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ENZYME entry: EC 1.14.11.65

Accepted Name
[Histone H3]-dimethyl-L-lysine(9) demethylase.
Reaction catalysed
A [histone H3]-N(6),N(6)-dimethyl-L-lysine(9) + 2 2-oxoglutarate + 2 O(2) <=> a [histone H3]-L-lysine(9) + 2 succinate + 2 formaldehyde + 2 CO(2)
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
UniProtKB/Swiss-Prot
O43593, HAIR_HUMAN;  Q61645, HAIR_MOUSE;  P97609, HAIR_RAT;  
Q6IRB8, KD3AA_XENLA;  Q5HZN1, KD3AB_XENLA;  Q5ZIX8, KDM3A_CHICK;  
Q9Y4C1, KDM3A_HUMAN;  Q6PCM1, KDM3A_MOUSE;  Q63679, KDM3A_RAT;  
Q7LBC6, KDM3B_HUMAN;  Q6ZPY7, KDM3B_MOUSE;  P0CH95, PHF8_DANRE;  
Q9UPP1, PHF8_HUMAN;  Q80TJ7, PHF8_MOUSE;  

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