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ENZYME

ENZYME entry: EC 1.14.11.65

Accepted Name
[histone H3]-dimethyl-L-lysine(9) demethylase
Reaction catalysed
2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + 2 O2 <=> 2 CO2 + 2 formaldehyde + L-lysyl(9)-[histone H3] + 2 succinate
Comment(s)
  • Requires iron(II).
  • This entry describes a group of enzymes that demethylate N-methylated Lys-9 residues in the tail of the histone protein H3 (H3K9).
  • This lysine residue can exist in three methylation states (mono-, di- and trimethylated), but this group of enzymes only act on the the di- and mono-methylated forms.
  • The enzymes are dioxygenases and act by hydroxylating the methyl group, forming an unstable hemiaminal that leaves as formaldehyde, cf. EC 1.14.11.66.
Cross-references
BRENDA1.14.11.65
EC2PDB1.14.11.65
ExplorEnz1.14.11.65
PRIAM enzyme-specific profiles1.14.11.65
KEGG Ligand Database for Enzyme Nomenclature1.14.11.65
IUBMB Enzyme Nomenclature1.14.11.65
IntEnz1.14.11.65
MEDLINEFind literature relating to 1.14.11.65
MetaCyc1.14.11.65
Rhea expert-curated reactions1.14.11.65
UniProtKB/Swiss-Prot
O43593, HAIR_HUMANQ61645, HAIR_MOUSEP97609, HAIR_RAT
Q9SSE9, JMJ25_ARATHQ8VYB9, JMJ27_ARATHQ6IRB8, KD3AA_XENLA
Q5HZN1, KD3AB_XENLAQ5ZIX8, KDM3A_CHICKQ9Y4C1, KDM3A_HUMAN
Q6PCM1, KDM3A_MOUSEQ63679, KDM3A_RATQ7LBC6, KDM3B_HUMAN
Q6ZPY7, KDM3B_MOUSEQ6ZMT4, KDM7A_HUMANQ3UWM4, KDM7A_MOUSE
P0CH95, PHF8_DANREQ9UPP1, PHF8_HUMANQ80TJ7, PHF8_MOUSE

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