Reaction participants Show >> << Hide
- Name help_outline A Identifier CHEBI:13193 Charge Formula R SMILEShelp_outline * 2D coordinates Mol file for the small molecule Search links Involved in 2,783 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 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-lysyl4-[histone H3]
Identifier
RHEA-COMP:15540
Reactive part
help_outline
- Name help_outline N6,N6-dimethyl-L-lysine residue Identifier CHEBI:61976 Charge 1 Formula C8H17N2O Positionhelp_outline 4 SMILEShelp_outline C([NH+](C)C)CCC[C@@H](C(*)=O)N* 2D coordinates Mol file for the small molecule Search links Involved in 40 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline AH2 Identifier CHEBI:17499 Charge 0 Formula RH2 SMILEShelp_outline *([H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 2,713 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 137 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
L-lysyl4-[histone H3]
Identifier
RHEA-COMP:15547
Reactive part
help_outline
- Name help_outline L-lysine residue Identifier CHEBI:29969 Charge 1 Formula C6H13N2O SMILEShelp_outline C([C@@H](C(*)=O)N*)CCC[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 134 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:60244 | RHEA:60245 | RHEA:60246 | RHEA:60247 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
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EC numbers help_outline | ||||
Gene Ontology help_outline | ||||
MetaCyc help_outline |
Publications
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Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process.
Forneris F., Binda C., Vanoni M.A., Mattevi A., Battaglioli E.
Lysine-specific histone demethylase 1 (LSD1) is a very recently discovered enzyme which specifically removes methyl groups from Lys4 of histone 3. We have addressed the functional properties of the protein demonstrating that histone demethylation involves the flavin-catalysed oxidation of the meth ... >> More
Lysine-specific histone demethylase 1 (LSD1) is a very recently discovered enzyme which specifically removes methyl groups from Lys4 of histone 3. We have addressed the functional properties of the protein demonstrating that histone demethylation involves the flavin-catalysed oxidation of the methylated lysine. The nature of the substrate that acts as the electron acceptor required to complete the catalytic cycle was investigated. LSD1 converts oxygen to hydrogen peroxide although this reactivity is not as pronounced as that of other flavin-dependent oxidases. Our findings raise the possibility that in vivo LSD1 might not necessarily function as an oxidase, but it might use alternative electron acceptors. << Less
FEBS Lett. 579:2203-2207(2005) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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New roles of flavoproteins in molecular cell biology: histone demethylase LSD1 and chromatin.
Forneris F., Battaglioli E., Mattevi A., Binda C.
Lysine-specific demethylase 1 (LSD1) is an enzyme that removes methyl groups from mono- and dimethylated Lys4 of histone H3, a post-translational modification associated with gene activation. Human LSD1 was the first histone demethylase to be discovered and this enzymatic activity is conserved amo ... >> More
Lysine-specific demethylase 1 (LSD1) is an enzyme that removes methyl groups from mono- and dimethylated Lys4 of histone H3, a post-translational modification associated with gene activation. Human LSD1 was the first histone demethylase to be discovered and this enzymatic activity is conserved among eukaryotes. LSD1 has been identified in a number of chromatin-remodeling complexes that control gene transcription and its demethylase activity has also been linked to pathological processes including tumorigenesis. The 852-residue sequence of LSD1 comprises an amine oxidase domain which identifies a family of enzymes that catalyze the FAD-dependent oxidation of amine substrates ranging from amino acids to aromatic neurotransmitters. Among these proteins, LSD1 is peculiar in that it acts on a protein substrate in the nuclear environment of chromatin-remodeling complexes. This functional divergence occurred during evolution from the eubacteria to eukaryotes by acquisition of additional domains such as the SWIRM domain. The N-terminal part of LSD1, predicted to be disordered, contains linear motifs that might represent functional sites responsible for the association of this enzyme with a variety of transcriptional protein complexes. LSD1 shares structural features with other flavin amine oxidases, including the overall fold of the amine oxidase domain region and details in the active site that are relevant for amine substrate oxidation. << Less
FEBS J 276:4304-4312(2009) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
Comments
Multi-step reaction: RHEA:60248 and RHEA:60256