Literature summary for 1.14.11.69 extracted from

Chen, Z.; Zang, J.; Kappler, J.; Hong, X.; Crawford, F.; Wang, Q.; Lan, F.; Jiang, C.; Whetstine, J.; Dai, S.; Hansen, K.; Shi, Y.; Zhang, G.
Structural basis of the recognition of a methylated histone tail by JMJD2A (2007), Proc. Natl. Acad. Sci. USA, 104, 10818-10823 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant JMJD2A catalytic core complexed with methylated H3K36 peptide substrates (trimethylated H3K36 peptide (H3K36me3) or a monomethylated H3K36 peptide (H3K36me)) in the presence of Fe(II) and N-oxalylglycine, vapor diffusion method at 4°C against a solution containing 200 mM MgCl2, 100 mM Tris, pH 8.5, and 13-15% PEG 5000, X-ray diffraction structure determination and analysis at 2.0 A resolution	Homo sapiens

Crystallization (Comment)

Organism

purified recombinant JMJD2A catalytic core complexed with methylated H3K36 peptide substrates (trimethylated H3K36 peptide (H3K36me3) or a monomethylated H3K36 peptide (H3K36me)) in the presence of Fe(II) and N-oxalylglycine, vapor diffusion method at 4°C against a solution containing 200 mM MgCl2, 100 mM Tris, pH 8.5, and 13-15% PEG 5000, X-ray diffraction structure determination and analysis at 2.0 A resolution

Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
N-oxalylglycine	-	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	required, binding structure determination	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	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
additional information	bifunctional enzyme active on H3K9me3/me2 (EC 1.14.11.66) and on H3K36me3/me2	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,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2	substrate binding structure, overview	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	-	?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2	substrate binding structure, overview	Homo sapiens	[histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2	-	?

Synonyms

Synonyms	Comment	Organism
JMJD2A	-	Homo sapiens
KDM4A	-	Homo sapiens
More	see also EC 1.14.11.66	Homo sapiens

General Information

General Information	Comment	Organism
additional information	interaction between JMJD2A and substrate peptides largely involves the main chains of the enzyme and the peptide. The peptide-binding specificity is primarily determined by the primary structure of the peptide, which explains the specificity of JMJD2A for methylated H3K9 and H3K36 instead of other methylated residues such as H3K27. The specificity for a particular methyl group is affected by multiple factors, such as space and the electrostatic environment in the catalytic center of the enzyme. Mechanisms and specificity of histone demethylation, overview. Residues Q86, N88, D135, and Y175 are involved in the interaction with the peptide, whereas residues Y177, N290, S288, and T289 are involved in methyl group binding. K241 is proposed to recruit the O2 molecule into the catalytic center. Glycine residues at +3 or +4 in the substrate are essential for substrate specificity	Homo sapiens