RHEA:42032
| Enzymes help_outline | 2,076 proteins (UniProtKB) |
| Enzyme class help_outline |
Reaction participants Show >> << Hide
- Name help_outline 2-oxoglutarate Identifier CHEBI:16810 (Beilstein: 3664503; CAS: 64-15-3) help_outline Charge -2 Formula C5H4O5 InChIKeyhelp_outline KPGXRSRHYNQIFN-UHFFFAOYSA-L SMILEShelp_outline [O-]C(=O)CCC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 335 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
N6,N6-dimethyl-L-lysyl36-[histone H3]
Identifier
RHEA-COMP:9787
Reactive part
help_outline
- Name help_outline N6,N6-dimethyl-L-lysine residue Identifier CHEBI:61976 Charge +1 Formula C8H17N2O Positionhelp_outline 36 SMILEShelp_outline C([NH+](C)C)CCC[C@@H](C(*)=O)N* 2D coordinates Mol file for the small molecule Search links Involved in 37 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,235 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CO2 Identifier CHEBI:16526 (Beilstein: 1900390; CAS: 124-38-9) help_outline Charge 0 Formula CO2 InChIKeyhelp_outline CURLTUGMZLYLDI-UHFFFAOYSA-N SMILEShelp_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 868 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline formaldehyde Identifier CHEBI:16842 (Beilstein: 1209228; CAS: 50-00-0) help_outline Charge 0 Formula CH2O InChIKeyhelp_outline WSFSSNUMVMOOMR-UHFFFAOYSA-N SMILEShelp_outline [H]C([H])=O 2D coordinates Mol file for the small molecule Search links Involved in 110 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
L-lysyl36-[histone H3]
Identifier
RHEA-COMP:9785
Reactive part
help_outline
- Name help_outline L-lysine residue Identifier CHEBI:29969 Charge +1 Formula C6H13N2O Positionhelp_outline 36 SMILEShelp_outline C([C@@H](C(*)=O)N*)CCC[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 107 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline succinate Identifier CHEBI:30031 (Beilstein: 1863859; CAS: 56-14-4) help_outline Charge -2 Formula C4H4O4 InChIKeyhelp_outline KDYFGRWQOYBRFD-UHFFFAOYSA-L SMILEShelp_outline [O-]C(=O)CCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 248 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Links to other resources
| RHEA:42032 | RHEA:42033 | RHEA:42034 | RHEA:42035 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Citations
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Histone demethylation by a family of JmjC domain-containing proteins.
Tsukada Y., Fang J., Erdjument-Bromage H., Warren M.E., Borchers C.H., Tempst P., Zhang Y.
Covalent modification of histones has an important role in regulating chromatin dynamics and transcription. Whereas most covalent histone modifications are reversible, until recently it was unknown whether methyl groups could be actively removed from histones. Using a biochemical assay coupled wit ... >> More
Covalent modification of histones has an important role in regulating chromatin dynamics and transcription. Whereas most covalent histone modifications are reversible, until recently it was unknown whether methyl groups could be actively removed from histones. Using a biochemical assay coupled with chromatography, we have purified a novel JmjC domain-containing protein, JHDM1 (JmjC domain-containing histone demethylase 1), that specifically demethylates histone H3 at lysine 36 (H3-K36). In the presence of Fe(ii) and alpha-ketoglutarate, JHDM1 demethylates H3-methyl-K36 and generates formaldehyde and succinate. Overexpression of JHDM1 reduced the level of dimethyl-H3-K36 (H3K36me2) in vivo. The demethylase activity of the JmjC domain-containing proteins is conserved, as a JHDM1 homologue in Saccharomyces cerevisiae also has H3-K36 demethylase activity. Thus, we identify the JmjC domain as a novel demethylase signature motif and uncover a protein demethylation mechanism that is conserved from yeast to human. << Less
Nature 439:811-816(2006) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.