ENZYME entry: EC 1.14.11.68
| Accepted Name |
|---|
| [histone H3]-trimethyl-L-lysine(27) demethylase.
|
| Reaction catalysed |
|---|
| 2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 2 O2 <=> 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(27)-[histone H3] + 2 succinate |
| Comment(s) |
|---|
- Requires iron(II).
- This entry describes a group of enzymes that demethylate N-methylated
L-lysine residues at position 27 of histone H3 (H3K27).
- The enzymes are dioxygenases and act by hydroxylating the methyl
group, forming an unstable hemiaminal that leaves as formaldehyde.
- They can act on tri- and di-methylated forms, but have no activity
with the mono-methylated form.
|
| Cross-references |
|---|
| BRENDA | 1.14.11.68 |
| EC2PDB | 1.14.11.68 |
| ExplorEnz | 1.14.11.68 |
| PRIAM enzyme-specific profiles | 1.14.11.68 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.14.11.68 |
| IUBMB Enzyme Nomenclature | 1.14.11.68 |
| IntEnz | 1.14.11.68 |
| MEDLINE | Find literature relating to 1.14.11.68 |
| MetaCyc | 1.14.11.68 |
| Rhea expert-curated reactions | 1.14.11.68 |
| UniProtKB/Swiss-Prot |
| Q5N712, JM705_ORYSJ; | Q8RWR1, JMJ30_ARATH; | Q0WVR4, JMJ32_ARATH; |
| O15550, KDM6A_HUMAN; | O70546, KDM6A_MOUSE; | O15054, KDM6B_HUMAN; |
| Q5NCY0, KDM6B_MOUSE; | O14607, UTY_HUMAN; | P79457, UTY_MOUSE; |
| Q6B4Z3, UTY_PANTR; |
|
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