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a [histone H3]-N6,N6-dimethyl-L-lysine4 + ferricenium + H2O
a [histone H3]-N6-methyl-L-lysine4 + formaldehyde + ferrocene
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-
?
a [histone H3]-N6,N6-dimethyl-L-lysine4 + O2 + 2 H2O
a [histone H3]-L-lysine4 + 2 formaldehyde + 2 H2O2
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-
?
a [histone H3]-N6-methyl-L-lysine4 + acceptor + H2O
a [histone H3]-L-lysine4 + formaldehyde + reduced acceptor
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-
-
?
dimethylated histone 3-Lys4 peptide + H2O
?
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the enzyme specifically removes methyl groups from Lys4 of histone 3. The enzyme exhibits oxidase activity (with production of H2O2) but it can function also with a synthetic mono-electronic acceptor
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-
?
H3(1-20) K4-dimethylated peptide + 2-oxoglutarate + O2
H3(1-20) K4-monomethylated peptide + succinate + formaldehyde + CO2
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-
?
H3K4me2 (1-21 aa) peptide + 2-oxoglutarate + O2
H3K4me1 (1-21 aa) peptide + succinate + formaldehyde + CO2
H3K4me2 1-21 peptide + 2-oxoglutarate + O2
H3K4me1 1-21 peptide + succinate + formaldehyde + CO2
-
-
-
?
H3K4me2 peptide 3-21 + 2-oxoglutarate + O2
H3K4me1 peptide 3-21 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
[histone H3 peptide 21mer P16A]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
?
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-
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-
?
[histone H3 peptide 21mer]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 peptide 21mer]-L-lysine4 + succinate + formaldehyde + CO2
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-
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?
[histone H3 peptide 21mer]-N6,N6-dimethyl-L-lysine4-dimethyl-L-lysine9 + 2-oxoglutarate + O2
?
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-
-
-
?
[histone H3 peptide 21mer]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 peptide 21mer]-L-lysine4 + succinate + formaldehyde + CO2
-
no activity with a monomethylated H3-Lys4 peptide with Arg2 mutated to Ala, Arg2 is central to substrate recognition also in LSD2
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-
?
[histone H3 peptide 21mer]-N6-methyl-L-lysine4-acetyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3 peptide 21mer]-L-lysine4-acetyl-L-lysine9 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3 peptide 21mer]-N6-methyl-L-lysine4-methyl-L-arginine17 + 2-oxoglutarate + O2
?
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-
-
-
?
[histone H3 peptide 21mer]-N6-methyl-L-lysine4-methyl-L-lysine9 + 2-oxoglutarate + O2
?
-
-
-
-
?
[histone H3 peptide 30mer]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 peptide 30mer]-L-lysine4 + succinate + formaldehyde + CO2
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-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
[histone H3]-N6,N6-dimethyl-L-lysine 4 + acceptor + H2O
[histone H3]-N6-methyl-L-lysine 4 + formaldehyde + reduced acceptor
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 acceptor + 2 H2O
[histone H3]-L-lysine4 + 2 formaldehyde + 2 reduced acceptor
overall reaction
-
-
?
[histone H3]-N6,N6-L-dimethyllysine21 + O2 + 2 H2O
[histone H3]-L-lysine + 2 formaldehyde + 2 H2O2
diMeK4H3-21 i.e. a dimethyl K4-containing histone H3 peptide
-
-
?
[histone H3]-N6,N6-L-dimethyllysine4 + O2 + 2 H2O
[histone H3]-N6,N6-L-dimethyllysine4 + 2 formaldehyde + 2 H2O2
-
-
-
?
[histone H3]-N6,N6-L-dimethyllysine4-1-21 + O2 + 2 H2O
[histone H3]-L-lysine4-1-21 + 2 formaldehyde + 2 H2O2
substrate is a dimethylated peptide corresponding to the first 21 amino acids of the N-terminal tail of histone H3
-
-
?
[histone H3]-N6,N6-methyl-L-lysine 4 + acceptor + H2O
[histone H3]-L-lysine 4 + formaldehyde + reduced acceptor
-
-
-
?
[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
[histone H3]-N6-methyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
[histone H4]-N6-methyl-L-lysine 20 + 2-oxoglutarate + O2
[histone H4]-L-lysine 20 + succinate + formaldehyde + CO2
-
-
-
?
additional information
?
-
H3K4me2 (1-21 aa) peptide + 2-oxoglutarate + O2
H3K4me1 (1-21 aa) peptide + succinate + formaldehyde + CO2
-
-
-
?
H3K4me2 (1-21 aa) peptide + 2-oxoglutarate + O2
H3K4me1 (1-21 aa) peptide + succinate + formaldehyde + CO2
a peptide corresponding to the first 21 amino acids of histone H3 with a dimethylated lysine at the fourth residue [ARTK(diMe)QTARKSTGGKAPRKQLA]
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?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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-
-
-
?
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
-
dimethyl-H3K4 is an activation markers for gene expression
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?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
dimethyl-H3K4 is an activation markers for gene expression
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
-
lack of H3K4diMe is possibly due to complex epigenetic regulation involving Ash2 and LSD1
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
specific pockets in the substrate-binding site of LSD1 that interact with several H3 side chains, Thr6, Arg8, Lys9 and Thr11, and also with the N-terminal amino group of Ala1, N-term pocket, overview
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?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
-
demethylation of H3K4 is critical for establishing the DNA methylation imprints during oogenesis
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-
?
[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
specific pockets in the substrate-binding site of LSD1 that interact with several H3 side chains, Thr6, Arg8, Lys9 and Thr11, and also with the N-terminal amino group of Ala1, N-term pocket
-
-
?
[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
-
demethylation of H3K4 is critical for establishing the DNA methylation imprints during oogenesis
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-
?
[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
-
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-
?
[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
additional information
?
-
-
LSD1 is specific for Lys4 of both mono- and dimethylated histone H3 using a highly specific recognition mechanism, LSD1-catalyzed reaction produces an imine intermediate that is hydrolyzed to the demethylated product and formaldehyde, Reduced flavin is reoxidized by molecular oxygen with the concomitant production of hydrogen peroxide, overview
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?
additional information
?
-
LSD1 shows demethylase activity toward mono- and dimethylated Lys4 but not dimethylated Lys9 and Lys27 of histone 3, substrate and product identification by MALDI mass spectrometry. No LSD1 activity toward the H3K4me1-phosphoSer10 peptide
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?
additional information
?
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LSD1 shows demethylase activity toward mono- and dimethylated Lys4 but not dimethylated Lys9 and Lys27 of histone 3, substrate and product identification by MALDI mass spectrometry. No LSD1 activity toward the H3K4me1-phosphoSer10 peptide
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?
additional information
?
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LSD1 is specific for Lys4 of both mono- and dimethylated histone H3 using a highly specific recognition mechanism, LSD1-catalyzed reaction produces an imine intermediate that is hydrolyzed to the demethylated product and formaldehyde, Reduced flavin is reoxidized by molecular oxygen with the concomitant production of hydrogen peroxide, overview
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?
additional information
?
-
-
LSD1 interacts with several interaction partners and transcription factors for performing its role in gene regulation, overview
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?
additional information
?
-
-
LSD1 catalyzes the demethylation of Lys4 of histone H3 through a flavin-dependent oxidative reaction via an imine intermediate. LSD1 can act both on mono- and dimethylated H3K4. The reaction involves several steps, overview
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-
?
additional information
?
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LSD1 is specific for Lys4 of both mono- and dimethylated histone H3 using a highly specific recognition mechanism, LSD1-catalyzed reaction produces an imine intermediate that is hydrolyzed to the demethylated product and formaldehyde, Reduced flavin is reoxidized by molecular oxygen with the concomitant production of hydrogen peroxide, overview
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?
additional information
?
-
the fly KDM1 protein has in vitro demethylase activity for H3K4me2/1
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?
additional information
?
-
functional interplay between histone demethylase and histone deacetylase
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?
additional information
?
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LSD1 forms a complex with CoREST and histone deacetylase 1. LSD1 mediates the transrepressive function of TLX, an orphan nuclear receptor, also called NR2E1, that regulates the expression of target genes by functioning as a constitutive transrepressor, through direct interaction via its SWIRM and amine oxidase domains. Physiological significance of TLX in the cytodifferentiation of neural cells in the brain
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?
additional information
?
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LSD1 forms a stable complex with Rb, but with E2F1, cell cycle regulatory proteins. LSD1 binds to Epstein-Barr virus C promoter Cp in a cell cycle-dependent manner, as do the the cell cycle regulatory proteins E2F1 and Rb. Rb and LSD1 binding to Cp increase after the S phase, corresponding to a decrease in histone H3 K4 methylation and Cp transcription, overview
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?
additional information
?
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LSD1 interacts with CoREST, a co-repressor protein that binds REST and recruits other histone-modifying enzymes such as histone deacetylases 1 ? 2. The function of the LSD1CoRESThistone deacetylase subcomplex in transcriptional repression events is not limited to REST-regulated neuronal genes, but can be extended to other contexts such as hematopoietic differentiation and the telomerase reverse transcriptase genes
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?
additional information
?
-
LSD1 interacts with several interaction partners and transcription factors for performing its role in gene regulation, overview. LSD1 forms a complex with CoREST, structure with bound histone H3 peptide substrate, overview. LSD1 tightly associates with the CoREST C-terminal SANT domain. This intermolecular association is mediated by the LSD1 tower domain, whose alpha-helices are embraced by a helical segment of CoREST, generating an intermolecular helical coil. The histone H3 N-terminal peptide binds deeply in the LSD1 amine oxidase domain in proximity to the flavin cofactor
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?
additional information
?
-
LSD1 catalyzes the demethylation of Lys4 of histone H3 through a flavin-dependent oxidative reaction via an imine intermediate. LSD1 can act both on mono- and dimethylated H3K4. The reaction involves several steps, overview
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-
?
additional information
?
-
-
LSD1 is specific for Lys4 of both mono- and dimethylated histone H3 using a highly specific recognition mechanism, LSD1-catalyzed reaction produces an imine intermediate that is hydrolyzed to the demethylated product and formaldehyde, Reduced flavin is reoxidized by molecular oxygen with the concomitant production of hydrogen peroxide, overview
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?
additional information
?
-
LSD1 specificity and mechanism of action are complex-dependent
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?
additional information
?
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LSD1 removes the methyl groups from lysines 4 and 9 of histone 3 with the generation of formaldehyde from the methyl group
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?
additional information
?
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LSD1 directly binds to the promoter of P21 where it catalyzes H3K4me2 demethylation. FEZF1-AS1, a 2564 bp RNA overexpressed in gastric cancer, epigenetically represses the expression of P21 via binding with LSD1
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?
additional information
?
-
lysine-specific demethylase 1(LSD1) demethylates mono- and dimethylated residues of lysine-4 on histone H3 (H3K4me1 and H3K4me2) and lysine-9 on histone H3 (H3K9me1 and H3K9me2)
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?
additional information
?
-
histone demethylase LSD1 demethylates Lys4 or Lys9 of histone H3 using FAD as cofactor
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?
additional information
?
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no substrates: dimethylated histone H3 K9 residues
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?
additional information
?
-
the bifunctional enzyme catalyzes the demethylation of H3K4me2/me1 and H3K9me2/me1 (EC 1.14.11.65)
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?
additional information
?
-
the bifunctional enzyme catalyzes the demethylation of H3K4me2/me1 and H3K9me2/me1 (EC 1.14.11.65)
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?
additional information
?
-
the bifunctional enzyme catalyzes the demethylation of H3K4me2/me1 and H3K9me2/me1 (EC 1.14.11.65), as well as non-histone substrates. Tight-binding nature of the H3/KDM1A interaction, kinetics, overview. No other core histones exhibits inhibition of KDM1A demethylation activity, which is consistent with H3 being the preferred histone substrate of KDM1A versus H2A, H2B, and H4. Kinetic analysis of full-length histone products against KDM1A. KDM1A requires a minimal substrate corresponding to the first 21 residues of the N-terminal histone H3 tail for efficient demethylation activity. Recombinant KDM1A/LSD11 forms a complex in vitro with recombinant transcription factor CoREST
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additional information
?
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the bifunctional enzyme catalyzes the demethylation of H3K4me2/me1 and H3K9me2/me1 (EC 1.14.11.65). Functional interplay between histone demethylase and histone deacetylase. The enzymatic activities of the histone demethylase and the deacetylase are intimately linked. The cross talk between the two enzymes is seen only when nucleosomal substrates are used and is mediated through different domains of the CoREST protein (FLAG-tagged CoREST and mutants are recombinantly expressed in HEK-293 cells and Escherichia coli strain BL21). LSD1-HDAC1 complexes display enhanced acetylation activity in presence of CoREST
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additional information
?
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the bifunctional enzyme catalyzes the demethylation of H3K4me2/me1 and H3K9me2/me1 (EC 1.14.11.65). LSD1 is specific for Lys-4 of histone H3 and can oxidatively demethylate the dimethyl or monomethyl Lys-containing substrates
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?
additional information
?
-
the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
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?
additional information
?
-
the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
-
-
?
additional information
?
-
the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
-
-
?
additional information
?
-
the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
-
-
?
additional information
?
-
the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
-
-
?
additional information
?
-
the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
-
-
?
additional information
?
-
-
the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
-
-
?
additional information
?
-
the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
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?
additional information
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the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1. As LSD1 can demethylate both H3K4 and H3K9, the coupling of this protein in the HCF-1 Set1 or MLL methyltransferase complex may enhance H3K9 demethylation or preferentially target it to this substrate, although additional histone modifications and modification activities may also contribute to the H3K4 or H3K9 recognition and specificity
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additional information
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the enzyme is specific for mono- and dimethylated Lys4 in histone H3 (H3K4me1/2). LSD1 prefers an unmodified alpha-amine three residues preceding the methyllysine in the protein substrate, consistent with its specificity for H3K4me1/2 in vitro. To catalyze efficient demethylation, the enzyme requires H3 peptides at least 16 residues in length. In addition, LSD1 exhibits a strong preference toward H3K4me2 substrates lacking other covalent modifications, including R2me, R8me, S10ph, K9ac, and K14ac. In addition, LSD1 might also by active with mono- and dimethylated Lys9 in histone H3 (H3K9me1/2), cf. EC 3.4.11.66
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additional information
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the rate-limiting reductive half-reaction of LSD1 employs a direct hydride transfer mechanism. Conserved residue Tyr761 and the lysine-water-flavin motif help properly orienting FAD with respect to substrate, thereby stabilizing the catalytic environment and facilitating the demethylation reaction
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additional information
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amine oxidase flavin-containing domain 1, AOF1, also called lysine demethylase 1B , KDM1B, is a protein related to the lysine demethylase KDM1or LSD1, it functions as a H3K4 demethylase and is required for de novo DNA methylation of some imprinted genes in oocytes
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additional information
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p53 directly interacts with LSD1 to alter chromatin structure and confer developmental repression of the tumor marker alpha-fetoprotein, AFP, p53 and LSD1 cooccupy a p53 response element, concomitant with dimethylated histone H3 lysine 4 demethylation and postnatal repression of AFP transcription, overview
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additional information
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the enzyme is organized in histone demethylase complexes containing LSD1, RE1 silencing transcription factor corepressor, CoREST, histone deacetylase 1, HDAC1, and histone deacetylase 2 in erythroleukemia and T cell leukemia cells. the Complex interacts with TAL, a critical transcription factor required for hematopoiesis, overview. The enzymatic domain of LSD1 plays an important role in repressing the TAL1-directed transcription, overview. TAL1-associated LSD1 and HDM activity are dynamically regulated during hematopoiesis
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additional information
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recombinant KDM1B shows no activity with H3K4me3, H3K9me2, H3K27me2 and H3K36me2
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additional information
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substrate specificity and effect of epigenetic marks, overview. No activity with peptide substrate of chain length below 21. Activity determinations of recombinant wild-type and mutant enzymes by horseradish peroxidase-coupled and formaldehyde dehydrogenase-coupled assays with histone H3 peptides as substrates, method optimization, e.g. with respect to pH and ionic strength, overview
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additional information
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LSD1 demethylates mono- and dimethylated H3K4 and H3K9, but does not alter trimethylated H3K4 and H3K9
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additional information
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LSD1 demethylates mono- and dimethylated H3K4 and H3K9, but does not alter trimethylated H3K4 and H3K9
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additional information
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no activity with histone H3 N6,N6,N6-dimethyl-L-lysine4
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additional information
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no activity with histone H3 N6,N6,N6-dimethyl-L-lysine4
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K4me2/me1 and H3K9me2/me1 (EC 1.14.11.65)
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a [histone H3]-N6,N6-dimethyl-L-lysine4 + O2 + 2 H2O
a [histone H3]-L-lysine4 + 2 formaldehyde + 2 H2O2
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
[histone H3]-N6,N6-dimethyl-L-lysine 4 + acceptor + H2O
[histone H3]-N6-methyl-L-lysine 4 + formaldehyde + reduced acceptor
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[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 acceptor + 2 H2O
[histone H3]-L-lysine4 + 2 formaldehyde + 2 reduced acceptor
overall reaction
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[histone H3]-N6,N6-methyl-L-lysine 4 + acceptor + H2O
[histone H3]-L-lysine 4 + formaldehyde + reduced acceptor
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[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
[histone H3]-N6-methyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-L-lysine 9 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
additional information
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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dimethyl-H3K4 is an activation markers for gene expression
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
dimethyl-H3K4 is an activation markers for gene expression
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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lack of H3K4diMe is possibly due to complex epigenetic regulation involving Ash2 and LSD1
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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demethylation of H3K4 is critical for establishing the DNA methylation imprints during oogenesis
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[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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demethylation of H3K4 is critical for establishing the DNA methylation imprints during oogenesis
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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additional information
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LSD1 interacts with several interaction partners and transcription factors for performing its role in gene regulation, overview
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additional information
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functional interplay between histone demethylase and histone deacetylase
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additional information
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LSD1 forms a complex with CoREST and histone deacetylase 1. LSD1 mediates the transrepressive function of TLX, an orphan nuclear receptor, also called NR2E1, that regulates the expression of target genes by functioning as a constitutive transrepressor, through direct interaction via its SWIRM and amine oxidase domains. Physiological significance of TLX in the cytodifferentiation of neural cells in the brain
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additional information
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LSD1 forms a stable complex with Rb, but with E2F1, cell cycle regulatory proteins. LSD1 binds to Epstein-Barr virus C promoter Cp in a cell cycle-dependent manner, as do the the cell cycle regulatory proteins E2F1 and Rb. Rb and LSD1 binding to Cp increase after the S phase, corresponding to a decrease in histone H3 K4 methylation and Cp transcription, overview
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additional information
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LSD1 interacts with CoREST, a co-repressor protein that binds REST and recruits other histone-modifying enzymes such as histone deacetylases 1 ? 2. The function of the LSD1CoRESThistone deacetylase subcomplex in transcriptional repression events is not limited to REST-regulated neuronal genes, but can be extended to other contexts such as hematopoietic differentiation and the telomerase reverse transcriptase genes
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additional information
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LSD1 interacts with several interaction partners and transcription factors for performing its role in gene regulation, overview. LSD1 forms a complex with CoREST, structure with bound histone H3 peptide substrate, overview. LSD1 tightly associates with the CoREST C-terminal SANT domain. This intermolecular association is mediated by the LSD1 tower domain, whose alpha-helices are embraced by a helical segment of CoREST, generating an intermolecular helical coil. The histone H3 N-terminal peptide binds deeply in the LSD1 amine oxidase domain in proximity to the flavin cofactor
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additional information
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LSD1 removes the methyl groups from lysines 4 and 9 of histone 3 with the generation of formaldehyde from the methyl group
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additional information
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LSD1 directly binds to the promoter of P21 where it catalyzes H3K4me2 demethylation. FEZF1-AS1, a 2564 bp RNA overexpressed in gastric cancer, epigenetically represses the expression of P21 via binding with LSD1
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additional information
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lysine-specific demethylase 1(LSD1) demethylates mono- and dimethylated residues of lysine-4 on histone H3 (H3K4me1 and H3K4me2) and lysine-9 on histone H3 (H3K9me1 and H3K9me2)
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additional information
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amine oxidase flavin-containing domain 1, AOF1, also called lysine demethylase 1B , KDM1B, is a protein related to the lysine demethylase KDM1or LSD1, it functions as a H3K4 demethylase and is required for de novo DNA methylation of some imprinted genes in oocytes
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additional information
?
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p53 directly interacts with LSD1 to alter chromatin structure and confer developmental repression of the tumor marker alpha-fetoprotein, AFP, p53 and LSD1 cooccupy a p53 response element, concomitant with dimethylated histone H3 lysine 4 demethylation and postnatal repression of AFP transcription, overview
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additional information
?
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the enzyme is organized in histone demethylase complexes containing LSD1, RE1 silencing transcription factor corepressor, CoREST, histone deacetylase 1, HDAC1, and histone deacetylase 2 in erythroleukemia and T cell leukemia cells. the Complex interacts with TAL, a critical transcription factor required for hematopoiesis, overview. The enzymatic domain of LSD1 plays an important role in repressing the TAL1-directed transcription, overview. TAL1-associated LSD1 and HDM activity are dynamically regulated during hematopoiesis
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additional information
?
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LSD1 demethylates mono- and dimethylated H3K4 and H3K9, but does not alter trimethylated H3K4 and H3K9
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additional information
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LSD1 demethylates mono- and dimethylated H3K4 and H3K9, but does not alter trimethylated H3K4 and H3K9
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(12E)-N,N'-diethyl-5,10,16,21-tetraazapentacos-12-ene-1,25-diamine
(13Z)-N,N'-diethyl-6,11,16,21-tetraazahexacos-13-ene-1,26-diamine
(19E)-N,N'-diethyl-6,12,17,22,27,33-hexaazaoctatriacont-19-ene-1,38-diamine
(19Z)-N,N'-diethyl-6,12,17,22,27,33-hexaazaoctatriacont-19-ene-1,38-diamine
(2-hydroxyacetyl)-L-alanyl-L-arginyl-L-threonyl-L-methionyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucine
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(2-hydroxyacetyl)-L-arginyl-L-threonyl-L-methionyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucine
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(25E)-N,N'-diethyl-5,11,17,23,28,33,39,45-octaazapentacont-25-ene-1,50-diamine
(25Z)-N,N'-diethyl-6,12,18,23,28,33,39,45-octaazapentacont-25-ene-1,50-diamine
(2Z)-N-ethyl-N'-[4-[(4-[[(2Z)-4-(ethylamino)but-2-en-1-yl]amino]butyl)amino]butyl]but-2-ene-1,4-diamine
(2Z)-N-[4-(ethylamino)butyl]-N'-(4-[[4-(ethylamino)butyl]amino]butyl)but-2-ene-1,4-diamine
1,1'-[butane-1,4-diylbis(iminopropane-3,1-diyl)]bis[3-(2,2-diphenylethyl)guanidine]
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1,1'-[butane-1,4-diylbis(iminopropane-3,1-diyl)]bis[3-(3,3-diphenylpropyl)guanidine]
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1,1'-[heptane-1,7-diylbis(iminopropane-3,1-diyl)]bis(3-methylguanidine)
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1,1'-[heptane-1,7-diylbis(iminopropane-3,1-diyl)]bis(3-phenylguanidine)
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1,1'-[propane-1,3-diylbis(iminopropane-3,1-diyl)]bis(2,3-dimethylguanidine)
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1,1'-[propane-1,3-diylbis(iminopropane-3,1-diyl)]bis(3-methylguanidine)
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1,1'-[propane-1,3-diylbis(iminopropane-3,1-diyl)]bis(3-phenylguanidine)
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1,11-bis(N2,N3-dimethyl-N1-guanidino)-4,8-diazaundecane
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1,11-bis-[3-[1-(1,1-diphenylmethyl)thioureado]]-4,8-diazaundecane
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48.9% inhibition at 0.01 mM
1,11-bis-[3-[1-(2,2-diphenylethyl)thioureado]]-4,8-diazaundecane
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75.2% inhibition at 0.01 mM
1,11-bis-[3-[1-(3,3-diphenylpropyl)thioureado]]-4,8-diazaundecane
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7.8% inhibition at 0.01 mM
1,11-bis-[3-[1-(3,3-diphenylpropyl)ureado]]-4,8-diazaundecane
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7.1% inhibition at 0.01 mM
1,11-bis-[3-[1-(benzyl)thioureado]]-4,8-diazaundecane
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47.9% inhibition at 0.01 mM
1,11-bis-[3-[1-(benzyl)ureado]]-4,8-diazaundecane
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39.5% inhibition at 0.01 mM
1,11-bis-[3-[1-(ethyl)thioureado]]-4,8-diazaundecane
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63.8% inhibition at 0.01 mM
1,11-bis-[3-[1-(ethyl)ureado]]-4,8-diazaundecane
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34.5% inhibition at 0.01 mM
1,11-bis-[3-[1-(n-propyl)ureado]]-4,8-diazaundecane
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48.7% inhibition at 0.01 mM
1,11-bis-[5-[1-(N,N-diphenyl)carbamyl]ureado]-4,8-diazaundecane
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8.5% inhibition at 0.01 mM
1,12-bis-[3-[1-(1,1-diphenylmethyl)thioureado]]-4,9-diazadodecane
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65.6% inhibition at 0.01 mM
1,12-bis-[3-[1-(2,2-diphenylethyl)thioureado]]-4,9-diazadodecane
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82.9% inhibition at 0.01 mM
1,12-bis-[3-[1-(3,3-diphenylpropyl)thioureado]]-4,9-diazadodecane
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21.4% inhibition at 0.01 mM
1,12-bis-[3-[1-(3,3-diphenylpropyl)ureado]]-4,9-diazadodecane
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25.4% inhibition at 0.01 mM
1,12-bis-[3-[1-(benzyl)ureado]]-4,9-diazadodecane
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50.5% inhibition at 0.01 mM
1,12-bis-[3-[1-(ethyl)thioureado]]-4,9-diazadodecane
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60% inhibition at 0.01 mM
1,12-bis-[3-[1-(ethyl)ureado]]-4,9-diazadodecane
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50.8% inhibition at 0.01 mM
1,12-bis-[3-[1-(n-propyl)thioureado]]-4,9-diazadodecane
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10.4% inhibition at 0.01 mM
1,12-bis-[3-[1-(n-propyl)ureado]]-4,9-diazadodecane
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21% inhibition at 0.01 mM
1,12-bis-[5-[1-(N,N-diphenyl)carbamyl]ureado]-4,9-diazadodecane
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73.9% inhibition at 0.01 mM
1,15-bis(N5-[3,3-(diphenyl)propyl]-N1-biguanido)-4,12-diazapentadecane
-
1,15-bis-[3-[1-(1,1-diphenylmethyl)thioureado]]-4,12-diazapentadecane
-
71.1% inhibition at 0.01 mM
1,15-bis-[3-[1-(2,2-diphenylethyl)thioureado]]-4,12-diazapentadecane
-
80.5% inhibition at 0.01 mM
1,15-bis-[3-[1-(3,3-diphenylpropyl)thioureado]]-4,12-diazapentadecane
-
22.7% inhibition at 0.01 mM
1,15-bis-[3-[1-(3,3-diphenylpropyl)ureado]]-4,12-diazapentadecane
-
48.5% inhibition at 0.01 mM
1,15-bis-[3-[1-(benzyl)thioureado]]-4,12-diazapentadecane
-
64.1% inhibition at 0.01 mM
1,15-bis-[3-[1-(benzyl)ureado]]-4,12-diazapentadecane
-
-
1,15-bis-[3-[1-(ethyl)ureado]]-4,12-diazapentadecane
-
-
1,15-bis-[3-[1-(n-propyl)ureado]]-4,12-diazapentadecane
-
8.5% inhibition at 0.01 mM
1,15-bis-[5-[1-(N,N-diphenyl)carbamyl]ureado]-4,12-diazapentadecane
-
30.0% inhibition at 0.01 mM
3,8,13,18,23-pentaazapentacosan-1-ol
3-((1S,2R)-2-(cyclobutylamino)cyclopropyl)-N-(5-methyl-1,3,4-thiadiazol-2-yl)benzamide
compound increases H3K4 methylation in the brain without causing hematological side effects. Compound increases brain H3K4 methylation and partially restores learning function in mice with NMDA receptor hypofunction. Compound has minimal impact on the LSD1-GFI1B complex in human TF-1alpha erythroblasts
3-[(E)-2-[2-(5-fluoro-2-hydroxyphenyl)pyridin-4-yl]ethenyl]N'-hydroxybenzene-1-carboximidamide
potently inhibits LSD1 in a reversible and FAD competitive manner. Compound is capable of upregulating the expression of the surrogate cellular biomarker CD86 in THP-1 human leukemia cells and shows good inhibition against THP-1 and MOLM-13 cells with IC50 values of 5.76 and 8.34 microM
4-([[(1S,2R)-2-phenylcyclopropyl]amino]ethyl)benzamide
tranylcypromine-based inhibitor with selectivity for LSD1 over MAO-A and MAO-B
4-([[(1S,2R)-2-phenylcyclopropyl]amino]ethyl)benzene-1-sulfonamide
tranylcypromine-based inhibitor with selectivity for LSD1 over MAO-A and MAO-B
biguanide
inhibits LSD1 and is capable of reactivating genes that are pathologically silenced in the development of colon cancer
bis-[3-[1-(benzyl)thioureado]]-4,9-diazadodecane
-
25.2% inhibition at 0.01 mM
bisguanidine polyamine analogues
inhibit LSD1 and are capable of reactivating genes that are pathologically silenced in the development of colon cancer
-
glycerol
inhibits at 10%, activates at above 30%
GSK2879552
inhibitor targets the FAD domain
HCF-1
a component of the Set1 and MLL1 histone H3 Lys4 methyltransferase complexes, which coordinates modulation of repressive H3 Lys9 methylation levels with addition of activating H3 Lys4 trimethylation marks
-
histone H3
full-length histone H3, which lacks any posttranslational modifications, is a tight-binding, competitive inhibitor; full-length histone H3, which lacks any posttranslational modifications, is a tight-binding, competitive inhibitor of KDM1A demethylation activity with a Ki of 18.9 nM, a value that is approximately 100fold higher than that of the 21-mer peptide of H3. The relative H3 affinity is independent of preincubation time, suggesting that H3 rapidly reaches equilibrium with KDM1A, tight-binding nature of the H3/KDM1A interaction, kinetics, overview. No other core histones exhibits inhibition of KDM1A demethylation activity, which is consistent with H3 being the preferred histone substrate of KDM1A versus H2A, H2B, and H4. Inhibition profiling of full-length histone H3 against KDM1A
-
histone H3 1-21 peptide
21-mer H3-derived peptide
-
histone H3-1-21
peptide corresponding to the first 21 amino acids of the N-terminal tail of histone H3, competitive inhibitor
-
KCl
50 mM, 50% inhibition
L-alanyl-L-arginyl-L-threonyl-6-(aziridin-1-yl)norleucyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucyl-L-alanine
compound 2 decomposes when lyophilized to dryness
L-alanyl-L-arginyl-L-threonyl-6-hydroxynorleucyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucyl-L-alanine
a peptide containing an oxa-analogue of lysine at the fourth position of a 21 amino acid N-terminal histone H3 tail
L-alanyl-L-arginyl-L-threonyl-6-[(methylsulfonyl)oxy]norleucyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucyl-L-alanine
mesylate peptide
L-alanyl-L-arginyl-L-threonyl-L-methionyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucine
-
L-alanyl-L-arginyl-L-threonyl-N6-(prop-2-yn-1-yl)lysyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucyl-L-alanine
a propargyl-Lys-derivatized peptide, MALDI-TOF spectrum of inhibitor-FAD conjugate, the reduced FAD (FADH2) undergoes nucleophilic attack on the propargylic imine and creates the covalent adduct
L-arginyl-L-threonyl-L-methionyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucine
-
L-homoseryseryl-L-arginyl-L-threonyl-L-methionyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucyl-(N6-(L-homoseryl))-L-lysine
enzyme binding structure, overview
L-seryl-L-arginyl-L-threonyl-L-methionyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucine
enzyme binding structure, overview
MgCl2
75% inhibition at 50 mM
N,N''''-[butane-1,4-diylbis(iminopropane-3,1-diyl)]bis[N'-(2,2-diphenylethyl)(imidodicarbonimidic diamide)]
-
N,N''''-[butane-1,4-diylbis(iminopropane-3,1-diyl)]bis[N'-(3,3-diphenylpropyl)(imidodicarbonimidic diamide)]
-
N,N''''-[heptane-1,7-diylbis(iminopropane-3,1-diyl)]bis[N'-(2,2-diphenylethyl)(imidodicarbonimidic diamide)]
-
N,N''''-[heptane-1,7-diylbis(iminopropane-3,1-diyl)]bis[N'-(3,3-diphenylpropyl)(imidodicarbonimidic diamide)]
-
N,N''''-[propane-1,3-diylbis(iminopropane-3,1-diyl)]bis[N'-(2,2-diphenylethyl)(imidodicarbonimidic diamide)]
-
N,N''''-[propane-1,3-diylbis(iminopropane-3,1-diyl)]bis[N'-(3,3-diphenylpropyl)(imidodicarbonimidic diamide)]
-
N,N'-diethyl-5,11,17,22,27,33-hexaazaoctatriacontane-1,38-diamine
N,N'-diethyl-5,11,17,23,28,33,39,45-octaazapentacontane-1,50-diamine
N-(hydroxyacetyl)-L-alanyl-L-arginyl-L-threonyl-L-methionyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-N6-(hydroxyacetyl)-L-lysyl-L-glutaminyl-L-leucine
-
N-(hydroxyacetyl)-L-alanyl-L-arginyl-L-threonyl-L-methionyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-N6-(hydroxyacetyl)-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucine
-
N-ethyl-N'-[[2-([[4-([[2-([[4-(ethylamino)butyl]amino]methyl)cyclopropyl]methyl]amino)butyl]amino]methyl)cyclopropyl]methyl]butane-1,4-diamine
N-methyl-N-propargylbenzylamine hydrochloride
i.e. pargyline
N2-L-alanyl-L-arginyl-L-threonyl-L-methionyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-N6-(2-hydroxyacetyl)-L-lysyl-L-glutaminyl-L-leucine
-
N2-L-alanyl-L-arginyl-L-threonyl-L-methionyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-N6-(2-hydroxyacetyl)-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucine
-
N2-L-seryl-L-arginyl-L-threonyl-L-methionyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-(N6-(L-seryl))-L-lysyl-L-glutaminyl-L-leucine
-
N2-L-seryl-L-arginyl-L-threonyl-L-methionyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucyl-(N6-(L-seryl))-L-lysine-amide
enzyme binding structure, overview
N2-L-seryl-L-arginyl-L-threonyl-L-methionyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucyl-L-alanyl-L-threonyl-(N6-(L-seryl))-L-lysine-amide
-
PCPA-Lys-4 H3-11
11-mer histone H3 peptide because the 11-mer bearing a trans-2-phenylcyclopropylamine moiety at Lys-4
PCPA-Orn-4 H3-11
11-mer histone H3 peptide because the 11-mer bearing a trans-2-phenylcyclopropylamine moiety at Orn-4
peptide H3K4M
the modified H3 peptide with substitution of Lys4 to Met [H3K4M] is known to be a potent competitive inhibitor of LSD1
-
Phenelzine
inhibitor targets both the flavin adenine dinucleotide and CoREST binding domains of LSD1. Treatment reduces nuclear demethylase activity and increases transcription and expression of M1-like signatures both in vitro and in a murine triple-negative breast cancer model
sodium butyrate
a histone deacetylase (HDAC) inhibitor
trans-2-phenylcyclopropylamine
trichostatin A
a histone deacetylase (HDAC) inhibitor
[histone H3 peptide 21mer]-L-arginine4
-
competitive inhibition of LSD2
-
[histone H3 peptide 21mer]-L-glutamine4
-
competitive inhibition of LSD2
-
[histone H3 peptide 21mer]-L-lysine4
-
the demethylated peptide, product of the LSD2 reaction, inhibits LSD2
-
[histone H3 peptide 21mer]-L-methionine4
-
competitive inhibition of LSD2
-
[histone H3 peptide 21mer]-N6,N6,N6-trimethyl-L-lysine4
-
-
-
[histone H3 peptide]-N6-methyl-L-lysine9
-
-
(12E)-N,N'-diethyl-5,10,16,21-tetraazapentacos-12-ene-1,25-diamine
-
-
(12E)-N,N'-diethyl-5,10,16,21-tetraazapentacos-12-ene-1,25-diamine
-
(13Z)-N,N'-diethyl-6,11,16,21-tetraazahexacos-13-ene-1,26-diamine
-
-
(13Z)-N,N'-diethyl-6,11,16,21-tetraazahexacos-13-ene-1,26-diamine
-
(19E)-N,N'-diethyl-6,12,17,22,27,33-hexaazaoctatriacont-19-ene-1,38-diamine
-
-
(19E)-N,N'-diethyl-6,12,17,22,27,33-hexaazaoctatriacont-19-ene-1,38-diamine
i.e PG-11144, exhibits competitive inhibition kinetics at concentrations below 0.010 mmol/l. PG-11144 combined with a DNMT inhibitor increases H3K4 methylation and profoundly inhibits growth of established tumors in vivo
(19Z)-N,N'-diethyl-6,12,17,22,27,33-hexaazaoctatriacont-19-ene-1,38-diamine
-
-
(19Z)-N,N'-diethyl-6,12,17,22,27,33-hexaazaoctatriacont-19-ene-1,38-diamine
-
(25E)-N,N'-diethyl-5,11,17,23,28,33,39,45-octaazapentacont-25-ene-1,50-diamine
-
-
(25E)-N,N'-diethyl-5,11,17,23,28,33,39,45-octaazapentacont-25-ene-1,50-diamine
-
(25Z)-N,N'-diethyl-6,12,18,23,28,33,39,45-octaazapentacont-25-ene-1,50-diamine
-
-
(25Z)-N,N'-diethyl-6,12,18,23,28,33,39,45-octaazapentacont-25-ene-1,50-diamine
-
(2Z)-N-ethyl-N'-[4-[(4-[[(2Z)-4-(ethylamino)but-2-en-1-yl]amino]butyl)amino]butyl]but-2-ene-1,4-diamine
-
-
(2Z)-N-ethyl-N'-[4-[(4-[[(2Z)-4-(ethylamino)but-2-en-1-yl]amino]butyl)amino]butyl]but-2-ene-1,4-diamine
-
(2Z)-N-[4-(ethylamino)butyl]-N'-(4-[[4-(ethylamino)butyl]amino]butyl)but-2-ene-1,4-diamine
-
-
(2Z)-N-[4-(ethylamino)butyl]-N'-(4-[[4-(ethylamino)butyl]amino]butyl)but-2-ene-1,4-diamine
-
3,8,13,18,23-pentaazapentacosan-1-ol
-
-
3,8,13,18,23-pentaazapentacosan-1-ol
-
N,N'-diethyl-5,11,17,22,27,33-hexaazaoctatriacontane-1,38-diamine
-
-
N,N'-diethyl-5,11,17,22,27,33-hexaazaoctatriacontane-1,38-diamine
-
N,N'-diethyl-5,11,17,23,28,33,39,45-octaazapentacontane-1,50-diamine
-
-
N,N'-diethyl-5,11,17,23,28,33,39,45-octaazapentacontane-1,50-diamine
-
N-ethyl-N'-[[2-([[4-([[2-([[4-(ethylamino)butyl]amino]methyl)cyclopropyl]methyl]amino)butyl]amino]methyl)cyclopropyl]methyl]butane-1,4-diamine
-
-
N-ethyl-N'-[[2-([[4-([[2-([[4-(ethylamino)butyl]amino]methyl)cyclopropyl]methyl]amino)butyl]amino]methyl)cyclopropyl]methyl]butane-1,4-diamine
-
trans-2-phenylcyclopropylamine
i.e. tranylcypromine; Parnate. Mechanism-based suicide inactivator, inactivation of LSD1 occurs with similar rates as the demethylation of substrates
trans-2-phenylcyclopropylamine
i.e. parnate or tranylcypromine, TCP
tranylcypromine
-
inhibits LSD1 by forming a covalent adduct with the flavin moiety through the opening of the inhibitor cyclopropyl ring, binding structure, overview
tranylcypromine
inhibits LSD1 by forming a covalent adduct with the flavin moiety through the opening of the inhibitor cyclopropyl ring, binding structure, overview
tranylcypromine
i.e. Parnate, binding structure analysis and modeling, overview. The LSD1-tranylcypromine complex is not completely composed of the five-membered adduct, but partially contains an intermediate. LSD1-flavin is the only place modified by this inhibition
tranylcypromine
an amino oxidase inhibitor, upregulates hTERT expression and telomerase activity concomitant with elevated H3K4me2 levels and H3 acetylation at the hTERT proximal promoter in cancer cells
additional information
phosphorylation of the H3Ser10 residue totally abolishes the AtLSD1 demethylase activity toward the H3K4me1 peptide
-
additional information
-
phosphorylation of the H3Ser10 residue totally abolishes the AtLSD1 demethylase activity toward the H3K4me1 peptide
-
additional information
design and development of LSD1 inhibitors, overview
-
additional information
-
oligoamine analogues inhibit lysine-specific demethylase 1 and induce reexpression of epigenetically silenced genes, overview. Treatment of HCT-116 colon adenocarcinoma cells in vitro results in increased H3K4 methylation and reexpression of silenced SFRP genes. This reexpression is also accompanied by a decrease in H3K9me2 repressive mark
-
additional information
-
(bis)urea and (bis)thiourea inhibitors of lysine-specific demethylase 1 as epigenetic modulators with the potential for use as antitumor agents, overview. No inhibition by 7 and 17, poor inhibition by 11
-
additional information
besides histone H3, no other core histones exhibit inhibition of KDM1A demethylation activity; KDM1A tolerance for 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS) at 0.01% w/v and dimethyl sulfoxide (DMSO) at 10% v/v
-
additional information
structural analysis of homoserine-substituted inhibitor peptide-bound LSD1-CoREST complex, overview
-
additional information
demethylation activity is decreased by other modifications on the H3 tail, such as acetylation and phosphorylation, suggesting possible regulatory mechanisms
-
additional information
a suicide inhibitor consisting of a 21-residue histone H3 peptide, in which K4 is modified by an N-methylpropargyl group, forms a covalent adduct with the reactive N5 atom of the flavin isoalloxazine ring via the N-methylpropargyl group, permitting the visualization of the first seven residues in the histone H3 peptide in the crystal structure. The residues adopt three successive gamma-turns, resulting in an approximately W-shaped conformation of the H3 peptide backbone. The inhibitor and LSD1 interact through a series of main and side chain hydrogen bonds and van der Waals contacts, further stabilizing the compact conformation of the H3 peptide. Notable interactions with the inhibitor include hydrogen bonds to its R2 and Q5 side chains and a salt bridge interaction between the alpha-amine of A1 and Asp555 in LSD. The addition of acetyl or glycyl blocking groups to the N-terminus of the H3K4me2 peptide or the substitution of the epsilon-amine of A1 with a methyl group disrupts the ionic interaction between Asp555 in LSD1 and the H3 peptide alpha-amine, diminishing specificity over 20fold. And analysis of the LSD1/CoREST-C complex co-crystallized with a 20-residue histone H3 peptide inhibitor in which Lys4 is mutated to a methionine (H3K4M). The overall conformation of the H3K4M peptide is roughly U-shaped, a binding mode that is strikingly different than the gamma-turn geometry adopted by the suicide inhibitor. The peptide's binding is stabilized by a complex network of intramolecular hydrogen bonds and intermolecular hydrogen bonds and van der Waals contacts with residues comprising the substrate binding cleft of LSD1. In particular, multiple hydrogen bonds and salt bridge interactions with the guanidinium groups of R2 and R8 in H3K4M appear to be important in maintaining the peptide's conformation and interactions with LSD1. This binding mode positions M4, which functions as a methyllysine mimic, into the pocket adjacent to the flavin moiety of FAD. Modeling of K4me2 based on the coordinates of the M4 side chain indicates that the dimethyl epsilon-amine group is at an appropriate distance for hydride transfer to the N5 atom in the FAD isoalloxazine ring
-
additional information
trans-2-phenylcyclopropylamine-modified peptides containing a longer side chain, which can react with FAD in the active site, are potent LSD1-selective inhibitors
-
additional information
small molecule inhibitors of LSD1 inhibit xenograft tumor growth
-
additional information
oligoamine analogues are competitive inhibitors of recombinant LSD1. Oligoamine analogues inhibit lysine-specific demethylase 1 and induce reexpression of epigenetically silenced genes, overview. Treatment of HCT-116 colon adenocarcinoma cells in vitro results in increased H3K4 methylation and reexpression of silenced SFRP genes. This reexpression is also accompanied by a decrease in H3K9me2 repressive mark. Use of LSD1 inhibitors in combination with a DNA methyltransferase (DNMT) inhibitors (5-aza-2'-deoxycitidine and 5-azacytidine) is a combination that is not only more efficacious in reactivating specific aberrantly silenced genes but also leads to profound inhibition of the growth of established human colon cancer xenografts in a nude mouse model
-
additional information
N-substituted tranylcypromine derivatives without a basic function or even a polar group are potent inhibitors of LSD1 in vitro and effectively inhibit colony formation of leukemic cells in culture, but block the structurally related monoamine oxidases. The introduction of a polar, non-basic function leads to optimized structures that retain potent LSD1 inhibitors but exhibit selectivity over MAOs and are highly potent in the suppression of colony formation of cultured leukemic cells
-
additional information
inhibitor synthesis and proposed inactivation mechanism of LSD1, overview
-
additional information
histone deacetylase (HDAC) inhibitors are a promising class of anticancer agents for the treatment of solid and hematological malignancies. HDAC inhibitors diminish histone H3 lysine 4 (H3K4) demethylation by LSD1 in vitro. In vivo analysis reveals an increased H3K4 methylation concomitant with inhibition of nucleosomal deacetylation by HDAC inhibitors. Histone H3K4 demethylation is a secondary target of HDAC inhibitors
-
additional information
depletion of LSD1 or inhibition of its activity with monoamine oxidase inhibitors (MAOIs) results in the accumulation of repressive chromatin and a block to viral gene expression
-
additional information
biguanide and bisguanidine polyamine analogues are potent inhibitors of LSD1. These analogues inhibit LSD1 in human colon carcinoma cells and affect a reexpression of multiple, aberrantly silenced genes important in the development of colon cancer, including members of the secreted frizzle-related proteins (SFRPs) and the GATA family of transcription factors. Reexpression is concurrent with increased H3K4me2 and acetyl-H3K9 marks, decreased H3K9me1 and H3K9me2 repressive marks. Inhibition detection via global H3K4me1 and H3K4me2 levels. HCT116 cells are exposed to increasing concentrations of the indicated compound for 48 h,and 00.03 mg of nuclear protein per lane is analyzed for expression of H3K4me1, H3K4me2, and H3K9me2, overview. Exposure to compounds 1c and 2d produces significant increases in both H3K4me1 and H3K4me2, without affecting global H3K9me2 levels
-
additional information
-
in p53-null mice, LSD1 binding is depleted, H3K4me2 is increased, and H3K9me2 remains unchanged compared to those of the wild type
-
additional information
-
TAL1-associated LSD1, HDAC1, and their enzymatic activities are coordinately down-regulated during the early phases of erythroid differentiation
-
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evolution
histone methylation can be reversed by several histone demethylases, including PAD4/PADI4, BHC110/LSD1, and JmjC domain-containing demethylases. a family of multiprotein complexes contains histone deacetylase 1/2 (HDAC1/2) and the histone demethylase LSD1 (BHC110). LSD1 demethylates mono- and dimethyl histone H3 lysine 4 (H3K4) and belongs to a family of FAD-dependent polyamine oxidases which use molecular oxygen as an electron acceptor to oxidize an amine group
evolution
LSD1 belongs to the amine oxidase family which are flavin-dependent enzymes that utilize O2 and generate H2O2 and formaldehyde as byproducts
evolution
LSD1 belongs to the flavin adenine dinucleotide (FAD)-dependent amino oxidase family and is conserved in Schizosaccharomyces pombe through humans
evolution
the enzyme belongs to the JARID family. JARID proteins contain, in addition to the JmjN and JmjC domains, ARID and C5HC2-zinc finger domains, which mediate DNA binding. JARID proteins are, in turn, divided into two subgroups according to the presence, JARID1, or not, JARID2, of chromatin-binding PHD domains
malfunction
-
dysregulation of the enzyme action, in balance with the H3K4 methylation, may be a major cause for vascular inflammation and metabolic memory associated with diabetic complications, overview
malfunction
-
in p53-null mice, LSD1 binding is depleted, H3K4me2 is increased, and H3K9me2 remains unchanged compared to those of the wild type. Partial hepatectomy of wild-type mouse liver and induces a regenerative response, which leads to a loss of p53, increases H3K4me2, and decreases LSD1 interaction at AFP chromatin, in parallel with reactivation of AFP expression
malfunction
-
oocytes from KDM1B-deficient females show a substantial increase in H3K4 methylation and fail to set up the DNA methylation marks at four out of seven imprinted genes examined
malfunction
-
Cre-induced deletion of SALL4 in gene-targeted BM progenitors results in a remarkable decrease of SALL4-bound and LSD1-bound EBF1, accompanied by a 750fold increase of Lys4-dimethylated histon H3. Knockdown of LSD1 in bone marrow hematopoietic stem and progenitor cells leads to altered SALL4 downstream gene expression and increased cellular activity
malfunction
-
loss of LSD1 causes gamma-irradiation hypersensitivity and increased homologous recombination
malfunction
-
LSD1 knockdown by RNA interference or its displacement from the chromatin by antineoplastic agents caused an increase in the levels of a subset of LSD1 target genes
malfunction
pharmacological inhibition of LSD1 in retinal explants cultured from PN1 to PN8 has three major effects. It prevents the normal decrease in expression of genes associated with progenitor function, it blocks rod photoreceptor development, and it increases expression of genes associated with other retinal cell types, e.g. genes Gnat2, Otop3, Pde6c, and Gnb3. Enzyme inhibition blocks rhodopsin expression in PN1 retinal explants, changes in rhodopsin expression caused by trans-2-phenylcyclopropylamine are not secondary to changes in cell proliferation or cell death. LSD1 enzyme inhibition changes the expression of many genes, but does not change the expression levels of these key regulators of retina development, microarrays, detailed overview
malfunction
a KDM1 mutant is embryonic lethal, analysis of demethylase developmental expression patterns and mutant/knockdown phenotypes, overview
malfunction
a KDM1 mutant T08D10.2 shows extended lifespan, analysis of demethylase developmental expression patterns and mutant/knockdown phenotypes, overview
malfunction
a strong increase in H3K4me3 is detected in polytene chromosomes from homozygous lid12367 mutants. Gene lid mutations result in small imaginal discs
malfunction
depletion of LSD1 in an immortalized olfactory-placode-derived cell line (OP6) results in multigenic and multiallelic odorant receptor (OR) transcription per cell, while not seemingly disrupting the ability of these cells to activate new OR genes during clonal expansion. LSD1 depletion does not seem to alter OR representation in OP6 cell populations. Apparent systematic accumulation of H3K4me2 (and possibly H3K9me2) in LSD1-depleted cell populations
malfunction
depletion of LSD1 or inhibition of its activity with monoamine oxidase inhibitors (MAOIs) results in the accumulation of repressive chromatin and a block to viral gene expression. HCF-1 depletion resulted in a concomitant decrease in the recruitment of LSD1
malfunction
Differentiation of neuroblastoma cells results in down-regulation of LSD1. Small interfering RNA-mediated knockdown of LSD1 decreases cellular growth, induces expression of differentiation-associated genes, and increases target gene-specific H3K4 methylation. LSD1 inhibition using monoamine oxidase inhibitors results in an increase of global H3K4 methylation and growth inhibition of neuroblastoma cells in vitro. Small molecule inhibitors of LSD1 inhibit xenograft tumor growth
malfunction
in normal human fibroblasts with a tight hTERT repression, a pharmacological inhibition of LSD1 leads to a weak hTERT expression, and a robust induction of hTERT mRNA occurs when LSD1 and histone deacetylases are both inhibited. Small interference RNA-mediated depletion of both LSD1 and CoREST, a co-repressor in HDAC-containing complexes, synergistically activate hTERT transcription. In cancer cells, inhibition of LSD1 activity or knocking-down of its expression lead to significant increases in levels of hTERT mRNA and telomerase activity, phenotype, overview. LSD1 occupies the hTERT proximal promoter, and its depletion results in elevated dimethylation of histone H3-K4 accompanied by increased H3 acetylation locally in cancer cells
malfunction
inhibition of LSD1 by polyamine analogues increases activating H3K4me2 and acetyl H3K9 marks and decreases repressive H3K9me1 and H3K9me2 marks at the promoters of reexpressed genes
malfunction
knockdown of LSD1 diminishes LSD1 occupancy on the IL1beta and the IL6 promoter, while promoter occupancy on those promoters cannot be detected with an IgG control antibody. Inhibition of LSD1 by an siRNA approach is accompanied by an increase of the active histone mark H3K4me2 and a decrease in the repressive H3K9me2 mark, resulting in activation of IL1beta and IL6 genes after LSD1 silencing
malfunction
mutations of the fly KDM1 homolog lead to sex-specific embryonic lethality and sterility in the surviving (primarily female) offspring, likely due to defects in ovary development, a KDM1 mutant shows female sterility, analysis of demethylase developmental expression patterns and mutant/knockdown phenotypes, overview
malfunction
treatment of HCT-116 colon adenocarcinoma cells with oligoamine analogues inhibitors in vitro results in increased H3K4 methylation and reexpression of silenced SFRP genes. This reexpression is also accompanied by a decrease in H3K9me2 repressive mark
malfunction
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Cre-induced deletion of SALL4 in gene-targeted BM progenitors results in a remarkable decrease of SALL4-bound and LSD1-bound EBF1, accompanied by a 750fold increase of Lys4-dimethylated histon H3. Knockdown of LSD1 in bone marrow hematopoietic stem and progenitor cells leads to altered SALL4 downstream gene expression and increased cellular activity
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malfunction
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a KDM1 mutant is embryonic lethal, analysis of demethylase developmental expression patterns and mutant/knockdown phenotypes, overview
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metabolism
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histone methylation is a dynamic process regulated by the addition of methyl groups by histone methyltransferases and removal of methyl groups from mono- and dimethyllysines by lysine specific demethylase 1, LSD1, and from mono-, di, and trimethyllysines by specific JumonjiC, JmjC, domain-containing demethylases
metabolism
LSD1 microarray transcriptome analysis, overview
metabolism
a family of multiprotein complexes contains histone deacetylase 1/2 (HDAC1/2) and the histone demethylase BHC110 (LSD1). Reconstitution of recombinant complexes reveals a functional connection between HDAC1 and BHC110 only when nucleosomal substrates are present. The enzymatic activity of BHC110 is required to achieve optimal deacetylation in vitro. In vivo functional cross talk between the demethylase and deacetylase enzymes is detected. Demethylation of nucleosomes enhances deacetylation
metabolism
demethylation activity is decreased by other modifications on the H3 tail, such as acetylation and phosphorylation, suggesting possible regulatory mechanisms
metabolism
histone modification is a major mechanism of regulation in gene expression, replication, and repair
metabolism
hyperglycemia/hyperinsulinemia induces changes in expression of chromatin modifying genes and their regulation by histone modifications, overview. Crosstalk between these histone modifications under hyperinsulinemic/hyperglycemic conditions: no change in H3K9me1 levels at the coding regions of histone H3K9 demethylase (Jmjd2b) and H3K4 demethylase (Aof1), and decreased H3K4me1 levels at Myst4 and Jmjd2b, and increased H3K4me1 levels at Set and Aof1. Levels of H3K9me1 are only changed at histone acetylase (Myst4) and deacetylase (Set), highlighting the role of this modification in regulating histone acetylation only. The chromatin remodelling genes Myst4, Jmjd2b, Set, and Aof1 show similar pattern of change for H3Ac and H3K4me1 on Myst4, Jmjd2b, Aof1 and Set gene promoter regions under both low glucose and high glucose condition after insulin stimulation
metabolism
LincRNAFEZF1-AS1 represses p21 expression to promote gastric cancer proliferation through LSD1-mediated H3K4me2 demethylation. FEZF1-AS1 recruits and binds to LSD1 to epigenetically repress downstream gene p21, thereby promoting proliferation in advanced stages of gastric cancer. FEZF1-AS1 is a long non-coding RNA (lncRNA) producing a 2564 bp transcript, located in chromosome 7. FEZF1-AS1 upregulation is associated with tumor size, stage and poor survival of gastric cancer patients. FEZF1-AS1 promotes gastric cancer cells proliferation in vitro and vivo
metabolism
the enzyme is involved in patterns of specific lysine methyl modifications achieved by a precise lysine methylation system, consisting of proteins that add, remove and recognize the specific lysine methyl marks. KDM1/LSD1 is linked to an ERalpha-mediated gene activation program in a ligand-dependent manner, with approximately 58% of ERalpha + promoters also exhibiting KDM1/LSD1 recruitment. H3K27me3 and H3K4me3 demethylation are likely to be coupled, the demethylases are also likely to be involved in the developmentally programmed silencing of PcG targets
metabolism
the enzyme is involved in patterns of specific lysine methyl modifications achieved by a precise lysine methylation system, consisting of proteins that add, remove and recognize the specific lysine methyl marks. KDM1/LSD1 is linked to an ERalpha-mediated gene activation program in a ligand-dependent manner, with approximately 58% of ERalpha + promoters also exhibiting KDM1/LSD1 recruitment. H3K27me3 and H3K4me3 demethylation are likely to be coupled, the demethylases are also likely to be involved in the developmentally programmed silencing of PcG targets
metabolism
the enzyme is involved in patterns of specific lysine methyl modifications achieved by a precise lysine methylation system, consisting of proteins that add, remove and recognize the specific lysine methyl marks. KDM1/LSD1 is linked to an ERalpha-mediated gene activation program in a ligand-dependent manner, with approximately 58% of ERalpha + promoters also exhibiting KDM1/LSD1 recruitment. H3K27me3 and H3K4me3 demethylation are likely to be coupled, the demethylases are also likely to be involved in the developmentally programmed silencing of PcG targets
metabolism
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the enzyme is involved in patterns of specific lysine methyl modifications achieved by a precise lysine methylation system, consisting of proteins that add, remove and recognize the specific lysine methyl marks. KDM1/LSD1 is linked to an ERalpha-mediated gene activation program in a ligand-dependent manner, with approximately 58% of ERalpha + promoters also exhibiting KDM1/LSD1 recruitment. H3K27me3 and H3K4me3 demethylation are likely to be coupled, the demethylases are also likely to be involved in the developmentally programmed silencing of PcG targets
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physiological function
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amine oxidase flavin-containing domain 1, AOF1, is required for de novo DNA methylation of some imprinted genes in oocytes
physiological function
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extensive involvement of LSD1 in gene activation, rather than repression
physiological function
generally LSD1 shows an extensive involvement in gene activation, rather than repression, dual role of LSD1 in gene repression and activation is demonstrated by the fine regulation of growth hormone expression during pituitary development
physiological function
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LSD1 acts as a prime corepressor for TLX, LSD1 interacts directly with TLX via its SWIRM and amine oxidase domains potentiating the transrepressive function of TLX through its histone demethylase activity. LSD1 and TLX are recruited to a TLX-binding site in the PTEN gene promoter, accompanied by the demethylation of H3K4me2 and deacetylation of H3
physiological function
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LSD1 contributes to germline immortality by reprogramming epigenetic memory, H3K4me2 can serve as a stable epigenetic memory, erasure of H3K4me2 by LSD/KDM1 in the germline prevents the inappropriate transmission of this epigenetic memory from one generation to the next
physiological function
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LSD1 is targeted to chromatin by p53, likely in a gene-specific manner, and define a molecular mechanism by which p53 mediates transcription repression in vivo during differentiation
physiological function
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LSD1 plays a role in gene expression regulation, it is a multidomain protein and its involvement in many diverse gene-expression programs is strictly related to its domain organization
physiological function
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LSD1 plays, together with H3K4 methylation, a functional role in inflammation in vascular smooth muscle cells, overview
physiological function
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the enzymatic domain of LSD1 plays an important role in repressing the TAL1-directed transcription. TAL1 recruits LSD1 to the silenced p4.2 promoter in undifferentiated, but not in differentiated, murine erythroleukemia cells. LSD1 negatively regulates TAL1-mediated transcription and suggest that the dynamic regulation of TAL1-associated LSD1/HDAC1 complex determines the onset of erythroid differentiation programs
physiological function
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LSD1 plays an important role in the epigenetic control of gene expression, and aberrant gene silencing secondary to LSD1 overexpression is thought to contribute to the development of cancer
physiological function
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H3K4me2 demethylation marks sites of DNA damage and is cell cycle and LSD1 dependent. LSD1 recruitment to sites of DNA damage is dependent on E3 ligase RNF168, overview. LSD1 is recruited to sites of DNA damage but its retention is relatively transient. LSD1 promotes 53BP1 foci formation primarily in late S/G2 cells, and LSD1 promotes H2A/H2A.X ubiquitylation upon DNA damage
physiological function
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histone demethylase LSD1 is involved in SALL4 mediated transcriptional repression in hematopoietic stem cells, SALL4 and LSD1 co-occupy the same regions of GATA1, CEBPA, and TNF promoters, and SALL4 does dynamically recruit LSD1 to its target genes. LSD1 also appears to act as a central regulator for hematopoietic stem and progenitor cell proliferation and differentiation
physiological function
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LSD1 is regulated in a cell cycle-dependent manner, overview. Histone demethylase LSD1, a component of the CoREST (corepressor for element 1-silencing transcription factor) corepressor complex, plays an important role in the downregulation of gene expression during development, correlation between the genomic levels of LSD1/H3K4me2 and gene expression, including many highly expressed ES cell genes, mechanisms underlying these two distinct functions of LSD1, overview. Cell cycle-dependent association and dissociation of LSD1 with chromatin mediates short-time-scale gene expression changes during embryonic stem cell cycle progression
physiological function
methylation on the N-terminal tails of histone lysines serves as an epigenetic control mechanism, which is regulated by demathylases
physiological function
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methylation on the N-terminal tails of histone lysines serves as an epigenetic control mechanism, which is regulated by demethylases
physiological function
enzyme LSD1 participates in development and differentiation regulation of chromatin remodeling and histone demethylation, and specifically catalyses the demethylation of mono- and di-methylated histone H3 lysine 4 (H3K4) and H3 lysine 9 (H3K9) through a redox process. LSD1 directly binds to the promoter of P21 where it catalyzes H3K4me2 demethylation. FEZF1-AS1, a 2564 bp RNA overexpressed in gastric cancer, epigenetically represses the expression of P21 via binding with LSD1. Knockdown FEZF1-AS1 significantly inhibits gastric cancer cells proliferation by inducing G1 arrest and apoptosis, whereas endogenous expression FEZF1-AS1 promotes cell growth. FEZF1-AS1 epigenetically silences P21 transcription through LSD1-mediated H3K4me2 demethylation
physiological function
LSD1 is an enzyme active at key stages of development in a number of tissues, including the central nervous system. LSD1-mediated demethylation of H3K4me2 is required for the transition from late progenitor to differentiated mouse rod photoreceptor. LSD1 acts in concert with a series of nuclear receptors to modify chromatin structure and repress progenitor genes as well as to inhibit ectopic patterns of gene expression in the differentiating postmitotic retinal cells
physiological function
dimethyl-lysine 4 histone H3 (H3K4me2) is a transcription-activating chromatin mark at gene promoters, and demethylation of this mark by the lysine-specific demethylase 1 (LSD1), a homologue of polyamine oxidases, broadly represses gene expression. Role of LSD1 in the regulation of gene expression, overview
physiological function
enzyme LSD1 participates in development and differentiation regulation of chromatin remodeling and histone demethylation, and specifically catalyses the demethylation of mono- and di-methylated histone H3 lysine 4 (H3K4) and H3 lysine 9 (H3K9) through a redox process. LSD1 directly binds to the promoter of P21 where it catalyzes H3K4me2 demethylation
physiological function
function of the mammalian olfactory system depends on specialized olfactory sensory neurons (OSNs) that each express only one allele of one odorant receptor (OR) gene (monogenic). The lysine-specific demethylase-1 (LSD1) has a role in silencing additional OR alleles in the immortalized olfactory-placode-derived cell line (OP6) cellular context. LSD1 protein removes activating H3K4 or silencing H3K9 methylation marks in a variety of developmental contexts
physiological function
histone demethylases play important roles in epigenetic regulation of gene expression, regulatory mechanisms that modulate demethylase recruitment and activity, overview. Modulation of demethylase activity involves regulation at multiple levels, including gene expression, recruitment, coordination with other epigenetic marks, and post translational modifications. Conserved role for KDM1 in meiosis and germ cell development. Demethylase activity can be modulated by DNA-binding transcription factors, and the local chromatin environment regulates demethylase accessibility. Non-coding RNAs might also play roles in recruiting H3K4 demethylase complexes to establish locus specific epigenetic patterns
physiological function
histone demethylases play important roles in epigenetic regulation of gene expression, regulatory mechanisms that modulate demethylase recruitment and activity, overview. Modulation of demethylase activity involves regulation at multiple levels, including gene expression, recruitment, coordination with other epigenetic marks, and post translational modifications. Conserved role for KDM1 in meiosis and germ cell development. Demethylase activity can be modulated by DNA-binding transcription factors, and the local chromatin environment regulates demethylase accessibility. Non-coding RNAs might also play roles in recruiting H3K4 demethylase complexes to establish locus specific epigenetic patterns
physiological function
histone demethylases play important roles in epigenetic regulation of gene expression, regulatory mechanisms that modulate demethylase recruitment and activity, overview. Modulation of demethylase activity involves regulation at multiple levels, including gene expression, recruitment, coordination with other epigenetic marks, and post translational modifications. Demethylase activity can be modulated by DNA-binding transcription factors, and the local chromatin environment regulates demethylase accessibility. Non-coding RNAs might also play roles in recruiting H3K4 demethylase complexes to establish locus specific epigenetic patterns
physiological function
in non-neural cells, LSD1 removes the transcriptionally active mark of histone H3 Lys4 (H3K4) methyl groups, thereby repressing neuron-specific genes. Recombinant LSD1 alone cannot demethylate nucleosomal H3K4, and CoREST, another component of the complex, is required for the nucleosome-dependent demethylation. LSD1 can act as a transcriptional activator. LSD1 can target different lysine residues and regulate transcription positively or negatively, depending on its binding partners. The large number of LSD1-enriched promoters suggest a broad role in transcriptional regulation for LSD1
physiological function
infection by the alpha-herpesviruses Herpes simplex virus and Varicella zoster virus results in the rapid accumulation of chromatin bearing repressive histone H3 Lys9 methylation. To enable expression of viral immediate early (IE) genes, both viruses use the cellular transcriptional coactivator host cell factor-1, HCF-1, to recruit the lysine-specific demethylase-1, LSD1, to the viral immediate early promoters. LSD1 has a role in viral IE62-mediated activation, LSD1 is crucial for IE gene expression during viral infection, HCF-1-LSD1 complex is essential for alpha-herpesvirus IE gene transcription. Reversible methylation of histone tails serves as either a positive signal recognized by transcriptional assemblies or a negative signal that result in repression. The H3K9 demethylase activity of LSD1 is crucial for nuclear hormone receptor-dependent transcription and cell fate determination, and LSD1 is crucial for viral activator-mediated transcription of herpes simplex virus and varicella zoster virus IE model promoters. As LSD1 can demethylate both H3K4 and H3K9, the coupling of this protein in the HCF-1 Set1 or MLL methyltransferase complex may enhance H3K9 demethylation or preferentially target it to this substrate, although additional histone modifications and modification activities may also contribute to the H3K4 or H3K9 recognition and specificity
physiological function
LSD1 allows transcription factors or corepressor complexes to selectively initiate or repress transcription via demethylation of lysine residues 4 or 9 of histone 3, thereby controlling gene expression programs. LSD1 modulates tumor cell biology by demethylating monomethyl and dimethyl lysines 4 or 9 in histone H3. LSD1 specificity and mechanism of action are complex-dependent. Expression of the chromatin-modifying enzyme lysine-specific demethylase 1 in neuroblastoma is correlated with adverse outcome and inversely correlated with differentiation in neuroblastic tumors
physiological function
LSD1 can repress gene expression through the demethylation H3K4me1/2, this methylation site is associated with transcriptionally poised or active genes. But LSD1 also associates with the androgen receptor (AR) to enhance the expression of AR target genes. LSD1 is implicated in AR-dependent demethylation of H3K9me1/2, a methylation site enriched in silent chromatin. Enzyme Lsd1 demethylate mono- and dimethylated Lys370 in the regulatory domain of the tumor suppressor p53, precluding the binding of the transcriptional coactivator 53BP1. The complexes in which LSD1 resides tightly coordinate its gene regulatory functions and also influence its specificity for histone and non-histone substrates. LSD1 possesses coactivator functions
physiological function
LSD1 catalyzes the demethylation of mono- and dimethylated histone H3-K4 and also H3-K9, it exhibits diverse transcriptional activities by mediating chromatin reconfiguration. LSD1 represses hTERT transcription via demethylating H3-K4 in normal and cancerous cells, and together with HDACs, participates in the establishment of a stable repression state of the hTERT gene in normal or differentiated malignant cells. Role for LSD1 in controlling hTERT transcription
physiological function
LSD1 is a nuclear amine oxidase that utilizes oxygen as an electron acceptor to reduce methylated lysine to form lysine. It demethylates H3K4m1 and H3K4m2, as well as H3K9m1 and H3K9m2 as a removal of the active methylation mark. LSD1 is associated with co-repressor complexes and promotes suppression or activation of gene expression, e.g. LSD1 might be associated to cooperative recruitment to the NFkappaB p65 site for activation in hyperglycemia
physiological function
LSD1 is a nuclear amine oxidase that utilizes oxygen as an electron acceptor to reduce methylated lysine to form lysine. It demethylates H3K4m1 and H3K4m2, as well as H3K9m1 and H3K9m2 as a removal of the active methylation mark. LSD1 is associated with co-repressor complexes and promotes suppression or activation of gene expression, e.g. LSD1 might be associated to cooperative recruitment to the NFkappaB p65 site for activation in hyperglycemia
physiological function
LSD1 is a substrate and an interacting partner of protein kinase CK2. The N-terminal region of LSD1 contains CK2 phosphosites Ser131, Ser137 and Ser166. This domain is not essential for LSD1 catalytic activity but may modulate the interaction with CK2 and with other partners in gene repressing and activating complexes
physiological function
lysine-specific demethylase 1A (KDM1A/LSD1) is a FAD-dependent enzyme that catalyzes the oxidative demethylation of histone H3K4me1/2 and H3K9me1/2 repressing and activating transcription, respectively
physiological function
overexpression of dJARID1/Lid results in a strong reduction in the overall levels of H3K4me3, on the other hand, no significant effects on the levels of H3K9me3, H3K27me3 and H3K36me3 are detected. Independent of its demethylase activity, lid regulates cell proliferation through its interaction with myc
physiological function
the catalytic activity of lysine-specific demethylase 1 (LSD1) is required for regulation of inflammatory cytokines. LSD1 functions as a transcriptional coregulator through demethylating histone H3 on lysine 4 and lysine 9. Repressive role of LSD1 in proinflammatory cytokine expression such as interleukins IL1alpha, IL1beta, IL6, and IL8 and classical complement components, LSD1 occupies and regulates the promoter of these genes. LSD1 regulates several genes of the complement system in Hep-G2 cells. LSD1 binds directly to the promoter of the IL1beta and IL6 genes
physiological function
the inhibition of LSD1 activates energy-expenditure genes by transcriptional and epigenetic mechanisms in adipocytes. Disruption of LSD1 function results in the derepression of these genes leading to the activation of mitochondrial respiration and lipolysis in adipocytes. LSD1-mediated tranxadscriptional repression is FAD-dependent, and the disruption of cellular FAD synthesis exerts similar effects on the metabolic gene expression as the LSD1 inhibition. The expression of LSD1-target genes is markedly repressed in high fat-exposed white adipose tissue, and can be reverted by LSD1 inhibition
physiological function
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histone demethylase LSD1 is involved in SALL4 mediated transcriptional repression in hematopoietic stem cells, SALL4 and LSD1 co-occupy the same regions of GATA1, CEBPA, and TNF promoters, and SALL4 does dynamically recruit LSD1 to its target genes. LSD1 also appears to act as a central regulator for hematopoietic stem and progenitor cell proliferation and differentiation
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physiological function
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LSD1 is a nuclear amine oxidase that utilizes oxygen as an electron acceptor to reduce methylated lysine to form lysine. It demethylates H3K4m1 and H3K4m2, as well as H3K9m1 and H3K9m2 as a removal of the active methylation mark. LSD1 is associated with co-repressor complexes and promotes suppression or activation of gene expression, e.g. LSD1 might be associated to cooperative recruitment to the NFkappaB p65 site for activation in hyperglycemia
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physiological function
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histone demethylases play important roles in epigenetic regulation of gene expression, regulatory mechanisms that modulate demethylase recruitment and activity, overview. Modulation of demethylase activity involves regulation at multiple levels, including gene expression, recruitment, coordination with other epigenetic marks, and post translational modifications. Conserved role for KDM1 in meiosis and germ cell development. Demethylase activity can be modulated by DNA-binding transcription factors, and the local chromatin environment regulates demethylase accessibility. Non-coding RNAs might also play roles in recruiting H3K4 demethylase complexes to establish locus specific epigenetic patterns
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additional information
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inhibition of LSD1 by oligoamines increases activating H3K4me2 and H3K4me1 marks and decreases repressive H3K9me2 marks at the promoters of reexpressed genes
additional information
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mechanism of histone H3 demethylation by demethylase LSD1, overview
additional information
mechanism of histone H3 demethylation by demethylase LSD1, overview
additional information
LSD1 has no DNA-binding domain, LSD1 may interact with nuclear receptors NR2E1/ NR2E3 to bind to specific loci around progenitor genes and its promoters and that this binding is developmentally regulated
additional information
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LSD1 has no DNA-binding domain, LSD1 may interact with nuclear receptors NR2E1/ NR2E3 to bind to specific loci around progenitor genes and its promoters and that this binding is developmentally regulated
additional information
although the active site is expanded compared to that of members of the greater amine oxidase superfamily, it is too much sterically restricted to encompass the minimal 21-mer peptide substrate footprint. The remainder of the substrate/product is therefore expected to extend along the surface of KDM1A
additional information
demethylation by LSD1 is consistent with an amine oxidase-based mechanism in which the methyllysine Nepsilon-CH3 bond is oxidized to an imine intermediate. The reducing equivalents are concomitantly transferred to FAD yielding FADH2, which is recycled to its oxidized state through reduction of molecular oxygen to hydrogen peroxide. The methyllysine imine intermediate subsequently undergoes hydrolysis, resulting in the demethylation of the lysine epsilon-amine group and the release of the byproduct formaldehyde. The reaction mechanism of LSD1 requires a protonatable lysine epsilon-amine for amine oxidation
additional information
KDM1/LSD1-mediated H3K4me2 demethylation and epigenetic regulation model. Model for demethylase regulation by expression, interacting proteins and local chromatin environment
additional information
KDM1/LSD1-mediated H3K4me2 demethylation and epigenetic regulation model. Model for demethylase regulation by expression, interacting proteins and local chromatin environment
additional information
KDM1/LSD1-mediated H3K4me2 demethylation and epigenetic regulation model. Model for demethylase regulation by expression, interacting proteins and local chromatin environment
additional information
transient hyperglycemia induces recruitment of LSD1 to gene regulation sites/promoters
additional information
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transient hyperglycemia induces recruitment of LSD1 to gene regulation sites/promoters
additional information
transient hyperglycemia induces recruitment of LSD1 to gene regulation sites/promoters
additional information
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transient hyperglycemia induces recruitment of LSD1 to gene regulation sites/promoters
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additional information
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KDM1/LSD1-mediated H3K4me2 demethylation and epigenetic regulation model. Model for demethylase regulation by expression, interacting proteins and local chromatin environment
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Lee, M.G.; Wynder, C.; Schmidt, D.M.; McCafferty, D.G.; Shiekhattar, R.
Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications
Chem. Biol.
13
563-567
2006
Mus musculus
brenda
Forneris, F.; Binda, C.; Vanoni, M.A.; Mattevi, A.; Battaglioli, E.
Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process
FEBS Lett.
579
2203-2207
2005
Homo sapiens
brenda
Chen, Y.; Yang, Y.; Wang, F.; Wan, K.; Yamane, K.; Zhang, Y.; Lei, M.
Crystal structure of human histone lysine-specific demethylase 1 (LSD1)
Proc. Natl. Acad. Sci. USA
103
13956-13961
2006
Homo sapiens
brenda
Mimasu, S.; Sengoku, T.; Fukuzawa, S.; Umehara, T.; Yokoyama, S.
Crystal structure of histone demethylase LSD1 and tranylcypromine at 2.25 A
Biochem. Biophys. Res. Commun.
366
15-22
2008
Homo sapiens (O60341)
brenda
Spedaletti, V.; Polticelli, F.; Capodaglio, V.; Schinina, M.E.; Stano, P.; Federico, R.; Tavladoraki, P.
Characterization of a lysine-specific histone demethylase from Arabidopsis thaliana
Biochemistry
47
4936-4947
2008
Arabidopsis thaliana (Q8VXV7), Arabidopsis thaliana
brenda
Katz, D.J.; Edwards, T.M.; Reinke, V.; Kelly, W.G.
A C. elegans LSD1 demethylase contributes to germline immortality by reprogramming epigenetic memory
Cell
137
308-320
2009
Caenorhabditis elegans
brenda
Reddy, M.A.; Villeneuve, L.M.; Wang, M.; Lanting, L.; Natarajan, R.
Role of the lysine-specific demethylase 1 in the proinflammatory phenotype of vascular smooth muscle cells of diabetic mice
Circ. Res.
103
615-623
2008
Mus musculus
brenda
Forneris, F.; Battaglioli, E.; Mattevi, A.; Binda, C.
New roles of flavoproteins in molecular cell biology: histone demethylase LSD1 and chromatin
FEBS J.
276
4304-4312
2009
Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens
brenda
Magerl, C.; Ellinger, J.; Braunschweig, T.; Kremmer, E.; Koch, L.K.; Hoeller, T.; Buettner, R.; Luescher, B.; Guetgemann, I.
H3K4 dimethylation in hepatocellular carcinoma is rare compared with other hepatobiliary and gastrointestinal carcinomas and correlates with expression of the methylase Ash2 and the demethylase LSD1
Hum. Pathol.
41
181-189
2009
Homo sapiens
brenda
Karytinos, A.; Forneris, F.; Profumo, A.; Ciossani, G.; Battaglioli, E.; Binda, C.; Mattevi, A.
A novel mammalian flavin-dependent histone demethylase
J. Biol. Chem.
284
17775-17782
2009
Mus musculus
brenda
Chau, C.M.; Deng, Z.; Kang, H.; Lieberman, P.M.
Cell cycle association of the retinoblastoma protein Rb and the histone demethylase LSD1 with the Epstein-Barr virus latency promoter Cp
J. Virol.
82
3428-3437
2008
Homo sapiens
brenda
Yokoyama, A.; Takezawa, S.; Schuele, R.; Kitagawa, H.; Kato, S.
Transrepressive function of TLX requires the histone demethylase LSD1
Mol. Cell. Biol.
28
3995-4003
2008
Homo sapiens
brenda
Tsai, W.W.; Nguyen, T.T.; Shi, Y.; Barton, M.C.
p53-targeted LSD1 functions in repression of chromatin structure and transcription in vivo
Mol. Cell. Biol.
28
5139-5146
2008
Mus musculus
brenda
Ciccone, D.N.; Su, H.; Hevi, S.; Gay, F.; Lei, H.; Bajko, J.; Xu, G.; Li, E.; Chen, T.
KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints
Nature
461
415-418
2009
Mus musculus
brenda
Hu, X.; Li, X.; Valverde, K.; Fu, X.; Noguchi, C.; Qiu, Y.; Huang, S.
LSD1-mediated epigenetic modification is required for TAL1 function and hematopoiesis
Proc. Natl. Acad. Sci. USA
106
10141-10146
2009
Mus musculus
brenda
Forneris, F.; Binda, C.; Battaglioli, E.; Mattevi, A.
LSD1: oxidative chemistry for multifaceted functions in chromatin regulation
Trends Biochem. Sci.
33
181-189
2008
Drosophila melanogaster, Homo sapiens (O75164)
brenda
Huang, Y.; Stewart, T.M.; Wu, Y.; Baylin, S.B.; Marton, L.J.; Perkins, B.; Jones, R.J.; Woster, P.M.; Casero, R.A.
Novel oligoamine analogues inhibit lysine-specific demethylase 1 and induce reexpression of epigenetically silenced genes
Clin. Cancer Res.
15
7217-7228
2009
Homo sapiens
brenda
Sharma, S.K.; Wu, Y.; Steinbergs, N.; Crowley, M.L.; Hanson, A.S.; Casero, R.A.; Woster, P.M.
(Bis)urea and (bis)thiourea inhibitors of lysine-specific demethylase 1 as epigenetic modulators
J. Med. Chem.
53
5197-5212
2010
Homo sapiens
brenda
Luka, Z.; Moss, F.; Loukachevitch, L.V.; Bornhop, D.J.; Wagner, C.
Histone demethylase LSD1 is a folate-binding protein
Biochemistry
50
4750-4756
2011
Homo sapiens
brenda
Liu, L.; Souto, J.; Liao, W.; Jiang, Y.; Li, Y.; Nishinakamura, R.; Huang, S.; Rosengart, T.; Yang, V.; Schuster, M.; Ma, Y.; Yang, J.
Histone demethylase LSD1 is involved in SALL4 mediated transcriptional repression in hematopoietic stem cells
J. Biol. Chem.
288
34719-34728
2013
Mus musculus, Mus musculus C57/BL6J
brenda
Mosammaparast, N.; Kim, H.; Laurent, B.; Zhao, Y.; Lim, H.J.; Majid, M.C.; Dango, S.; Luo, Y.; Hempel, K.; Sowa, M.E.; Gygi, S.P.; Steen, H.; Harper, J.W.; Yankner, B.; Shi, Y.
The histone demethylase LSD1/KDM1A promotes the DNA damage response
J. Cell Biol.
203
457-470
2013
Homo sapiens
brenda
Nair, V.D.; Ge, Y.; Balasubramaniyan, N.; Kim, J.; Okawa, Y.; Chikina, M.; Troyanskaya, O.; Sealfon, S.C.
Involvement of histone demethylase LSD1 in short-time-scale gene expression changes during cell cycle progression in embryonic stem cells
Mol. Cell. Biol.
32
4861-4876
2012
Mus musculus
brenda
Burg, J.M.; Gonzalez, J.J.; Maksimchuk, K.R.; McCafferty, D.G.
Lysine-specific demethylase 1A (KDM1A/LSD1) product recognition and kinetic analysis of full-length histones
Biochemistry
55
1652-1662
2016
Homo sapiens (O60341)
brenda
Amano, Y.; Kikuchi, M.; Sato, S.; Yokoyama, S.; Umehara, T.; Umezawa, N.; Higuchi, T.
Development and crystallographic evaluation of histone H3 peptide with N-terminal serine substitution as a potent inhibitor of lysine-specific demethylase 1
Bioorg. Med. Chem.
25
2617-2624
2017
Homo sapiens (O60341)
brenda
Liu, Y.W.; Xia, R.; Lu, K.; Xie, M.; Yang, F.; Sun, M.; De, W.; Wang, C.; Ji, G.
LincRNAFEZF1-AS1 represses p21 expression to promote gastric cancer proliferation through LSD1-mediated H3K4me2 demethylation
Mol. Cancer
16
39
2017
Homo sapiens (O60341)
brenda
Vyas, R.N.; Meredith, D.; Lane, R.P.
Lysine-specific demethylase-1 (LSD1) depletion disrupts monogenic and monoallelic odorant receptor (OR) expression in an olfactory neuronal cell line
Mol. Cell. Neurosci.
82
1-11
2017
Mus musculus (Q6ZQ88)
brenda
Popova, E.Y.; Pinzon-Guzman, C.; Salzberg, A.C.; Zhang, S.S.; Barnstable, C.J.
LSD1-mediated demethylation of H3K4me2 is required for the transition from late progenitor to differentiated mouse rod photoreceptor
Mol. Neurobiol.
53
4563-4581
2016
Mus musculus (Q6ZQ88), Mus musculus
brenda
Mimasu, S.; Sengoku, T.; Fukuzawa, S.; Umehara, T.; Yokoyama, S.
Crystal structure of histone demethylase LSD1 and tranylcypromine at 2.25 A
Biochem. Biophys. Res. Commun.
366
15-22
2008
Homo sapiens (O60341)
brenda
Janzer, A.; Lim, S.; Fronhoffs, F.; Niazy, N.; Buettner, R.; Kirfel, J.
Lysine-specific demethylase 1 (LSD1) and histone deacetylase 1 (HDAC1) synergistically repress proinflammatory cytokines and classical complement pathway components
Biochem. Biophys. Res. Commun.
421
665-670
2012
Homo sapiens (O60341)
brenda
Yang, M.; Culhane, J.C.; Szewczuk, L.M.; Jalili, P.; Ball, H.L.; Machius, M.; Cole, P.A.; Yu, H.
Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2-phenylcyclopropylamine
Biochemistry
46
8058-8065
2007
Homo sapiens (O60341)
brenda
Gaweska, H.; Henderson Pozzi, M.; Schmidt, D.M.; McCafferty, D.G.; Fitzpatrick, P.F.
Use of pH and kinetic isotope effects to establish chemistry as rate-limiting in oxidation of a peptide substrate by LSD1
Biochemistry
48
5440-5445
2009
Homo sapiens (O60341)
brenda
Luka, Z.; Moss, F.; Loukachevitch, L.V.; Bornhop, D.J.; Wagner, C.
Histone demethylase LSD1 is a folate-binding protein
Biochemistry
50
4750-4756
2011
Homo sapiens (O60341)
brenda
Marmorstein, R.; Trievel, R.C.
Histone modifying enzymes structures, mechanisms, and specificities
Biochim. Biophys. Acta
1789
58-68
2009
Homo sapiens (O60341)
brenda
Costa, R.; Arrigoni, G.; Cozza, G.; Lolli, G.; Battistutta, R.; Izpisua Belmonte, J.C.; Pinna, L.A.; Sarno, S.
The lysine-specific demethylase 1 is a novel substrate of protein kinase CK2
Biochim. Biophys. Acta
1844
722-729
2014
Homo sapiens (O60341)
brenda
Gupta, J.; Kumar, S.; Li, J.; Krishna Murthy Karuturi, R.; Tikoo, K.
Histone H3 lysine 4 monomethylation (H3K4me1) and H3 lysine 9 monomethylation (H3K9me1) distribution and their association in regulating gene expression under hyperglycaemic/hyperinsulinemic conditions in 3T3 cells
Biochimie
94
2656-2664
2012
Mus musculus (Q8CIG3)
brenda
Duan, Y.; Qin, W.; Suo, F.; Zhai, X.; Guan, Y.; Wang, X.; Zheng, Y.; Liu, H.
Design, synthesis and in vitro evaluation of stilbene derivatives as novel LSD1 inhibitors for AML therapy
Bioorg. Med. Chem.
26
6000-6014
2018
Homo sapiens (O60341)
brenda
Kakizawa, T.; Ota, Y.; Itoh, Y.; Suzuki, T.
Histone H3 peptides incorporating modified lysine residues as lysine-specific demethylase 1 inhibitors
Bioorg. Med. Chem. Lett.
28
167-169
2018
Homo sapiens (O60341)
brenda
Schulte, J.H.; Lim, S.; Schramm, A.; Friedrichs, N.; Koster, J.; Versteeg, R.; Ora, I.; Pajtler, K.; Klein-Hitpass, L.; Kuhfittig-Kulle, S.; Metzger, E.; Schuele, R.; Eggert, A.; Buettner, R.; Kirfel, J.
Lysine-specific demethylase 1 is strongly expressed in poorly differentiated neuroblastoma implications for therapy
Cancer Res.
69
2065-2071
2009
Homo sapiens (O60341)
brenda
Huang, Y.; Stewart, T.M.; Wu, Y.; Baylin, S.B.; Marton, L.J.; Perkins, B.; Jones, R.J.; Woster, P.M.; Casero, R.A.
Novel oligoamine analogues inhibit lysine-specific demethylase 1 and induce reexpression of epigenetically silenced genes
Clin. Cancer Res.
15
7217-7228
2009
Homo sapiens (O60341)
brenda
Lan, F.; Nottke, A.C.; Shi, Y.
Mechanisms involved in the regulation of histone lysine demethylases
Curr. Opin. Cell Biol.
20
316-325
2008
Mus musculus (Q6ZQ88), Drosophila melanogaster (Q9VMJ7), Caenorhabditis elegans (Q9XWP6), Mus musculus C57BL/6J (Q6ZQ88)
brenda
Brasacchio, D.; Okabe, J.; Tikellis, C.; Balcerczyk, A.; George, P.; Baker, E.K.; Calkin, A.C.; Brownlee, M.; Cooper, M.E.; El-Osta, A.
Hyperglycemia induces a dynamic cooperativity of histone methylase and demethylase enzymes associated with gene-activating epigenetic marks that coexist on the lysine tail
Diabetes
58
1229-1236
2009
Homo sapiens (O60341), Homo sapiens, Mus musculus (Q6ZQ88), Mus musculus C57BL/6 (Q6ZQ88)
brenda
Schulz-Fincke, J.; Hau, M.; Barth, J.; Robaa, D.; Willmann, D.; Kuerner, A.; Haas, J.; Greve, G.; Haydn, T.; Fulda, S.; Luebbert, M.; Luedeke, S.; Berg, T.; Sippl, W.; Schuele, R.; Jung, M.
Structure-activity studies on N-substituted tranylcypromine derivatives lead to selective inhibitors of lysine specific demethylase 1 (LSD1) and potent inducers of leukemic cell differentiation
Eur. J. Med. Chem.
144
52-67
2018
Homo sapiens (O60341)
brenda
Forneris, F.; Binda, C.; Vanoni, M.A.; Mattevi, A.; Battaglioli, E.
Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process
FEBS Lett.
579
2203-2207
2005
Homo sapiens (O60341)
brenda
Hirano, K.; Namihira, M.
FAD influx enhances neuronal differentiation of human neural stem cells by facilitating nuclear localization of LSD1
FEBS open bio
7
1932-1942
2017
Homo sapiens (O60341)
brenda
Tan, A.H.Y.; Tu, W.; McCuaig, R.; Hardy, K.; Donovan, T.; Tsimbalyuk, S.; Forwood, J.K.; Rao, S.
Lysine-specific histone demethylase 1A regulates macrophage polarization and checkpoint molecules in the tumor microenvironment of triple-negative breast cancer
Front. Immunol.
10
1351
2019
Mus musculus (Q6ZQ88), Mus musculus
brenda
Culhane, J.C.; Szewczuk, L.M.; Liu, X.; Da, G.; Marmorstein, R.; Cole, P.A.
A mechanism-based inactivator for histone demethylase LSD1
J. Am. Chem. Soc.
128
4536-4537
2006
Homo sapiens (O60341)
brenda
Lee, M.G.; Wynder, C.; Bochar, D.A.; Hakimi, M.A.; Cooch, N.; Shiekhattar, R.
Functional interplay between histone demethylase and deacetylase enzymes
Mol. Cell. Biol.
26
6395-6402
2006
Homo sapiens (O60341)
brenda
Hino, S.; Sakamoto, A.; Nagaoka, K.; Anan, K.; Wang, Y.; Mimasu, S.; Umehara, T.; Yokoyama, S.; Kosai, K.; Nakao, M.
FAD-dependent lysine-specific demethylase-1 regulates cellular energy expenditure
Nat. Commun.
3
758
2012
Mus musculus (Q6ZQ88)
brenda
Liang, Y.; Vogel, J.; Narayanan, A.; Peng, H.; Kristie, T.
Inhibition of the histone demethylase LSD1 blocks alpha-herpesvirus lytic replication and reactivation from latency
Nat. Med.
15
1312-1317
2009
Homo sapiens (O60341)
brenda
Matsuda, S.; Baba, R.; Oki, H.; Morimoto, S.; Toyofuku, M.; Igaki, S.; Kamada, Y.; Iwasaki, S.; Matsumiya, K.; Hibino, R.; Kamada, H.; Hirakawa, T.; Iwatani, M.; Tsuchida, K.; Hara, R.; Ito, M.; Kimura, H.
T-448, a specific inhibitor of LSD1 enzyme activity, improves learning function without causing thrombocytopenia in mice
Neuropsychopharmacology
44
1505-1512
2019
Mus musculus (Q6ZQ88)
brenda
Lloret-Llinares, M.; Carre, C.; Vaquero, A.; de Olano, N.; Azorin, F.
Characterization of Drosophila melanogaster JmjC+N histone demethylases
Nucleic Acids Res.
36
2852-2863
2008
Drosophila melanogaster (Q9VMJ7)
brenda
Zhu, Q.; Liu, C.; Ge, Z.; Fang, X.; Zhang, X.; Straat, K.; Bjoerkholm, M.; Xu, D.
Lysine-specific demethylase 1 (LSD1) is required for the transcriptional repression of the telomerase reverse transcriptase (hTERT) gene
PLoS ONE
3
e1446
2008
Homo sapiens (O60341)
brenda
Kong, X.; Ouyang, S.; Liang, Z.; Lu, J.; Chen, L.; Shen, B.; Li, D.; Zheng, M.; Li, K.K.; Luo, C.; Jiang, H.
Catalytic mechanism investigation of lysine-specific demethylase 1 (LSD1) a computational study
PLoS ONE
6
e25444
2011
Homo sapiens (O60341)
brenda
Huang, Y.; Greene, E.; Murray Stewart, T.; Goodwin, A.C.; Baylin, S.B.; Woster, P.M.; Casero, R.A.
Inhibition of lysine-specific demethylase 1 by polyamine analogues results in reexpression of aberrantly silenced genes
Proc. Natl. Acad. Sci. USA
104
8023-8028
2007
Homo sapiens (O60341)
brenda