1.14.11.4 | 0.4 | - |
(Ile-Lys-Gly)3 | lysyl hydroxylase 1 | Homo sapiens | |
| 1.14.11.4 | 0.43 | - |
(L-Ile-L-Lys-Gly)3 | lysyl hydroxylase 3 | Homo sapiens | |
| 2.4.1.66 | additional information | - |
additional information | Km: 4 mg/ml, denatured citrate soluble rat skin collagen | Homo sapiens | |
| 2.4.1.66 | 0.15 | - |
UDP-glucose | recombinant LH3/GGT | Homo sapiens | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.11.4 | Fe2+ | required, Km: 0.001-0.005 mM | Homo sapiens | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.14.11.4 | 180000 | - |
gel filtration, isoforms 1-3 | Homo sapiens |
| 2.4.1.66 | 180000 | - |
LH3 with GGT activity, gel filtration | Homo sapiens |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.11.4 | collagen + 2-oxoglutarate + O2 | Homo sapiens | enzyme required during collagen biosynthesis | 5-hydroxylysyl-collagen + succinate + CO2 | - |
? | |
| 1.14.11.4 | collagen + 2-oxoglutarate + O2 | Homo sapiens | influence the integrity and stability of collagen | 5-hydroxylysyl-collagen + succinate + CO2 | - |
? | |
| 2.4.1.66 | additional information | Homo sapiens | there must be an additional glucosyltransferase to LH3 that is responsible for most of the collagen glucosylation in vivo | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.11.4 | Homo sapiens | - |
three isoenzymes | - |
| 2.4.1.66 | Homo sapiens | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 1.14.11.4 | side-chain modification | hydroxylation of lysyl residue in -X-Lys-Gly | Homo sapiens |
| 2.4.1.66 | additional information | structural domain fragment A of LH3 with GGT activity contains 2 N-glycosylation sites | Homo sapiens |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.11.4 | three recombinant isoenzymes | Homo sapiens |
| 2.4.1.66 | His-tagged recombinant LH3/GGT/GT and N-terminal 30kDa fragment A of LH3 with GGT activity expressed in High Five insect cells | Homo sapiens |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.14.11.4 | additional information | existence of isoforms | Homo sapiens | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.11.4 | (Ile-Lys-Gly)3 + 2-oxoglutarate + O2 | - |
Homo sapiens | (Ile-5-hydroxylyseine-Gly)3 + succinate + CO2 | - |
? | |
| 1.14.11.4 | 2-oxoglutarate + O2 + ascorbate | - |
Homo sapiens | succinate + CO2 + dehydroascorbate + H2O | - |
? | |
| 1.14.11.4 | collagen + 2-oxoglutarate + O2 | enzyme required during collagen biosynthesis | Homo sapiens | 5-hydroxylysyl-collagen + succinate + CO2 | - |
? | |
| 1.14.11.4 | collagen + 2-oxoglutarate + O2 | influence the integrity and stability of collagen | Homo sapiens | 5-hydroxylysyl-collagen + succinate + CO2 | - |
? | |
| 1.14.11.4 | peptidyl-L-lysine + 2-oxoglutarate + O2 | synthetic peptides | Homo sapiens | peptidyl-5-hydroxy-L-lysine + succinate + CO2 | - |
? | |
| 2.4.1.66 | additional information | multifunctional lysyl hydroxylase isoform 3, LH3 protein, possesses lysyl hydroxylase, collagen glucosyltransferase and galactosyltransferase activities | Homo sapiens | ? | - |
? | |
| 2.4.1.66 | additional information | GGT and GT activities reside in the N-terminal 30.4 kDa structural domain fragment A of LH3, which plays no role in hydroxylase activity, only trace amounts of GT activity of LH3 | Homo sapiens | ? | - |
? | |
| 2.4.1.66 | additional information | there must be an additional glucosyltransferase to LH3 that is responsible for most of the collagen glucosylation in vivo | Homo sapiens | ? | - |
? | |
| 2.4.1.66 | UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen | heat-denatured citrate-soluble rat skin collagen | Homo sapiens | UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.11.4 | homodimer | 2 * 80000-85000, SDS-PAGE, isoforms 1-3 | Homo sapiens |
| 2.4.1.66 | homodimer | 2 * 80000-85000, recombinant LH3 with GGT/GT activities, SDS-PAGE | Homo sapiens |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 2.4.1.66 | More | GGT activity is associated with lysyl hydroxylase isoform 3, LH3, EC 1.14.11.4 | Homo sapiens |
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