Literature summary for 1.14.11.4 extracted from

  • Mantri, M.; Krojer, T.; Bagg, E.A.; Webby, C.J.; Butler, D.S.; Kochan, G.; Kavanagh, K.L.; Oppermann, U.; McDonough, M.A.; Schofield, C.J.
    Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6 (2010), J. Mol. Biol., 401, 211-222.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
DTT
-
Homo sapiens
ascorbic acid
-
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
Ni2+ can substitute for Fe2+ Homo sapiens
Fe2+ dependent on, binding site structure, overview 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