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Literature summary for 1.14.11.4 extracted from
- Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6 (2010), J. Mol. Biol., 401, 211-222.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| ascorbic acid | - |
Homo sapiens |  |
| DTT | - |
Homo sapiens | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of His-tagged full-length JMJD6 and JMJD61-343 in Escherichia coli strain Rosetta | Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant His-tagged SeMet-derivatised and wild-type JMJD61-343, at both 20°C and 4°C by the sitting drop vapour diffusion method, X-ray diffraction structure determination and analysis at 1.75-2.0 A resolution | Homo sapiens |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | dependent on, binding site structure, overview | Homo sapiens | |
| Ni2+ | can substitute for Fe2+ | Homo sapiens | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 42000 | - |
x * 42000, recombinant His-tagged catalytic domain of JMJD6, residues 1-343 | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | JMJD6 catalyses the iron- and 2-oxoglutarate-dependent hydroxylation of lysyl residues in arginine-serine-rich domains of RNAsplicing-related proteins. It catalyses C5 hydroxylation rather than Nepsilon demethylation | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q6NYC1 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged full-length JMJD6 and JMJD61-343 from Escherichia coli strain Rosetta by nickel affinity chromatography | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| luc7like2(267-278) + 2-oxoglutarate | substrate is a Luc7like2 protein fragment | Homo sapiens | ? + succinate + CO2 | - |
? | |
| additional information | JMJD6 catalyses the iron- and 2-oxoglutarate-dependent hydroxylation of lysyl residues in arginine-serine-rich domains of RNAsplicing-related proteins. It catalyses C5 hydroxylation rather than Nepsilon demethylation | Homo sapiens | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 42000, recombinant His-tagged catalytic domain of JMJD6, residues 1-343 | Homo sapiens |
| More | structure of the catalytic domain of recombinant His-tagged JMJD6 and active site structure, overview | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Jmjd6 | - |
Homo sapiens |
| lysyl hydroxylase | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Homo sapiens |
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Release 2023.1 (January 2023)
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