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ENZYME

ENZYME entry: EC 1.14.11.65

PURL: https://purl.expasy.org/enzyme/EC/1.14.11.65
Accepted Name
[histone H3]-dimethyl-L-lysine(9) demethylase
Reaction catalysed
N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + 2 2-oxoglutarate + 2 O2 = L-lysyl(9)-[histone H3] + 2 formaldehyde + 2 succinate + 2 CO2
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
Rhea expert-curated reactions1.14.11.65
ExplorEnz1.14.11.65
IUBMB Enzyme Nomenclature1.14.11.65
UniProtKB/Swiss-Prot
O43593, HAIR_HUMANQ61645, HAIR_MOUSEP97609, HAIR_RAT
Q9SSE9, JMJ25_ARATHQ8VYB9, JMJ27_ARATHQ6IRB8, KD3AA_XENLA
Q5HZN1, KD3AB_XENLAO60341, KDM1A_HUMANQ6ZQ88, KDM1A_MOUSE
A0A8I6G2K8, KDM1A_RATQ5ZIX8, KDM3A_CHICKQ9Y4C1, KDM3A_HUMAN
Q6PCM1, KDM3A_MOUSEQ63679, KDM3A_RATQ7LBC6, KDM3B_HUMAN
Q6ZPY7, KDM3B_MOUSEQ9VHC5, KDM3_DROMEQ6ZMT4, KDM7A_HUMAN
Q3UWM4, KDM7A_MOUSEP0CH95, PHF8_DANREQ9UPP1, PHF8_HUMAN
Q80TJ7, PHF8_MOUSE
BRENDA1.14.11.65
MetaCyc1.14.11.65
KEGG Ligand Database for Enzyme Nomenclature1.14.11.65
EC2PDB1.14.11.65
MEDLINEFind literature relating to 1.14.11.65

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