Information on EC 1.14.11.B1 - [histone-H3]-lysine-9-demethylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.11.B1
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
[histone-H3]-lysine-9-demethylase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
protein N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2 = protein N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene PFF1440w
-
-
Manually annotated by BRENDA team
hypoxia can stimulate enzyme mRNA and protein expression involving binding of hypoxia-induced factor 1 to a specific hypoxia responsive element in the enzyme's promoter
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-
Manually annotated by BRENDA team
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-
-
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 L-lysine 9 + alpha-ketoglutarate + O2
methyl-histone 3 L-lysine 9 + ?
show the reaction diagram
-
-
-
?
dimethyl-histone 3 lysine 9 + ?
methyl-histone 3 lysine 9 + ?
show the reaction diagram
dimethylated histone 3 lysine 9 + ?
methyl-histone 3 lysine 9 + ?
show the reaction diagram
-
proteins Swm1 and Swm2 associate together in a complex that specifically demethylates lysine 9 in histone H3 and both up- and down-regulates expression of different groups of genes. Protein Swm1 may act in concert with the histone deacetylase Clr6 and chromatin remodeller Hrp1 to repress gene expression
-
-
?
dimethylated histone 3-Lys4 peptide + H2O
?
show the reaction diagram
-
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
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
histone H3 N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6-methyl-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
-
-
-
-
?
protein 6-N,6-N-dimethyl-L-lysine + 2-oxoglutarate + O2
?
show the reaction diagram
-
demethylation of lysine 4
-
-
?
trimethyl-histone 3 L-lysine 9 + 2-oxoglutarate + O2
dimethyl-histone 3 L-lysine 9 + ?
show the reaction diagram
-
-
-
?
trimethyl-histone 3 L-lysine 9 + alpha-ketoglutarate + O2
dimethyl-histone 3 L-lysine 9 + ?
show the reaction diagram
trimethyl-histone 3 L-lysine 9 mutant A7H + alpha-ketoglutarate + O2
dimethyl-histone 3 L-lysine 9 mutant A7H + ?
show the reaction diagram
-
-
-
?
trimethyl-histone 3 L-lysine 9 mutant A7R + alpha-ketoglutarate + O2
dimethyl-histone 3 L-lysine 9 mutant A7R + ?
show the reaction diagram
-
-
-
?
trimethyl-histone 3 L-lysine 9 mutant G12P + alpha-ketoglutarate + O2
dimethyl-histone 3 lysine 9 mutant G12P + ?
show the reaction diagram
-
-
-
?
[Dnmt1]-methyl-L-lysine + 2-oxoglutarate + O2
[Dnmt1]-L-lysine + succinate + formaldehyde + CO2
show the reaction diagram
[Dnmt1]-methyl-L-lysine1096 + 2-oxoglutarate + O2
[Dnmt1]-L-lysine1096 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3 peptide 21mer P16A]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
[histone H3 peptide 21mer]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 peptide 21mer]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
[histone H3 peptide 21mer]-N6,N6-dimethyl-L-lysine4-dimethyl-L-lysine9 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
[histone H3 peptide 21mer]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 peptide 21mer]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
-
no activity with a monomethylated H3-Lys4 peptide with Arg2 mutated to Ala, Arg2 is central to substrate recognition also in LSD2
-
-
?
[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
show the reaction diagram
-
-
-
-
?
[histone H3 peptide 21mer]-N6-methyl-L-lysine4-methyl-L-arginine17 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
[histone H3 peptide 21mer]-N6-methyl-L-lysine4-methyl-L-lysine9 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
[histone H3 peptide 30mer]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 peptide 30mer]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
[histone H3 peptide]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 peptide]-L-lysine4 + succinate + H2O2
show the reaction diagram
-
the peptide substrate comprises the 21 N-terminal residues of histone H3, with a dimethylated lysyl residue at position 4. The reductive half-reaction is rate-limiting at physiological pH
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-L-lysine4 + 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
-
predicted site-specificity from phylogenetic analysis
-
-
?
[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
[histone H3]-N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-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
[p53]-methyl-L-lysine + 2-oxoglutarate + O2
[p53]-L-lysine + succinate + formaldehyde + CO2
show the reaction diagram
[protein p53]-N6,N6-dimethyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
show the reaction diagram
[protein p53]-N6-methyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
show the reaction diagram
additional information
?
-
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
dimethyl-histone 3 lysine 9 + ?
methyl-histone 3 lysine 9 + ?
show the reaction diagram
Q6PCM1
Jmjd1a demethylates dimethyl-histone 3 lysine 9 at the promoter regions of Tcl1, Tcfcp2l1, and Zfp57 and positively regulates the expression of these pluripotency-associated genes
-
-
?
dimethylated histone 3 lysine 9 + ?
methyl-histone 3 lysine 9 + ?
show the reaction diagram
-
proteins Swm1 and Swm2 associate together in a complex that specifically demethylates lysine 9 in histone H3 and both up- and down-regulates expression of different groups of genes. Protein Swm1 may act in concert with the histone deacetylase Clr6 and chromatin remodeller Hrp1 to repress gene expression
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
histone H3 N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6-methyl-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
-
-
-
-
?
[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-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-L-lysine4 + 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
-
predicted site-specificity from phylogenetic analysis
-
-
?
[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
[histone H3]-N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-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
[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
-
-
?
[protein p53]-N6,N6-dimethyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
show the reaction diagram
O60341
LSD1 demethylates mono- and dimethylated Lys370 in the regulatory domain of the tumor suppressor p53, precluding the binding of the transcriptional coactivator 53BP1
-
-
?
[protein p53]-N6-methyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
show the reaction diagram
O60341
LSD1 demethylates mono- and dimethylated Lys370 in the regulatory domain of the tumor suppressor p53, precluding the binding of the transcriptional coactivator 53BP1
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-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
structure of Zn2+ binding sites of the isozymes, overview; structure of Zn2+ binding sites of the isozymes, overview; structure of Zn2+ binding sites of the isozymes, overview; structure of Zn2+ binding sites of the isozymes, overview; structure of Zn2+ binding sites of the isozymes, overview
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
-
-
(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
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3,8,13,18,23-pentaazapentacosan-1-ol
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biguanide
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inhibits LSD1 and is capable of reactivating genes that are pathologically silenced in the development of colon cancer
bisguanidine
bisguanidine polyamine analogues
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inhibit LSD1 and are capable of reactivating genes that are pathologically silenced in the development of colon cancer
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glycerol
inhibits at 10%, activates at above 30%
H3 21mer peptide
-
the peptide is covalently attached to LSD1-flavin by suicide inactivation
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HCF-1
-
is a component of the Set1 and MLL1 histone H3 Lys4 methyltransferase complexes, it thus coordinates modulation of repressive H3 Lys9 methylation levels with addition of activating H3 Lys4 trimethylation marks
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KCl
50 mM, 50% inhibition
MgCl2
75% inhibition at 50 mM
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-ethyl-N'-[[2-([[4-([[2-([[4-(ethylamino)butyl]amino]methyl)cyclopropyl]methyl]amino)butyl]amino]methyl)cyclopropyl]methyl]butane-1,4-diamine
-
-
Pargyline
-
i.e. N-methyl-N-propargylbenzylamine, the LSD1 inhibitor prevents demethylation of Dnmt1-C by LSD1
Peptide inhibitor
a suicide inhibitor consisting of a 21 residue histone H3 peptide in which K4 is modified by an Nmethylpropargyl group. 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 LSD1, binding structure, overview
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Tranylcypromine
yMYC
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LID appears to interact with the cell growth regulator dMYC, which binds the jumonji domain of LID to inhibit its demethylase activity
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[histone H3 peptide 21mer]-L-arginine4
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competitive inhibition of LSD2
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[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
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[histone H3 peptide 21mer]-N6,N6,N6-trimethyl-L-lysine4
-
-
-
[histone H3 peptide]-N6-methyl-L-lysine9
-
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
CoREST
-
the co-repressor CoREST stabilizes LSD1 and increases in vitro LSD1 activity by approximately twofold and is essential for LSD1-mediated demethylation in intact nucleosomes in vivo and for the in vitro demethylation of nucleosomal particles, binding structure, overview
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glycerol
inhibits at 10%, activates at above 30%
tetrahydrofolate
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23 - 0.41
dimethyl-histone 3 L-lysine 9
-
0.023 - 0.048
histone H3 N6,N6,N6-trimethyl-L-lysine9
-
0.025 - 0.074
histone H3 N6,N6-dimethyl-L-lysine9
-
0.195
O2
-
pH 7.5, 25C, recombinant enzyme
0.063 - 0.071
trimethyl-histone 3 L-lysine 9
-
0.11
trimethyl-histone 3 L-lysine 9 mutant A7H
-
pH 7.3, 37C
-
0.18
trimethyl-histone 3 L-lysine 9 mutant A7R
-
pH 7.3, 37C
-
0.93
trimethyl-histone 3 L-lysine 9 mutant G12P
-
pH 7.3, 37C
-
0.0125
[histone H3 peptide 21mer P16A]-N6-methyl-L-lysine4
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.0066
[histone H3 peptide 21mer]-N6,N6-dimethyl-L-lysine4-dimethyl-L-lysine9
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.0113 - 0.092
[histone H3 peptide 21mer]-N6-methyl-L-lysine4
-
0.0705
[histone H3 peptide 21mer]-N6-methyl-L-lysine4-acetyl-L-lysine9
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.0081
[histone H3 peptide 21mer]-N6-methyl-L-lysine4-methyl-L-arginine17
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.009
[histone H3 peptide 21mer]-N6-methyl-L-lysine4-methyl-L-lysine9
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.0051
[histone H3 peptide 30mer]-N6-methyl-L-lysine4
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.0026
[histone H3 peptide]-N6,N6-dimethyl-L-lysine4
-
pH 7.5, 25C, recombinant enzyme
-
0.0107
[histone H3]-N6,N6-dimethyl-L-lysine4
pH 8.0, 22C, recombinant LSD1
-
0.0089
[histone H3]-N6-methyl-L-lysine4
pH 8.0, 22C, recombinant LSD1
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00008 - 0.005
dimethyl-histone 3 L-lysine 9
-
0.01 - 0.076
histone H3 N6,N6,N6-trimethyl-L-lysine9
-
0.0029 - 0.065
histone H3 N6,N6-dimethyl-L-lysine9
-
0.00025 - 0.0005
trimethyl-histone 3 L-lysine 9
-
0.00018
trimethyl-histone 3 L-lysine 9 mutant A7H, trimethyl-histone 3 L-lysine 9 mutant A7R
Homo sapiens
-
pH 7.3, 37C
-
0.00012
trimethyl-histone 3 L-lysine 9 mutant G12P
Homo sapiens
-
pH 7.3, 37C
-
0.0043
[histone H3 peptide 21mer P16A]-N6-methyl-L-lysine4
Mus musculus
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.0222
[histone H3 peptide 21mer]-N6,N6-dimethyl-L-lysine4-dimethyl-L-lysine9
Mus musculus
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.0046 - 0.033
[histone H3 peptide 21mer]-N6-methyl-L-lysine4
-
0.0058
[histone H3 peptide 21mer]-N6-methyl-L-lysine4-acetyl-L-lysine9
Mus musculus
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.005
[histone H3 peptide 21mer]-N6-methyl-L-lysine4-methyl-L-arginine17
Mus musculus
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.004
[histone H3 peptide 21mer]-N6-methyl-L-lysine4-methyl-L-lysine9
Mus musculus
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.0068
[histone H3 peptide 30mer]-N6-methyl-L-lysine4
Mus musculus
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.199
[histone H3 peptide]-N6,N6-dimethyl-L-lysine4
Homo sapiens
-
pH 7.5, 25C, recombinant enzyme
-
0.011
[histone H3]-N6,N6-dimethyl-L-lysine4
Arabidopsis thaliana
Q8VXV7
pH 8.0, 22C, recombinant LSD1
-
0.008
[histone H3]-N6-methyl-L-lysine4
Arabidopsis thaliana
Q8VXV7
pH 8.0, 22C, recombinant LSD1
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22 - 330
histone H3 N6,N6,N6-trimethyl-L-lysine9
7053
4 - 260
histone H3 N6,N6-dimethyl-L-lysine9
6384
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.046
[histone H3 peptide 21mer]-L-arginine4
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.002
[histone H3 peptide 21mer]-L-glutamine4
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.033
[histone H3 peptide 21mer]-L-lysine4
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.00015
[histone H3 peptide 21mer]-L-methionine4
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.058
[histone H3 peptide 21mer]-N6,N6,N6-trimethyl-L-lysine4
-
pH 8.0, 25C, recombinant wild-type LSD2
-
0.0066
[histone H3 peptide 21mer]-N6-methyl-L-lysine9
-
pH 8.0, 25C, recombinant wild-type LSD2
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 7.5
-
assay at
7.5
-
assay at
8.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
kcat/KM-pH profiles for LSD1 with protiated and deuterated H3 K4 21-mer dimethylated peptide, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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of control and hyperglycemic mice
Manually annotated by BRENDA team
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levels of KDM4B histone demethylase are elevated in different types of cancer cells
Manually annotated by BRENDA team
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JHMD1A and JARID1B
Manually annotated by BRENDA team
high expression level
Manually annotated by BRENDA team
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JMJD1A is expressed in human cancers such as glioblastoma and breast cancer in vivo, and expression is associated with the hypoxic marker CA9
Manually annotated by BRENDA team
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whisker follicle, JARID1B
Manually annotated by BRENDA team
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BALB c nu/nu athymic nude mice are implanted with the human colorectal cancer HCT-116 cells
Manually annotated by BRENDA team
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up-regulation of mRNA and protein after exposure to hypoxia or iron scavengers in vitro. Blocking of hypoxia-inducible factor 1 signaling abrogates the up-regulation
Manually annotated by BRENDA team
rosette and cauline leaves
Manually annotated by BRENDA team
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JARID1B
Manually annotated by BRENDA team
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JARID1C
Manually annotated by BRENDA team
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elevated activity of JMJD2B expression
Manually annotated by BRENDA team
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H3-K4 mono-, di-, and tri-methylation in large luteal cells increases as differentiation evolves but remains low in small luteal cells
Manually annotated by BRENDA team
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JARID1B
Manually annotated by BRENDA team
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short isoform of JMJD2A is upregulated during muscle differentiation, expression analysis and pattern, overview
Manually annotated by BRENDA team
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LSD1 expression correlates with adverse outcome and is inversely correlated with differentiation in neuroblastic tumors; LSD1 is strongly expressed in poorly differentiated neuroblastomas, real-time reverse transcription-PCR expression analysis
Manually annotated by BRENDA team
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embryonal carcinoma cell
Manually annotated by BRENDA team
protein level is the highest in round spermatids, compared with spermatocyte and elogating spermatids
Manually annotated by BRENDA team
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LSD1 and JARID1D
Manually annotated by BRENDA team
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JHMD1A and JARID1A
Manually annotated by BRENDA team
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JARID1B
Manually annotated by BRENDA team
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elevated levels of JMJD2B expression
Manually annotated by BRENDA team
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JHMD1A and JHMD1B
Manually annotated by BRENDA team
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developing, JHDM1B
Manually annotated by BRENDA team
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retinoblastoma cells
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
JMJD1A is localized in both cytoplasm and nucleus
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
about, recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 95059, LSD1 without N-terminal methionine, mass spectrometry
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
flavoprotein
additional information
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the histone 3 lysine 9 demethylase activity requires an unidentified post-translational modification to allow it to act
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of Caenorhabditis elegans KIAA1718 with H3K9me2, H3K27me2 and H3K4me3 peptides in the presence of Fe2+
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crystal structures of LSD1/Co-REST complexes bound to histone H3 peptides. LSD1/Co-REST-C complex co-crystallized with a 20-residue histone H3 peptide inhibitor in which Lys4 is mutated to a methionine. Cocrystallization of the enzyme with a suicide inhibitor consisting of a 21-residue histone H3 peptide in which K4 is modified by an N-methylpropargylgroup. Complex structure analysis, overview
enzyme complex LSD1-CoREST crystal structure in complex with a histone H3 peptide, overview
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in complex with trimethyl-histone 3 L-lysine 9, dimethyl-histone 3 L-lysine 36, and trimethyl-histone 3 L-lysine 36, and N-oxalylglycine, alpha-ketoglutarate, and succinate, respectively. Histone substrates are recognized through a network of backbone hydrogen bonds and hydrophobic interactions that deposit the trimethyllysine into the active site. The trimethylated epsilon-ammonium cation is coordinated within a methylammonium-binding pocket through carbonoxygen hydrogen bonds that position one of the methyl groups adjacent to the Fe(II) center for hydroxylation and demethylation
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JMJD2A-tudor in complex with H4K20me3, X-ray diffraction structure determination and analysis at 2.8 A resolution
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LSD1 with bound inhibitor histone H3 21mer peptide, protein to peptide ratio of 1:5, with or without inhibitor tranylcypromine, from 20 mM MES-Na buffer, pH 6.0, containing 1 mM DTT, with 100 mM HEPES-Na buffer, pH 7.5, containing 5% 2-methyl-2,4-pentanediol and 3.5-4.0% w/v PEG monomethyl ether 2000, with or without 5 mM tranylcypromine, the cryoprotectant contains 25% w/v 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 2.25-2.7 A resolution
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purified recombinant KDM4C, sitting drop vapor diffusion method, mixing of 7 mg/ml protein with 2 mM N-oxalylglycine with well solution, containing 25% v/v PEG 3350, 0.2 M sodium nitrate, 0.1 M Bis tris propane, pH 6.5, 5% v/v ethylene glycol, 0.01 M NiCl2, in a 2:1 ratio, 4C, X-ray diffraction structure determination and analysis at 2.55 A resolution
recombinant enzyme, hanging-drop vapor diffusion method, 2.8 A-resolution crystal structure
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structures of JMJD2A-Ni(II)-Zn(II) inhibitor complexes bound to tri-, di- and monomethyl forms of histone 3 lysine 9 and the trimethyl form of histone 3 lysine 36. The structures reveal a lysyl-binding pocket in which substrates are bound in distinct bent conformations involving the Zn-binding site. The mechansim for achieving methylation state selectivity involves the orientation of the substrate methyl groups towards a ferryl intermediate
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
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purified recombinant enzyme, 60 min, inactivation
696340
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the molecular chaperon Hsp90 interacts with and stabilizes KDM4B protein
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
LSD1 in the histone demethylase complex also containing CoREST, HDAC1, and HDAC2
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recombinant
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recombinant Flag-tagged wild-type KDM1B and mutant KDM1B from HEK 293T cells to near homogeneity
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recombinant GST-tagged LSD1 from Escherichia coli by glutathione affinity chromatography, cleavageof the tag, and cation exchange chromatography
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recombinant His-tagged LSD1 from Escherichia coli by nickel and heparin affinity chromatography
recombinant His-tagged truncated LSD1 mutant from Escherichia coli strain Rosetta 2 by nickel affinity chromatography, gel filtration, and anion exchange chromatography
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recombinant His6-tagged wild-type LSD2 and truncated mutants from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, followed by ultra- and gel filtration
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recombinant N-terminally His-tagged enzyme by nickel affinity chromatography from Escherichia coli BL21(DE3), or by ammonium sulfate fractionation and anionexchange chrmatography, recombinant N-terminally truncated GST-tagged LSD1 by glutathione affinity chromatography
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recombinant N-terminally His-tagged KDM4A from Escherichia coli by nickel affinity chromatography; recombinant N-terminally His-tagged KDM4B from Escherichia coli by nickel affinity chromatography; recombinant N-terminally His-tagged KDM4C from Escherichia coli by nickel affinity chromatography; recombinant N-terminally His-tagged KDM4D from Escherichia coli by nickel affinity chromatography; recombinant N-terminally His-tagged KDM4E from Escherichia coli by nickel affinity chromatography
two LSD1 truncated forms, lacking the first 157 and 184 amino acids, respectively
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Cloned/COMMENTARY
ORGANISM