ENZYME entry: EC 1.14.11.66
| Accepted Name |
|---|
| [Histone H3]-trimethyl-L-lysine(9) demethylase.
|
| Reaction catalysed |
|---|
| A [histone H3]-N(6),N(6),N(6)-trimethyl-L-lysine(9) + 2 2-oxoglutarate + 2 O(2) <=> a [histone H3]-N(6)-methyl-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
tri- and di-methylated forms.
- The enzymes are dioxygenases and act by hydroxylating the methyl
group, forming an unstable hemiaminal that leaves as formaldehyde,
cf. EC 1.14.11.65.
|
| Cross-references |
|---|
| BRENDA | 1.14.11.66 |
| EC2PDB | 1.14.11.66 |
| ExplorEnz | 1.14.11.66 |
| PRIAM enzyme-specific profiles | 1.14.11.66 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.14.11.66 |
| IUBMB Enzyme Nomenclature | 1.14.11.66 |
| IntEnz | 1.14.11.66 |
| MEDLINE | Find literature relating to 1.14.11.66 |
| MetaCyc | 1.14.11.66 |
| UniProtKB/Swiss-Prot |
| Q9V333, KDM4A_DROME; | O75164, KDM4A_HUMAN; | Q8BW72, KDM4A_MOUSE; |
| Q5RD88, KDM4A_PONAB; | Q9V6L0, KDM4B_DROME; | O94953, KDM4B_HUMAN; |
| Q91VY5, KDM4B_MOUSE; | Q9H3R0, KDM4C_HUMAN; | Q8VCD7, KDM4C_MOUSE; |
| Q6B0I6, KDM4D_HUMAN; | Q3U2K5, KDM4D_MOUSE; | A1A5Q5, KDM4D_RAT; |
| B2RXH2, KDM4E_HUMAN; | Q9U297, KDM4_CAEEL; |
|
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