Information on EC 1.14.11.B1 - [histone-H3]-lysine-9-demethylase and Organism(s) Homo sapiens and UniProt Accession Q6B0I6

for references in articles please use BRENDA:EC1.14.11.B1
Word Map on EC 1.14.11.B1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: Q6B0I6
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)


The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected 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
the catalytic mechanism, shared by all the JumonjiC-domain-containing demethylases, requires the presence of iron(II) in the active site, the co-substrate 2-oxoglutarate, and molecular oxygen. The methyl groups attached to the epsilon-amino group of lysines are oxidized to a hemiaminal, which spontaneously decomposes, releasing formaldehyde and demethylated lysine
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
-
dysregulated expression of KDM4A-D family promotes chromosomal instabilities
physiological function
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
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
-
-
-
?
ATKAARK(me3)-SAPATGGVKKPHRYRPG-GK(biotin) + 2-oxoglutarate + O2
ATKAARKSAPATGGVKKPHRYRPG-GK(biotin) + succinate + formaldehyde + CO2
show the reaction diagram
-
usage of immunodetection for assay quantification
-
-
?
dimethyl-histone 3 L-lysine 9 + alpha-ketoglutarate + O2
methyl-histone 3 L-lysine 9 + ?
show the reaction diagram
-
-
-
?
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
-
-
?
H3(1-20) K4-dimethylated peptide + 2-oxoglutarate + O2
H3(1-20) K4-monomethylated peptide + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
H31-15K9me3 + 2-oxoglutarate + O2
H31-15K9me2 + succinate + formaldehyde + CO2
show the reaction diagram
-
a 15mer histone peptide substrate H31-15K9me3
-
-
?
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
histone H4 N6-methyl-L-lysine20 + 2-oxoglutarate + O2
histone H4 L-lysine20 + 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
-
-
?
protein N6,N6-dimethyl-L-lysine + 2 2-oxoglutarate + 2 O2
protein L-lysine + 2 succinate + 2 formaldehyde + 2 CO2
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
-
-
-
?
[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-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-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 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
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
B2RXH2, O75164, O94953, Q6B0I6, Q9H3R0
-
-
-
?
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
histone H4 N6-methyl-L-lysine20 + 2-oxoglutarate + O2
histone H4 L-lysine20 + succinate + formaldehyde + CO2
show the reaction diagram
protein N6,N6-dimethyl-L-lysine + 2 2-oxoglutarate + 2 O2
protein L-lysine + 2 succinate + 2 formaldehyde + 2 CO2
show the reaction diagram
-
-
-
-
?
[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-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-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 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
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
required for activity
Zn2+
structure of Zn2+ binding sites of the isozymes, overview
Zn2+
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
-
-
(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
-
-
(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
-
-
(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
-
-
(R)-2-(1-(1-benzoylpiperidin-3-yl)-1H-1,2,3-triazol-4-yl)isonicotinic acid
-
-
1-(3-(ethylsulfonyl)phenyl)-2-(4-(pyridin-2-yl)thiazol-2-yl)ethan-1-one
-
-
1-(3-(methylsulfonyl)phenyl)-2-(4-(pyridin-2-yl)thiazol-2-yl)ethan-1-one
-
-
1-(4-(methylsulfonyl)phenyl)-2-(4-(pyridin-2-yl)thiazol-2-yl)ethan-1-one
-
-
1-phenyl-2-(4-(pyridin-2-yl)thiazol-2-yl)ethan-1-one
-
-
2-(1-hydroxyvinyl)isonicotinic acid
-
-
2-(2-((chroman-6-ylmethyl)amino)pyrimidin-4-yl)isonicotinic acid
-
-
2-(2-aminothiazol-4-yl)isonicotinamide
2-(2-aminothiazol-4-yl)isonicotinic acid
2-(2-benzamidothiazol-4-yl)isonicotinic acid
-
-
2-(2-methylthiazol-4-yl)isonicotinic acid
-
-
2-(thiazol-4-yl)isonicotinic acid
-
-
3,8,13,18,23-pentaazapentacosan-1-ol
-
-
3-((2-(pyridin-2-yl)-6-(1,2,4,5-tetrahydro-3H-benzo[d]azepin-3-yl)pyrimidin-4-yl)amino)propanoic acid
-
-
3-(2-((2-aminoethyl)carbamoyl)pyridin-4-yl)benzoic acid
-
-
3-(9-(dimethylamino)-N-hydroxynonanamido)propanoic acid
-
-
3-[hydroxy-[5-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-5-oxo-pentanoyl]amino]propanoic acid
-
-
3-[hydroxy-[5-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-5-oxo-pentanoyl]amino]propanoic acid
-
-
3-[hydroxy-[7-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-7-oxo-heptanoyl]amino]propanoic acid
-
-
3-[hydroxy-[8-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
-
-
3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
-
-
3-[hydroxy-[8-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
-
-
4-((methyl((1-(4-oxo-3,4-dihydropyrido[3,4-d]pyrimidin-8-yl)-1H-pyrazol-4-yl)methyl)amino)methyl)benzonitrile
-
-
4-((methyl(2-(1-(4-oxo-3,4-dihydropyrido[3,4-d]pyrimidin-8-yl)-1H-pyrazol-4-yl)ethyl)amino)methyl)benzonitrile
-
-
4-(1-(2-(1-(4-oxo-3,4-dihydropyrido[3,4-d]pyrimidin-8-yl)-1H-pyrazol-4-yl)ethyl)piperidin-4-yl)benzonitrile
-
-
4-(pyridin-2-yl)thiazol-2-amine
-
low inhibition activity
4-(pyridin-3-yl)thiazol-2-amine
-
low inhibition activity
5-tetrazolyl acetohydrazide
-
-
8-(((furan-2-ylmethyl)amino)methyl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-((4-(pyridin-2-yl)piperazin-1-yl)methyl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-((4-methylpiperazin-1-yl)methyl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-((4-phenylpiperazin-1-yl)methyl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-((benzylamino)methyl)pyrido[3,4-d]pyrimidin-4(3H)-one
8-((dimethylamino)methyl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(1-methyl-1H-pyrazol-3-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(1H-pyrazol-3-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(2-aminothiazol-4-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
8-(4-(((3,4-dichlorobenzyl)(methyl)amino)methyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-((dimethylamino)methyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-((methyl(4-(methylsulfonyl)benzyl)amino)methyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-((4-fluorobenzyl) (methyl)amino)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
8-(4-(2-(4-((5-cyclopropyl-1,2,4-oxadiazol-3-yl)methyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-(2,4-difluorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-(2-chlorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-(3,4-dichlorobenzyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-(3,5-dichlorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
8-(4-(2-(4-(3,5-difluorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-(3-(trifluoromethyl)phenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-(3-chlorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
8-(4-(2-(4-(3-methoxybenzyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-(4-(methylsulfonyl)phenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-(4-(trifluoromethyl)benzyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-(4-chlorobenzyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
8-(4-(2-(4-(4-chlorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
8-(4-(2-(4-(4-fluorobenzyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-(4-fluorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-(4-methoxyphenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-(benzo[d][1,3]dioxol-5-ylmethyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-(pyridin-3-ylmethyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-(pyridin-4-yl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-(thiophen-2-yl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-benzylpiperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(2-(4-phenylpiperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(hydroxymethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(piperidin-1-ylmethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(4-(pyrrolidin-1-ylmethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(hydroxyamino)-N-[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]-8-oxo-octanamide
-
-
8-(piperidin-1-ylmethyl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
8-(thiazol-4-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
8-chloropyrido[3,4-d]pyrimidin-4(3H)-one
-
-
biguanide
-
inhibits LSD1 and is capable of reactivating genes that are pathologically silenced in the development of colon cancer
bisguanidine
-
inhibits LSD1/KDM1
bisguanidine polyamine analogues
-
inhibit LSD1 and are capable of reactivating genes that are pathologically silenced in the development of colon cancer
-
caffeic acid
-
the KDM4C inhibitor caffeic acid preferentially abolishes human tumor-initiating cells in ALDHbri+-derived xenograft mouse model in vivo. KDM4C inhibition decreases the percentage, clonogenicity and self-renewal of esophageal squamous cell carcinoma ALDHbri+ tumor-initiating cells in vitro
Cd2+
-
at 0.001-0.005 mM, cadmium increases global histone H3 methylation, H3K4me3 and H3K9me2, by inhibiting the activities of histone demethylases, and aberrant histone methylation that occurs early (48 h) and at 4 weeks is associated with cadmium-induced transformation of BEAS-2B cells at the early stage
DMOG
a small molecule JMJD1A inhibitor. N-oxalglycine dimethyl ester prodrug, DMOG, exerts histone lysine methylating activity in cells
H3 21mer peptide
-
the peptide is covalently attached to LSD1-flavin by suicide inactivation
-
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
-
histone H3
-
full-length histone H3, H3_1-135, which lacks any posttranslational modifications, is a tight-binding, competitive inhibitor of KDM1A demethylation activity. Full-length H3 rapidly reaches equilibrium with KDM1A and shows 100fold increased binding affinity compared to a 21-mer H3-derived 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-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
lithium 2-(((furan-2-ylmethyl)amino)methyl)isonicotinate
-
-
lithium 2-((benzylamino)methyl)isonicotinate
methyl (2S)-2-[[4-[3-(hydroxyamino)-3-oxo-propyl]benzoyl]amino]-3-(4-phenylphenyl)propanoate
-
-
methyl (2S)-2-[[7-(hydroxyamino)-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate
-
-
methyl (2S)-2-[[7-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate
-
-
methyl (2S)-2-[[8-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate
-
-
methyl (S)-3-(2'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
-
methyl (S)-3-(3'-cyano-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
-
-
methyl (S)-3-(3'-fluoro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
-
methyl (S)-3-(4'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
-
methyl (S)-3-(4'-cyano-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
-
methyl (S)-3-(4'-fluoro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
-
methyl (S)-3-(6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
-
-
methyl (S)-3-([1,1'-biphenyl]-4-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
-
methyl 3-(3'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
-
methyl 3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoate
-
-
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-oxalylglycine
NOG, selectively inhibits JMJD1A
N-[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]heptanamide
-
-
N1-((3'-chloro-6-methoxy-[1,1'-biphenyl]-3-yl)methyl)-N8-hydroxyoctanediamide
-
-
N1-(2-(3'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)ethyl)-N8-hydroxyoctanediamide
-
-
N1-(2-(3'-chloro-6-methoxy-[1,1'-biphenyl]-3-yl)ethyl)-N8-hydroxyoctanediamide
-
-
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
-
-
Pargyline
-
-
peptide H31-21
-
21-mer H3-derived peptide
-
peptide H3K4M
-
the modified H3 peptide with substitution of Lys4 to Met [H3K4M] is known to be a potent competitive inhibitor of 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
-
pyrido[3,4-d]pyrimidin-4(3H)-one
-
-
SW55
-
a hydroxamate-based histone deacetylase (HDAC) inhibitor, slight inhibition
-
tert-butyl (2S)-2-[[8-(hydroxyamino)-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate
-
-
tert-butyl (2S)-2-[[8-(hydroxyamino)-8-oxo-octanoyl]amino]-3-phenyl-propanoate
-
-
Tranylcypromine
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
-
required for activity
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
-
tetrahydrofolate
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037
histone H3 N6,N6,N6-trimethyl-L-lysine9
KDM4D, pH and temperature not specified in the publication
-
0.074
histone H3 N6,N6-dimethyl-L-lysine9
KDM4D, pH and temperature not specified in the publication
-
0.0247
2-oxoglutarate
-
pH and temperature not specified in the publication
0.23 - 0.41
dimethyl-histone 3 L-lysine 9
-
0.0232
H31-15K9me3
-
pH and temperature not specified in the publication
-
0.023 - 0.048
histone H3 N6,N6,N6-trimethyl-L-lysine9
-
0.025 - 0.073
histone H3 N6,N6-dimethyl-L-lysine9
-
0.173 - 0.195
O2
0.063 - 0.071
trimethyl-histone 3 L-lysine 9
-
0.11
trimethyl-histone 3 L-lysine 9 mutant A7H
-
pH 7.3, 37°C
-
0.18
trimethyl-histone 3 L-lysine 9 mutant A7R
-
pH 7.3, 37°C
-
0.93
trimethyl-histone 3 L-lysine 9 mutant G12P
-
pH 7.3, 37°C
-
0.0026
[histone H3 peptide]-N6,N6-dimethyl-L-lysine4
-
pH 7.5, 25°C, recombinant enzyme
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
histone H3 N6,N6,N6-trimethyl-L-lysine9
KDM4D, pH and temperature not specified in the publication
-
0.012
histone H3 N6,N6-dimethyl-L-lysine9
KDM4D, pH and temperature not specified in the publication
-
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
-
pH 7.3, 37°C
-
0.00012
trimethyl-histone 3 L-lysine 9 mutant G12P
-
pH 7.3, 37°C
-
0.199
[histone H3 peptide]-N6,N6-dimethyl-L-lysine4
-
pH 7.5, 25°C, recombinant enzyme
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
41
histone H3 N6,N6,N6-trimethyl-L-lysine9
KDM4D, pH and temperature not specified in the publication
-
16
histone H3 N6,N6-dimethyl-L-lysine9
KDM4D, pH and temperature not specified in the publication
-
22 - 330
histone H3 N6,N6,N6-trimethyl-L-lysine9
-
4 - 260
histone H3 N6,N6-dimethyl-L-lysine9
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
(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
-
pH 7.5, 25°C
0.17
(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
-
pH 7.5, 25°C
0.00189
histone H3
-
pH 7.5, 25°C
-
0.000098
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
-
pH 7.5, 25°C
0.5
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
-
pH 7.5, 25°C
0.0063
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
-
pH 7.5, 25°C
-
0.00003
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
-
pH 7.5, 25°C
0.5
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
-
pH 7.5, 25°C
0.5
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
-
pH 7.5, 25°C
0.0014
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
-
pH 7.5, 25°C
0.0098
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
-
pH 7.5, 25°C
0.00038
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
-
pH 7.5, 25°C
0.00006
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
-
pH 7.5, 25°C
0.00029
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
-
pH 7.5, 25°C
0.0018
peptide H31-21
-
pH 7.5, 25°C
-
additional information
additional information
-
kinetic analysis of full-length histone products against KDM1A
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037
2-(2-((chroman-6-ylmethyl)amino)pyrimidin-4-yl)isonicotinic acid
Homo sapiens;
-
pH 7.5, 37°C
0.003
3-(9-(dimethylamino)-N-hydroxynonanamido)propanoic acid
Homo sapiens;
-
pH 7.5, 37°C
0.2
3-[hydroxy-[5-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-5-oxo-pentanoyl]amino]propanoic acid
Homo sapiens;
-
above, pH 7.5, 37°C
0.0703
3-[hydroxy-[5-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-5-oxo-pentanoyl]amino]propanoic acid
Homo sapiens;
-
pH 7.5, 37°C
0.0606
3-[hydroxy-[7-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-7-oxo-heptanoyl]amino]propanoic acid
Homo sapiens;
-
pH 7.5, 37°C
0.0068
3-[hydroxy-[8-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
Homo sapiens;
-
pH 7.5, 37°C
0.0136
3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
Homo sapiens;
-
pH 7.5, 37°C
0.0371
3-[hydroxy-[8-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
Homo sapiens;
-
pH 7.5, 37°C
0.0466
5-tetrazolyl acetohydrazide
Homo sapiens;
-
pH 7.5, 37°C
0.0085
8-(hydroxyamino)-N-[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]-8-oxo-octanamide
Homo sapiens;
-
pH 7.5, 37°C
0.0258
methyl (2S)-2-[[4-[3-(hydroxyamino)-3-oxo-propyl]benzoyl]amino]-3-(4-phenylphenyl)propanoate
Homo sapiens;
-
pH 7.5, 37°C
0.0706
methyl (2S)-2-[[7-(hydroxyamino)-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate
Homo sapiens;
-
pH 7.5, 37°C
0.056
methyl (2S)-2-[[7-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate
Homo sapiens;
-
pH 7.5, 37°C
0.0171
methyl (2S)-2-[[8-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate
Homo sapiens;
-
pH 7.5, 37°C
0.0563
methyl (S)-3-(2'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens;
-
pH 7.5, 37°C
0.0476
methyl (S)-3-(3'-cyano-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens;
-
pH 7.5, 37°C
-
0.029
methyl (S)-3-(3'-fluoro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens;
-
pH 7.5, 37°C
0.0483
methyl (S)-3-(4'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens;
-
pH 7.5, 37°C
0.0548
methyl (S)-3-(4'-cyano-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens;
-
pH 7.5, 37°C
0.0522
methyl (S)-3-(4'-fluoro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens;
-
pH 7.5, 37°C
0.0939
methyl (S)-3-(6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens;
-
pH 7.5, 37°C
-
0.0254
methyl (S)-3-([1,1'-biphenyl]-4-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens;
-
pH 7.5, 37°C
0.0276
methyl 3-(3'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens;
-
pH 7.5, 37°C
0.0068
methyl 3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoate
Homo sapiens;
-
pH 7.5, 37°C
0.067
N-oxalylglycine
Homo sapiens;
D6W5M4
pH and temperature not specified in the publication
0.2
N-[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]heptanamide
Homo sapiens;
-
above, pH 7.5, 37°C
0.0145
N1-((3'-chloro-6-methoxy-[1,1'-biphenyl]-3-yl)methyl)-N8-hydroxyoctanediamide
Homo sapiens;
-
above, pH 7.5, 37°C
0.0188
N1-(2-(3'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)ethyl)-N8-hydroxyoctanediamide
Homo sapiens;
-
above, pH 7.5, 37°C
0.0166
N1-(2-(3'-chloro-6-methoxy-[1,1'-biphenyl]-3-yl)ethyl)-N8-hydroxyoctanediamide
Homo sapiens;
-
above, pH 7.5, 37°C
0.00484
peptide H31-21
Homo sapiens;
-
pH 7.5, 25°C
-
0.0143
tert-butyl (2S)-2-[[8-(hydroxyamino)-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate
Homo sapiens;
-
pH 7.5, 37°C
0.201
tert-butyl (2S)-2-[[8-(hydroxyamino)-8-oxo-octanoyl]amino]-3-phenyl-propanoate
Homo sapiens;
-
pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
-
demethylase assay at
7.6
-
RNA binding assay at
7.2 - 7.5
-
assay at
8
-
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
22
-
RNA binding assay at room temperature
37
-
demethylase assay at
22
-
assay at room temperature
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
levels of KDM4B histone demethylase are elevated in different types of cancer cells
Manually annotated by BRENDA team
-
osteoarthritic chondrocytes
Manually annotated by BRENDA team
-
expression pattern in early mammalian development: the maternally stored transcript is no longer detectable by the maternal-to-embryo transition, when the embryo becomes transcriptionally competent. LSD1/KDM1 expression then recovers to oocyte levels by the blastula stage
Manually annotated by BRENDA team
-
JMJD2C/KDM4C is preferentially expressed in undifferentiated embryonic stem cells, as compared with blastocysts and both hepatocyte and neural progenitor cells
Manually annotated by BRENDA team
enzyme JMJD1C is upregulated in patient esophageal cancer tissues and different esophageal cancer cell lines
Manually annotated by BRENDA team
-
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
-
BALB c nu/nu athymic nude mice are implanted with the human colorectal cancer HCT-116 cells
Manually annotated by BRENDA team
-
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
-
short isoform of JMJD2A is upregulated during muscle differentiation, expression analysis and pattern, overview
Manually annotated by BRENDA team
-
expression pattern in early mammalian development: the maternally stored transcript is no longer detectable by the maternal-to-embryo transition, when the embryo becomes transcriptionally competent. LSD1/KDM1 expression then recovers to oocyte levels by the blastula stage
Manually annotated by BRENDA team
high expression level
Manually annotated by BRENDA team
-
elevated levels of JMJD2B expression
Manually annotated by BRENDA team
-
retinoblastoma cells
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
KDM4D is recruited to chromatin and recognizes its histone substrates
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
UNIPROT
ORGANISM
-
-
-
-
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95059
-
1 * 95059, LSD1 without N-terminal methionine, mass spectrometry
100000
-
about, recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 95059, LSD1 without N-terminal methionine, mass spectrometry
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
flavoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
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
-
JMJD2A-tudor in complex with H4K20me3, X-ray diffraction structure determination and analysis at 2.8 A resolution
-
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
-
purified recombinant detagged enzyme in apo form and in complex with several inhibitors, hanging drop vapor diffusion method, mixing of 0.0015 ml of 7 mg/ml protein solution with 0.0015 ml of reservoir solution containing 2-16% w/v PEG 4000 and 0.1 M BTP, pH 7.5, and equilibration against 0.8 ml, 18°C, 1 week, the crystals are then soaked by addition of 750 nL of ligand solution at 10-200 mM in DMSO directly to the crystallizatin drops, followed by 4-48 h incubation at 18°C, X-ray diffraction structure determination and analysis
-
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, 4°C, X-ray diffraction structure determination and analysis at 2.55 A resolution
purified recombinant truncated enzyme LSD1 comprising residues 172-833 in complex with recombinant human CoREST residues 308-440, and peptide inhibitors 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, 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, and 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, by hanging drop vapor diffusion method, mixing of 0.001 ml of 9 mg/m protein solution with 0.001 ml of reservoir solution containing 100 mM N-(carbamoylmethyl)iminodiacetic acid, pH 5.5, and 1.18-1.28M potassium sodium tartrate tetrahydrate, 20°C, crystals are soaked in a solution containing 100 mM N-(carbamoylmethyl) iminodiacetic acid buffer, pH 5.5, with 1.14 M potassium sodium tartrate tetrahydrate, 10% glycerol, and 2 mM LSD1 inhibitor peptide 9, 11 or 13 for 2 h, X-ray diffraction structure determination and analysis at 2.53-2.69 A resolution
-
recombinant enzyme, hanging-drop vapor diffusion method, 2.8 A-resolution crystal structure
-
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
-
purified recombinant enzyme, 60 min, inactivation
696340
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the molecular chaperon Hsp90 interacts with and stabilizes KDM4B protein
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant benzonae-treated His6-tagged full-length enzyme by nickel affinity chromatography from Escherichia coli strain BL21(DE3)
-
recombinant N-terminally His-tagged KDM4D from Escherichia coli by nickel affinity chromatography
recombinant
-
recombinant GST-tagged LSD1 from Escherichia coli by glutathione affinity chromatography, cleavageof the tag, and cation exchange chromatography
-
recombinant His-tagged KDM4A residues 1-359 from Escherichia coli strain BL21 Codon-Plus-Ril by metal chelating affinity chromatography to over 90% purity
-
recombinant His-tagged truncated LSD1 mutant from Escherichia coli strain Rosetta 2 by nickel affinity chromatography, gel filtration, and anion exchange chromatography
-
recombinant N-terminally GST-tagged enzyme from Spodoptera frugiperda Sf9 cells by glutathione affinity chromatography and gel filtration, recombinant N-terminally His-tagged KDM4A 1-359 from Escherichia coli by nickel affinity chromatography, followed by tag removal with TEV protease, another step of nickel affinity chromatography using the eluate, and gel filtration
-
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
-
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 KDM4E from Escherichia coli by nickel affinity chromatography
recombinant N-terminally His6-tagged truncated KDM4A1-359 from Escherichia coli BL21(DE3) by nickel affinity chromatography and gel filtration
-
two LSD1 truncated forms, lacking the first 157 and 184 amino acids, respectively
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of N-terminally His-tagged KDM4D in Escherichia coli
gene KDM4D, functional recombinant expression of His6-tagged full-length enzyme in Escherichia coli strain BL21(DE3). To establish the U2OS-TetON stable cell line that conditionally expresses myc-KDM4D or EGFP-KDM4D-1H4R-HRK-FL, fragments including the myc-KDM4D or EGFP-KDM4D-1H4R-HRK-FL are subcloned into pTRE2-puro plasmid. The resulting pTRE2-puro-myc-KDM4D and pTRE2-puro-EGFP-KDM4D-1H4R-HRK-FL vectors are transfected into U2OS-Tet-ON cells
-
expression in Escherichia coli, His-tagged
-
expression of functional doxycycline-inducible EGFP-KDM4B in U2-OSTetON cell line
-
expression of N-terminally His-tagged KDM4A in Escherichia coli
expression of N-terminally His-tagged KDM4B in Escherichia coli
expression of N-terminally His-tagged KDM4C in Escherichia coli
expression of N-terminally His-tagged KDM4E in Escherichia coli
expression of the His-tagged truncated LSD1 mutant in Escherichia coli strain Rosetta 2
-
gene HR, real-time RT-PCR enzyme expression analysis, ectopic expression of wild-type protein hairless, HR, but not JmjC-mutant HR, leads to pronounced demethylation of H3K9 in cultured human HeLa cells, reombinant expression of Flag-tagged HR in HEK-293 cells
gene JMJD1A, real-time quantitative RT-PCR enzyme expression analysis
gene JMJD2A, recombinant expression of His-tagged KDM4A residues 1-359 in Escherichia coli strain BL21 Codon-Plus-Ril from plasmid pNIC28-Bsa4
-
gene Jmjd2b, real-time quantitative PCR expression analysis
-
gene KDM1A, real-time PCR enzyme expression analysis
-
gene KDM3A, quantitative RT-PCR enzyme expression analysis, recombinant expression of wild-type KDM3A or catalytically inactive KDM3A mutant [KDM3A(H1120G/D1122N)] in MCF-10A cells
-
gene KDM4A, recombinant expression of EGFP-tagged full-length and truncated enzymes versions
-
gene KDM4A, recombinant expression of N-terminally FLAG-tagged wild-type KDM4A or KDM4A H188A variant in U2OS cells and in HeLa cells, quantitative RT-PCR enzyme expression analysis, recombinant expression of N-terminally His6-tagged truncated KDM4A1-359 in Escherichia coli BL21(DE3)
-
gene KDM4B, quantitative real-time PCR enzyme expression analysis
-
gene KDM4B, recombinant isozyme expression in U2OS-TetON stable cell line that conditionally expresses the fusion protein EGFP-KDM4B
-
gene KDM4C, recombinant isozyme expression in U2OS-TetON stable cell line that conditionally expresses the fusion protein EGFP-KDM4C, recombinant expression of EGFP-tagged full-length and truncated enzymes versions
-
gene KDM7A, quantitative RT-PCR enzyme expression analysis
gene KMD4A, recombinant expression of N-terminally His-tagged KDM4A construct (residues 1-359) in Escherichia coli, recombinant expression of N-terminally GST-tagged enzyme in Spodoptera frugiperda Sf9 cells via baculovirus transfection method
-
gene PHF8, quantitative real-time PCR enzyme expression analysis
-
gene PHF8, quantitative RT-PCR enzyme expression analysis
-
JMJD2B quantitative real-time PCR expression analysis
-
JMJD2B quantitative RT-PCR expression analysis, overview
-
LSD1 expression analysis; real-time reverse transcription-PCR expression analysis
-
LSD1 expression in Escherichia coli as GST-tagged protein
-
LSD1 overexpression in HCT cells
-
mouse Jmjd2b is transfected into JMJD2B-depleted MCF-7 cells, with stable transfection of JMJD2B-specific siRNA molecules
-
quantitative RT-PCR enzyme expression analysis
RBP2, gene expression profiling and computational analyses of gene targeting
-
real-time RT-PCR enzyme expression analysis
-
short isoform of JMJD2A expression analysis, overview
-
two LSD1 truncated forms, lacking the first 157 and 184 amino acids, respectively, expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
differentiation of neuroblastoma cells result in downregulation of LSD1; differentiation of neuroblastoma cells results in down-regulation of LSD1
-
estrogen receptor alpha is important for JMJD2B expression in hypoxia, JMJD2B can be upregulated in hypoxia in an HIF-1alpha-dependent manner
-
in attached breast epithelial cells, KDM3A expression is maintained at low levels by integrin signaling. Following detachment, integrin signaling is decreased resulting in increased KDM3A expression. Expression of either EGFR or MEK2DD decreases the levels of KDM3A in detached MCF10A cells
-
in attached breast epithelial cells, KDM3A expression is maintained at low levels by integrin signaling. Following detachment, integrin signaling is decreased resulting in increased KDM3A expression. KDM3A protein levels are increased in attached MCF-10A cells treated with the EGFR inhibitor gefitinib. Detachment and loss of integrin and growth factor receptor signaling induces KDM3A expression
-
JMJD1A gene expression is downregulated by the microRNA mir-155
JMJD1A gene expression is upregulated by beta-adrenergic agonists, and by hypoxia-inducible factor 1alpha (HIF1alpha), hypoxia, starvation and iron scavengers in tumor tissues
JMJD2B, JMJD2C, JMJD1A, and JMJD1B are induced by hypoxia. HIFalpha-dependent induction of JMJD1A
-
short isoform of JMJD2A is upregulated during muscle differentiation
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N202M
-
site-directed mutagenesis, a KDM4D demethylase-dead mutant, that binds RNA like the wild-type enzyme
D1012N
site-directed mutagenesis, reduced activity of the mutant compared to wild-type
D939R
-
the mutation increases the Kd of JMJD2A for H4K20me3 by about 200fold but does not markedly change the affinity for H3K4me3
D945R
-
the mutation increases the Kd of JMJD2A for H3K4me3 by about 200fold, but does not affect the interaction with H4K20me3
H1120G/D1122N
-
a catalytically-inactive KDM3A mutant
H188A/E190A
-
site-directed mutagenesis, inactive mutant
H18G
-
the mutation increases the Kd for H3K4me3 by fivefold compared to the wild-type enzyme
I71L
KDM4E mutant, no demethylation of H3K9me2, but the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
I87K
KDM4E mutant, no demethylation of H3K9me2, but the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
N86H
KDM4E mutant, no demethylation of H3K9me2, but the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
N940R
-
the mutation does not perturb JMJD2A binding to H4K20me3 but decreases its affinity for H3K4me3 by about 46fold
Q88K
KDM4E mutant, the mutant shows demethylation of H3K9me2, and the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
R309G
KDM4E mutant, poor demethylation of H3K9me2, but the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
R919D
-
site-directed mutagenesis, the mutant is not associated with mitotic chromatin in contrast to the wild-type enzyme
S198M
-
site-directed mutagenesis, a KDM4C demethylase dead mutant
S288A
-
demethylation of trimethyl-histone 3 L-lysine 9 and dimethyl-histone 3 L-lysine 9 with 2-fold and 12-fold greater efficiency, respectively
T968A
-
the mutation does not appreciably alter the interaction of JMJD2A with either H3K4me3 or H4K20me3
T968R
-
the mutation does not appreciably alter the interaction of JMJD2A with either H3K4me3 or H4K20me3
V1056M
site-directed mutagenesis, reduced activity of the mutant compared to wild-type
Y942A
-
the mutation has no marked effect on the Kd of JMJD2A for H3K4me3 or H4K20me3
Y942R
-
the mutation has no marked effect on the Kd of JMJD2A for H3K4me3 or H4K20me3
additional information