Information on EC 1.14.11.B2 - [histone-H3]-lysine-4-demethylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.11.B2
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
[histone-H3]-lysine-4-demethylase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
protein N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2 = protein N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
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-
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
gene MAL8P1.111
-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dimethyl-histone 3-Lys4 peptide + H2O
histone 3-Lys4 peptide + ?
show the reaction diagram
-
amino acids 1-21 of histone 3
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
protein 6-N,6-N-dimethyl-L-lysine + 2-oxoglutarate + O2
protein 6-N-methyl-L-lysine + succinate + formaldehyde + CO2
show the reaction diagram
-
LSD1 relieves repressive histone marks by demethylation of histone H3 at lysine 9, thereby leading to derepression of androgen receptor target genes
-
-
?
protein 6-N-methyl-L-lysine + 2-oxoglutarate + O2
protein L-lysine + succinate + formaldehyde + CO2
show the reaction diagram
-
LSD1 relieves repressive histone marks by demethylation of histone H3 at lysine 9, thereby leading to derepression of androgen receptor target genes
-
-
?
[chromodomain Y-like protein]-N6,N6,N6-trimethyl-L-lysine135 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
[Cockayne syndrome group B protein]-N6,N6,N6-trimethyl-L-lysine1054 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
[Cockayne syndrome group B protein]-N6,N6,N6-trimethyl-L-lysine170 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
[Cockayne syndrome group B protein]-N6,N6,N6-trimethyl-L-lysine297 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
[Cockayne syndrome group B protein]-N6,N6,N6-trimethyl-L-lysine448 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
[Dnmt1]-methyl-L-lysine + 2-oxoglutarate + O2
[Dnmt1]-L-lysine + succinate + formaldehyde + CO2
show the reaction diagram
[Dnmt1]-methyl-L-lysine-1096 + 2-oxoglutarate + O2
[Dnmt1]-L-lysine-1096 + succinate + formaldehyde + CO2
show the reaction diagram
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human substrate protein, demethylation of the non-histone substrate at the Set7/9 methylation site Lys1096. Dnmt1, which contains over 120 lysine residues, seems to be methylated at multiple sites, as metabolic labeling experiments reveal that mutating K1096 in mouse Dnmt1 slightly reduces, but does not abolish, Dnmt1 methylation. Probably methylation at other sites is also involved in the regulation of Dnmt1 stability
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-
?
[Dnmt1]-methyl-L-lysine1096 + 2-oxoglutarate + O2
[Dnmt1]-L-lysine1096 + succinate + formaldehyde + CO2
show the reaction diagram
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mechanistic link between the histone and DNA methylation systems
-
-
?
[G9a protein]-N6,N6,N6-trimethyl-L-lysine185 + 2-oxoglutarate + O2
?
show the reaction diagram
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a customer synthesized protein
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-L-lysine36 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6-methyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
[histone-H3]-dimethyllysine4 + 2-oxoglutarate + O2
?
show the reaction diagram
[histone-H3]-tridimethyllysine4 + 2-oxoglutarate + O2
?
show the reaction diagram
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RBP2 is a demethylase that specifically catalyzes demethylation. RBP2 displayes robust H3K4 demethylase activity against H3K4me3 and me2, resulting in 80%-90% demethylation of the modified substrate, but fails to catalyze removal of the me1 modification state. The enzyme is capable of processively demethylating the H3K4me3 and me2 modifications to the unmodified state
-
-
?
[histone-H3]-trimethyllysine4 + 2-oxoglutarate + O2
?
show the reaction diagram
[p53]-methyl-L-lysine + 2-oxoglutarate + O2
[p53]-L-lysine + succinate + formaldehyde + CO2
show the reaction diagram
[widely interspaced zinc finger motifs protein]-N6,N6,N6-trimethyl-L-lysine305 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
protein 6-N,6-N-dimethyl-L-lysine + 2-oxoglutarate + O2
protein 6-N-methyl-L-lysine + succinate + formaldehyde + CO2
show the reaction diagram
-
LSD1 relieves repressive histone marks by demethylation of histone H3 at lysine 9, thereby leading to derepression of androgen receptor target genes
-
-
?
protein 6-N-methyl-L-lysine + 2-oxoglutarate + O2
protein L-lysine + succinate + formaldehyde + CO2
show the reaction diagram
-
LSD1 relieves repressive histone marks by demethylation of histone H3 at lysine 9, thereby leading to derepression of androgen receptor target genes
-
-
?
[Dnmt1]-methyl-L-lysine + 2-oxoglutarate + O2
[Dnmt1]-L-lysine + succinate + formaldehyde + CO2
show the reaction diagram
-
LSD1 demethylates the protein and regulates its function
-
-
?
[Dnmt1]-methyl-L-lysine1096 + 2-oxoglutarate + O2
[Dnmt1]-L-lysine1096 + succinate + formaldehyde + CO2
show the reaction diagram
-
mechanistic link between the histone and DNA methylation systems
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-L-lysine36 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6-methyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
[histone-H3]-dimethyllysine4 + 2-oxoglutarate + O2
?
show the reaction diagram
[histone-H3]-tridimethyllysine4 + 2-oxoglutarate + O2
?
show the reaction diagram
-
RBP2 is a demethylase that specifically catalyzes demethylation. RBP2 displayes robust H3K4 demethylase activity against H3K4me3 and me2, resulting in 80%-90% demethylation of the modified substrate, but fails to catalyze removal of the me1 modification state. The enzyme is capable of processively demethylating the H3K4me3 and me2 modifications to the unmodified state
-
-
?
[histone-H3]-trimethyllysine4 + 2-oxoglutarate + O2
?
show the reaction diagram
[p53]-methyl-L-lysine + 2-oxoglutarate + O2
[p53]-L-lysine + succinate + formaldehyde + CO2
show the reaction diagram
-
LSD1 demethylates the protein and regulates its function
-
-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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LSD1 recruitment to sites of DNA damage is dependent on E3 ligase RNF168, RNF168 interacts with LSD1, overview. Rapid, transient recruitment of RNF168 to damage sites is H2A.X independent
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
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iron-dependent dioxygenase
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(12E)-N,N'-diethyl-5,10,16,21-tetraazapentacos-12-ene-1,25-diamine
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(13Z)-N,N'-diethyl-6,11,16,21-tetraazahexacos-13-ene-1,26-diamine
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(19E)-N,N'-diethyl-6,12,17,22,27,33-hexaazaoctatriacont-19-ene-1,38-diamine
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(19Z)-N,N'-diethyl-6,12,17,22,27,33-hexaazaoctatriacont-19-ene-1,38-diamine
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(25E)-N,N'-diethyl-5,11,17,23,28,33,39,45-octaazapentacont-25-ene-1,50-diamine
-
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(25Z)-N,N'-diethyl-6,12,18,23,28,33,39,45-octaazapentacont-25-ene-1,50-diamine
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(2Z)-N-ethyl-N'-[4-[(4-[[(2Z)-4-(ethylamino)but-2-en-1-yl]amino]butyl)amino]butyl]but-2-ene-1,4-diamine
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(2Z)-N-[4-(ethylamino)butyl]-N'-(4-[[4-(ethylamino)butyl]amino]butyl)but-2-ene-1,4-diamine
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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
-
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
-
82.9% inhibition at 0.01 mM
1,12-bis-[3-[1-(3,3-diphenylpropyl)thioureado]]-4,9-diazadodecane
-
21.4% inhibition at 0.01 mM
1,12-bis-[3-[1-(3,3-diphenylpropyl)ureado]]-4,9-diazadodecane
-
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
-
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
-
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-[3-[1-(1,1-diphenylmethyl)thioureado]]-4,12-diazapentadecane
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71.1% inhibition at 0.01 mM
1,15-bis-[3-[1-(2,2-diphenylethyl)thioureado]]-4,12-diazapentadecane
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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
1,2-dimethyl-3-[(13E)-13-(methylamino)-4,8,12,14-tetraazapentadec-13-en-1-yl]guanidine
-
1 mM, about 80% inhibition. Inhibition affects a reexpression of multiple, aberrantly silenced genes important in the develoment of colon cancer. Reexpression is concurrent with increased dimethylated histone 3 lysine 4 and acetyl-histone 3 lysine 4 marks
1-(2,2-diphenylethyl)-3-(14-imino-17,17-diphenyl-4,9,13,15-tetraazaheptadec-1-yl)guanidine
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1 mM, about 55% inhibition. Inhibition affects a reexpression of multiple, aberrantly silenced genes important in the develoment of colon cancer. Reexpression is concurrent with increased dimethylated histone 3 lysine 4 and acetyl-histone 3 lysine 4 marks
1-(3,3-diphenylpropyl)-3-(14-imino-18,18-diphenyl-4,9,13,15-tetraazaoctadec-1-yl)guanidine
-
1 mM, about 60% inhibition. Inhibition affects a reexpression of multiple, aberrantly silenced genes important in the develoment of colon cancer. Reexpression is concurrent with increased dimethylated histone 3 lysine 4 and acetyl-histone 3 lysine 4 marks
3,8,13,18,23-pentaazapentacosan-1-ol
-
-
bis-[3-[1-(benzyl)thioureado]]-4,9-diazadodecane
-
25.2% inhibition at 0.01 mM
Co2+
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cobalt ions increase H3K9me3 and H3K36me3 by inhibiting histone demethylation process. cobalt ions do not affect JMJD2A protein level but directly inhibit its demethylase activity. Exposure of both lung carcinoma A549 cells and bronchial epithelial Beas-2B cells, to CoCl2 at 0.2 mM for 24 h increases methylation of histone H3 lysine residues 4, 9, 27 and 36, i.e. H3K4me3, H3K9me2, H3K9me3, H3K27me3, H3K36me3, as well as ubiquitination of histone H2A and H2B, while it decreases acetylation at histone H4, overview
N'-(13,15-diimino-18,18-diphenyl-4,8,12,14,16-pentaazaoctadec-1-yl)-N-(2,2-diphenylethyl)imidodicarbonimidic diamide
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1 mM, about 65% inhibition. Inhibition affects a reexpression of multiple, aberrantly silenced genes important in the develoment of colon cancer. Reexpression is concurrent with increased dimethylated histone 3 lysine 4 and acetyl-histone 3 lysine 4 marks
N'-(14,16-diimino-20,20-diphenyl-4,9,13,15,17-pentaazaicos-1-yl)-N-(3,3-diphenylpropyl)imidodicarbonimidic diamide
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1 mM, about 70% inhibition. Inhibition affects a reexpression of multiple, aberrantly silenced genes important in the develoment of colon cancer. Reexpression is concurrent with increased dimethylated histone 3 lysine 4 and acetyl-histone 3 lysine 4 marks
N'-(17,19-diimino-23,23-diphenyl-4,12,16,18,20-pentaazatricos-1-yl)-N-(3,3-diphenylpropyl)imidodicarbonimidic diamide
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1 mM, about 90% inhibition. Inhibition affects a reexpression of multiple, aberrantly silenced genes important in the develoment of colon cancer. Reexpression is concurrent with increased dimethylated histone 3 lysine 4 and acetyl-histone 3 lysine 4 marks
N,N'-diethyl-5,11,17,22,27,33-hexaazaoctatriacontane-1,38-diamine
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N,N'-diethyl-5,11,17,23,28,33,39,45-octaazapentacontane-1,50-diamine
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N-ethyl-N'-[[2-([[4-([[2-([[4-(ethylamino)butyl]amino]methyl)cyclopropyl]methyl]amino)butyl]amino]methyl)cyclopropyl]methyl]butane-1,4-diamine
-
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N-oxalylglycine
i.e. NOG, a non-reactive 2-oxoglutarate analogue
Ni2+
substitutes Fe2+ and inhibits the hydroxylation reaction
Pargyline
Tranylcypromine
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
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required
HP1a
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Suv(Var)3-9/KMT1 interacts with HP1 that binds [histone H3]-N6,N6-trimethyl-L-lysine9
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N-oxalylglycine
required, essential for the demethylase activity in vivo
tetrahydrofolate
-
-
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00029
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recombinant purified isozyme JMJD2B, substrate histone H3K9
0.0005
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recombinant purified isozyme JMJD2C, substrate histone H3K9
0.001
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recombinant purified isozyme JMJD2A, substrate histone H3K9
additional information
-
specific isozyme activities with non-histone substrates, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 7.5
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assay at
7.9
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assay at
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
25
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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of control and hyperglycemic mice
Manually annotated by BRENDA team
histone H3-K4 demethylase is restricted to the corpus luteum
Manually annotated by BRENDA team
-
LSD1 is strongly expressed in poorly differentiated neuroblastomas, real-time reverse transcription-PCR expression analysis
Manually annotated by BRENDA team
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histone H3 lysine 4 demethylase JARID1B is up-regulated in prostate cancer. JARID1B associates with androgen receptor and regulates its transcriptional activity
Manually annotated by BRENDA team
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lysine-specific demethylase 1 colocalizes with androgen receptor
Manually annotated by BRENDA team
-
lysine-specific demethylase 1 colocalizes with androgen receptor
Manually annotated by BRENDA team
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JMJ703 is expressed at relatively high levels in leaves of 7 d-after-germination in seedlings compared with all of the other tissues tested
Manually annotated by BRENDA team
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Beko cell, spontaneous T-cell lymphoma cell line derived from T-cell receptor beta knockout mice, only KDM5A and KDM5C are expressed
Manually annotated by BRENDA team
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specific expression of PLU-1
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
LSD1 is present on chromatin in both the presence and the absence of estrogens
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
about, recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 95059, LSD1 without N-terminal methionine, mass spectrometry
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallization of JMJD2A in complex with histone H3 peptides bearing different methylated forms of K9 and K36, cocrystallization of inactivated substrate with either N-oxalylglycine, a non-reactive 2-OG analog, or with Ni(II), which substitutes for Fe(II) and inhibits the hydroxylation reaction. Structures analysis, overview
in complex with inhibitor tranylcypromine, diffraction to 2.25 A. In the inhibitor-free structure, a water molecule forms a hydrogen bond with the flavin N(5) atom and Lys661. The LSD1-tranylcypromine complex is not completely composed of the five-membered adduct, but partially contains an intermediate
purified recombinant enzyme, free or in complex with N-oxalylglycine, X-ray diffraction structure determination and analysis at 2.35 A resolution
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant FLAG:HA-tagged JmjN-JmjC-zinc finger region from Nicotiana tabacum leaf nuclei byy affinity chromatography
recombinant GST-tagged isozymes JMJD2A, JMJD2B, and JMJD2C from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography
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recombinant His-tagged N-terminal fragment of JARID1B from Sf9 insect cells by nickel affinity chromatography
-
recombinant N-terminally His-tagged enzyme by nickel affinity chromatography from Escherichia coli BL21(DE3), or by ammonium sulfate fractionation and anion exchange chromatography, recombinant N-terminally truncated GST-tagged LSD1 by glutathione affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA encoding for Myc-tagged JARID1B is transfected into HeLa cells, and the effect on histone lysine methylation is examined
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co-expression of FLAG-CMV-tagged hPc2 and the HA-tagged N-terminal fragment of JARDI1B in HEK-293T cells. Expression the His-tagged N-terminal fragment of JARID1B in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
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coexpression of HA-tagged SALL4 and FLAG-tagged LSD1 in HEK-293 cells, coexpression of LSD1 and SALL4 proteins in mouse bone marrow hematopoietic stem and progenitor cells
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expression in Escherichia coli
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expression of FLAG-tagged JMJD2A in Spodoptera frugiperda Sf9 cells
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expression of FLAG-tagged wild-type and H190A mutant Jmjd2c in mouse embryonic fibroblasts
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expression of His6-tagged LSD1 in Escherichia coli strain BL21(DE3)
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fragment consisting of residues 172-833, expression as glutathione S-transferase fusion protein in Escherichia coli
full-length Flag-tagged human PLU-1 is expressed in SF9 cells. PLU-1 is overexpressed in U2OS cells
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gene Aof1
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gene Aof2
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gene JMJ703, functional overexpression of YFP-HA-tagged JMJ703 in Nicotiana tabacum cells
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gene JMJ703, functional transient overexpression of the FLAG:HA-tagged JmjN-JmjC-zinc finger region in Nicotiana tabacum leaf nuclei
gene JMJ706, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression as GST-fusion protein
gene Kdm5c, encoded on the X-chromosome, genotyping, quantitative real-time RT-PCR expression analysis
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gene MAL8P1.111, located on chromosome 8, DNA and amino acid sequence determination and analysis, detailed phylogenetic analysis, overview
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JMJD2A-C genes, DNA and amino acid sequence determination and analysis, expression of the GST-tagged isozymes JMJD2A, JMJD2B, and JMJD2C in Escherichia coli strain BL21(DE3)
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LSD1 genome-wide mapping and expression analysis, LSD1 genomic regions overlap H3K4me2 regions, transcriptional corepressor LSD1 is enriched at the promoter regions of highly expressed genes in ES cells
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overexpression of FLAG-tagged CG15835 in S2 cells
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real-time reverse transcription-PCR expression analysis
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stable overexpression of N-terminally HA-tagged Fbxl10 in murine embryonic fibroblasts leading to an increase in cell and nuclear size and changes the transcriptome, but with no effect on proliferation, mitosis, and apoptosis or global histone marks, quantitative real-time PCR expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
differentiation of neuroblastoma cells results in down-regulation of LSD1
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LSD1 expression in the brain is induced both region and cell specifically after ischemic/perfusion
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S288A
the mutant displays enhanced specificity for H3K9me2 and H3K36me2 without altering activity toward trimethyllysines, consistent with the H3K9me2/3 specificity of JMJD2D which possesses an alanine, Ala29, in this position. Kinetic analysis of S288A mutant shows a 12fold increase in H3K9me2 specificity versus the native enzyme, whereas the converse A291S mutant in JMJD2D reduces H3K9me2 specificity approximately fivefold
H190A
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inactive mutant
H483A
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inactive KDM5A mutant
K1096R
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the mutant Dnmt1 shows highly reduced Dnmt1 methylation activity compared to the wild-type enzyme, and is more stable than wild-type Dnmt1 when expressed in Dnmt1-/- embryonic stem cells
E396A
site directed mutagenesis of a Fe2+ binding active site residue, inactive mutant, the mutation impairs the H3K4 demethylase activity of JMJ703 in tobacco cells
G376A
site directed mutagenesis, inactive mutant, the mutation impairs the H3K4 demethylase activity of JMJ703 in tobacco cells, the mutation impairs the H3K4 demethylase activity of JMJ703 in tobacco cells
H394A
site directed mutagenesis of a Fe2+ binding active site residue, inactive mutant
H482A
site directed mutagenesis of a Fe2+ binding active site residue, inactive mutant
K412A
site directed mutagenesis, the mutation abolishes the demethylation activity of H3K4 in all three methylation states
N496A
site directed mutagenesis, the mutant retains a residual activity to demethylate H3K4me2/3, the mutation impairs the H3K4 demethylase activity of JMJ703 in tobacco cells
Y321A
site directed mutagenesis decreases H3K4me1 demethylase activity but does not affect H3K4me2 and H3K4me3 demethylase activity
Y383A
site directed mutagenesis, the mutant retains a residual activity to demethylate H3K4me2, the mutation impairs the H3K4 demethylase activity of JMJ703 in tobacco cells
additional information