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Literature summary for 1.14.11.69 extracted from

  • Hillringhaus, L.; Yue, W.W.; Rose, N.R.; Ng, S.S.; Gileadi, C.; Loenarz, C.; Bello, S.H.; Bray, J.E.; Schofield, C.J.; Oppermann, U.
    Structural and evolutionary basis for the dual substrate selectivity of human KDM4 histone demethylase family (2011), J. Biol. Chem., 286, 41616-41625 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.11.69

Cloned(Commentary)

Cloned (Comment) Organism
gene KDM4A, phylogenetic analysis, recombinant expression of N-terminally His-tagged KDM4A catalytic domain in Escherichia coli Homo sapiens
gene KDM4B, phylogenetic analysis, recombinant expression of N-terminally His-tagged KDM4B catalytic domain in Escherichia coli Homo sapiens
gene KDM4C, phylogenetic analysis, recombinant expression of N-terminally His-tagged KDM4C catalytic domain in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme in complex with inhibitor, sitting drop vapor diffusion method, mixing of 7 mg/ml protein and 2 mM N-oxalylglycine with well solution, containing 25% v/v PEG 3350, 0.2 M sodium nitrate, 0.1 M bis-tris propane, pH 6.5, 5% v/v ethylene glycol, 0.01 M NiCl2, in a 2:1 ratio, 4°C, X-ray diffraction structure determination and analysis at 2.55 A resolution Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
-
 Homo sapiens 5634
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required Homo sapiens
Zn2+ comparison of the Zn(II)-binding site Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2 Homo sapiens
-
 [histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
-
 ?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2 Homo sapiens
-
 [histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens O75164
-
-
Homo sapiens O94953
-
-
Homo sapiens Q9H3R0
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His-tagged KDM4A catalytic domain from Escherichia coli Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4A preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides Homo sapiens ?
-
 ?
additional information bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4B preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides Homo sapiens ?
-
 ?
additional information bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4C preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides Homo sapiens ?
-
 ?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
-
 Homo sapiens [histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
-
 ?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2
-
 Homo sapiens [histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
-
 ?

Synonyms

Synonyms Comment Organism
JMJD2A
-
 Homo sapiens
JMJD2B
-
 Homo sapiens
JMJD2C
-
 Homo sapiens
KDM4A
-
 Homo sapiens
KDM4B
-
 Homo sapiens
Kdm4c
-
 Homo sapiens
More see also EC 1.14.11.66 Homo sapiens

General Information

General Information Comment Organism
evolution the enzyme belongs to the KDM4/JmjC demethylase histone demethylase family. The selectivity of KDM4 enzymes is determined by multiple interactions within the catalytic domain but outside the active site. All KDM4 subfamily members have highly conserved residues lining the methylammonium-binding pocket. The exceptions are Ser288A/Ser-289B/Ser290C and Thr289A/Thr290B/Thr291C in KDM4A, B, and C, which are substituted by Ala287D/Ala289E/Ala286F and Ile288D/Ile290E/Ile287F in KDM4D-F, respectively. Evolutionary analysis of the KDM4 demethylase subfamily Homo sapiens
evolution the enzyme belongs to the KDM4/JmjC demethylase histone demethylase family. The selectivity of KDM4 enzymes is determined by multiple interactions within the catalytic domain but outside the active site. Evolutionary analysis of the KDM4 demethylase subfamily Homo sapiens
additional information enzyme structure-function relationships and substrate selectivity, comparisons of KDM4 enzymes, overview Homo sapiens